Rv3358 (relK)

Current annotations:
- TBCAP: (community-based annotations - see table at bottom of page)
- TBDB: toxin
- REFSEQ: hypothetical protein
- PATRIC: YoeB toxin protein
- TUBERCULIST: Toxin RelK
- NCBI: Toxin RelK
- updated information (H37Rv4):
  - gene name: relK
  - function: relE3?
  - reference: Singh (2010) PMID: 20061486
Type: Not Target
Start: 3771045
End: 3771302
Operon:

Trans-membrane region:
Role: VI - Unknowns
GO terms:
- GO:0090305 - nucleic acid phosphodiester bond hydrolysis (Uniprot)
- GO:0045892 - negative regulation of transcription, DNA-templated (Uniprot)
- GO:0016787 - hydrolase activity (Uniprot)
- GO:0006401 - RNA catabolic process (Uniprot)
- GO:0006355 - regulation of transcription, DNA-templated (Uniprot)
- GO:0006351 - transcription, DNA-templated (Uniprot)
- GO:0005515 - protein binding (Uniprot)
- GO:0004519 - endonuclease activity (Uniprot)
- GO:0004518 - nuclease activity (Uniprot)
- GO:0003677 - DNA binding (Uniprot)
Reaction(s) (based on iSM810 metabolic model):
Gene Expression Profile (Transcriptional Responses to Drugs; Boshoff et al, 2004)
Gene Modules extracted from cluster analysis of 249 transcriptomic datasets using ICA
Orthologs among selected mycobacteria
Protein structure: 3oei
Search for Homologs in PDB

Top 10 Homologs in PDB (as of Nov 2020):

PDB	aa ident	species	PDB title
3OEI	100%	Mycobacterium tuberculosis	Crystal structure of Mycobacterium tuberculosis RelJK (Rv3357-Rv3358-RelBE3)
6OXI	49%	Escherichia coli	Dimeric E.coli YoeB bound to Thermus thermophilus 70S post-cleavage (UAA)
6OXA	49%	Escherichia coli	Dimeric E.coli YoeB bound to Thermus thermophilus 70S pre-cleavage (AAU)
6OTR	49%	Escherichia coli	Dimeric E.coli YoeB bound to Thermus thermophilus 70S post-cleavage (AAU)
6NY6	49%	Escherichia coli	Structure of dimeric Escherichia coli toxin YoeB bound to the Thermus thermophilus 30S ribosome
4V8X	49%	ESCHERICHIA COLI	Structure of Thermus thermophilus ribosome
2A6S	49%	Escherichia coli	Crystal structure of YoeB under isopropanol condition
2A6R	49%	Escherichia coli	Crystal structure of YoeB under PEG condition
2A6Q	49%	Escherichia coli	Crystal structure of YefM-YoeB complex
6N90	43%	Agrobacterium tumefaciens	YoeB/ParE toxin from Agrobacterium tumefaciens

Links to additional information on relK:
- TBDB (updated)
- Phyre2 structure prediction, model: final.casp.pdb (from Mao et al, 2013)
- UniProt
- AlphaFold model
- Vulnerability = 0.946 (from Jeremy Rock's lab)
- KEGG - nucleotide and amino acid sequences of gene
- Mycobrowser
- PATRIC
- BioCyc
- Systems Biology

Amino Acid Sequence

VRSVNFDPDAWEDFLFWLAADRKTARRITRLIGEIQRDPFSGIGKPEPLQGELSGYWSRRIDDEHRLVYRAGDDEVTMLKARYHY

(Nucleotide sequence available on KEGG)

Additional Information

relE3
http://www.ncbi.nlm.nih.gov/pubmed/20061486

ESSENTIALITY

MtbTnDB - interactive tool for exploring a database of published TnSeq datasets for Mtb

TnSeqCorr - genes with correlated TnSeq profiles across >100 conditions *new*

Classification	Condition	Strain	Method	Reference	Notes
Too-Short	Sodium Oleate	H37RvMA	Gumbel	Subhalaxmi Nambi	Probability of Essentiality: -1.000000; 1 non-insertions in a row out of 4 sites
Too-Short	Lignoceric Acid	H37RvMA	Gumbel	Subhalaxmi Nambi	Probability of Essentiality: -1.000000; 0 non-insertions in a row out of 4 sites
Too-Short	Phosphatidylcholine	H37RvMA	Gumbel	Subhalaxmi Nambi	Probability of Essentiality: -1.000000; 0 non-insertions in a row out of 4 sites
Too-Short	minimal media + 0.1% glycerol	H37RvMA	Gumbel	Griffin et al. (2011)	Probability of Essentiality: -1.000000; 1 non-insertions in a row out of 4 sites
Too-Short	minimal media + 0.01% cholesterol	H37RvMA	Gumbel	Griffin et al. (2011)	Probability of Essentiality: -1.000000; 1 non-insertions in a row out of 4 sites
Non-Essential	7H10-glycerol	H37RvMA	TraSH	Sassetti et al. (2003a)
Non-Essential	C57BL/6J mice (8 weeks)	H37RvMA	TraSH	Sassetti et al. (2003b)	Hybridization Ratio: 1.82
Non-Essential	7H09/7H10 + rich media	H37RvMA	MotifHMM	DeJesus et al. (2017)	Fully saturated (14 reps).

TnSeq Data No data currently available.

No TnSeq data currently available for this Target.

RNASeq Data No data currently available.

No RNA-Seq data currently available for this Target.

Metabolomic Profiles No data currently available.

No Metabolomic data currently available for this Target.

Proteomic Data No data currently available.

No Proteomic data currently available for this Target.

Regulatory Relationships from Systems Biology

BioCyc

Gene interactions based on ChIPSeq and Transcription Factor Over-Expression (TFOE) (Systems Biology)

NOTE: Green edges represent the connected genes being classified as differentially essential as a result of the middle gene being knocked out. These interactions are inferred based on RNASeq.

Interactions based on ChIPSeq data

Binds To:
- No bindings to other targets were found.
Bound By:

Interactions based on ChIPSeq data (Minch et al. 2014)

Binds To:
- No bindings to other targets were found.
Bound By:
- Rv1033c (trcR) (Upstream of operon)
- Rv1719 (-) (Upstream of operon)
- Rv2011c (-) (Upstream of operon)

Interactions based on TFOE data (Rustad et al. 2014)

Upregulates:
- Does not upregulate other genes.
Upregulated by:
- Rv0023 (-)
Downregulates:
- Does not downregulate other genes.
Downregulated by:
- Rv0260c (-)

TBCAP

Tubculosis Community Annotation Project (

Slayden et al., 2013

Rv3358 (relK)

Property	Value	Creator	Evidence	PMID	Comment
Citation	The three RelE homologs of Mycobacterium tuberculosis have individual, drug-specific effects on bacterial antibiotic tolerance. authors,R. Singh,CE. Barry,HI. Boshoff J. Bacteriol. 2010	shahanup86	IPI	20061486	Affinity purification (Physical interaction)
Interaction	PhysicalInteraction Rv3357	shahanup86	IPI		Affinity purification (Physical interaction) authors,R. Singh,CE. Barry,HI. Boshoff The three RelE homologs of Mycobacterium tuberculosis have individual, drug-specific effects on bacterial antibiotic tolerance. J. Bacteriol. 2010
Citation	Crystal structure of Mycobacterium tuberculosis YefM antitoxin reveals that it is not an intrinsically unstructured protein. authors,P. Kumar,B. Issac,EJ. Dodson,JP. Turkenburg,SC. Mande J. Mol. Biol. 2008	vashishtrv	IPI	18793646	Affinity purification (Physical interaction)
Interaction	PhysicalInteraction Rv3357	vashishtrv	IPI		Affinity purification (Physical interaction) authors,P. Kumar,B. Issac,EJ. Dodson,JP. Turkenburg,SC. Mande Crystal structure of Mycobacterium tuberculosis YefM antitoxin reveals that it is not an intrinsically unstructured protein. J. Mol. Biol. 2008
Citation	Three Mycobacterium tuberculosis Rel toxin:antitoxin modules inhibit mycobacterial growth and are expressed in human-infected macrophages. SB. Korch, H. Contreras et al. J. Bacteriol. 2008	vashishtrv	IPI	19114484	Affinity purification (Physical interaction)
Interaction	PhysicalInteraction Rv3357	vashishtrv	IPI		Affinity purification (Physical interaction) SB. Korch, H. Contreras et al. Three Mycobacterium tuberculosis Rel toxin:antitoxin modules inhibit mycobacterial growth and are expressed in human-infected macrophages. J. Bacteriol. 2008
Citation	The three RelE homologs of Mycobacterium tuberculosis have individual, drug-specific effects on bacterial antibiotic tolerance. authors,R. Singh,CE. Barry,HI. Boshoff J. Bacteriol. 2010	vashishtrv	IPI	20061486	Affinity purification (Physical interaction)
Interaction	PhysicalInteraction Rv3357	vashishtrv	IPI		Affinity purification (Physical interaction) authors,R. Singh,CE. Barry,HI. Boshoff The three RelE homologs of Mycobacterium tuberculosis have individual, drug-specific effects on bacterial antibiotic tolerance. J. Bacteriol. 2010
Interaction	PhysicalInteraction Rv3357	vashishtrv	IPI		Affinity purification (Physical interaction) authors,P. Kumar,B. Issac,EJ. Dodson,JP. Turkenburg,SC. Mande Crystal structure of Mycobacterium tuberculosis YefM antitoxin reveals that it is not an intrinsically unstructured protein. J. Mol. Biol. 2008
Interaction	PhysicalInteraction Rv3357	vashishtrv	IPI		Affinity purification (Physical interaction) SB. Korch, H. Contreras et al. Three Mycobacterium tuberculosis Rel toxin:antitoxin modules inhibit mycobacterial growth and are expressed in human-infected macrophages. J. Bacteriol. 2008
Interaction	PhysicalInteraction Rv3357	vashishtrv	IPI		Affinity purification (Physical interaction) authors,R. Singh,CE. Barry,HI. Boshoff The three RelE homologs of Mycobacterium tuberculosis have individual, drug-specific effects on bacterial antibiotic tolerance. J. Bacteriol. 2010
Citation	Crystal structure of Mycobacterium tuberculosis YefM antitoxin reveals that it is not an intrinsically unstructured protein. authors,P. Kumar,B. Issac,EJ. Dodson,JP. Turkenburg,SC. Mande J. Mol. Biol. 2008	shahanup86	IPI	18793646	Affinity purification (Physical interaction)
Interaction	PhysicalInteraction Rv3357	shahanup86	IPI		Affinity purification (Physical interaction) authors,P. Kumar,B. Issac,EJ. Dodson,JP. Turkenburg,SC. Mande Crystal structure of Mycobacterium tuberculosis YefM antitoxin reveals that it is not an intrinsically unstructured protein. J. Mol. Biol. 2008
Citation	Three Mycobacterium tuberculosis Rel toxin:antitoxin modules inhibit mycobacterial growth and are expressed in human-infected macrophages. SB. Korch, H. Contreras et al. J. Bacteriol. 2008	shahanup86	IPI	19114484	Affinity purification (Physical interaction)
Interaction	PhysicalInteraction Rv3357	shahanup86	IPI		Affinity purification (Physical interaction) SB. Korch, H. Contreras et al. Three Mycobacterium tuberculosis Rel toxin:antitoxin modules inhibit mycobacterial growth and are expressed in human-infected macrophages. J. Bacteriol. 2008
Interaction	PhysicalInteraction Rv3357	shahanup86	IPI		Affinity purification (Physical interaction) authors,P. Kumar,B. Issac,EJ. Dodson,JP. Turkenburg,SC. Mande Crystal structure of Mycobacterium tuberculosis YefM antitoxin reveals that it is not an intrinsically unstructured protein. J. Mol. Biol. 2008
Interaction	PhysicalInteraction Rv3357	shahanup86	IPI		Affinity purification (Physical interaction) SB. Korch, H. Contreras et al. Three Mycobacterium tuberculosis Rel toxin:antitoxin modules inhibit mycobacterial growth and are expressed in human-infected macrophages. J. Bacteriol. 2008
Interaction	PhysicalInteraction Rv3357	shahanup86	IPI		Affinity purification (Physical interaction) authors,R. Singh,CE. Barry,HI. Boshoff The three RelE homologs of Mycobacterium tuberculosis have individual, drug-specific effects on bacterial antibiotic tolerance. J. Bacteriol. 2010
Citation	Comprehensive functional analysis of Mycobacterium tuberculosis toxin-antitoxin systems: implications for pathogenesis, stress responses, and evolution. authors,HR. Ramage,LE. Connolly,JS. Cox PLoS Genet. 2009	jlew		20011113	RelE homolog, Toxic when expressed in Msmeg, not rescued by antitoxin (Rv3358)
Symbol	relK	jlew			Each pair shows interaction by two-hybrid and GST pulldown. F and B each interact with E, G, K, and itself. authors,M. Yang,C. Gao,Y. Wang,H. Zhang,ZG. He Characterization of the interaction and cross-regulation of three Mycobacterium tuberculosis RelBE modules. PLoS ONE 2010
Citation	Characterization of the interaction and cross-regulation of three Mycobacterium tuberculosis RelBE modules. authors,M. Yang,C. Gao,Y. Wang,H. Zhang,ZG. He PLoS ONE 2010	jlew		20498855	Each pair shows interaction by two-hybrid and GST pulldown. F and B each interact with E, G, K, and itself.
Symbol	relE3	jlew			Each toxin individually arrests growth of both M. tuberculosis and E. coli, an effect that is neutralized by coexpression of the cognate antitoxin. authors,R. Singh,CE. Barry,HI. Boshoff The three RelE homologs of Mycobacterium tuberculosis have individual, drug-specific effects on bacterial antibiotic tolerance. J. Bacteriol. 2010
Citation	The three RelE homologs of Mycobacterium tuberculosis have individual, drug-specific effects on bacterial antibiotic tolerance. authors,R. Singh,CE. Barry,HI. Boshoff J. Bacteriol. 2010	jlew		20061486	Each toxin individually arrests growth of both M. tuberculosis and E. coli, an effect that is neutralized by coexpression of the cognate antitoxin.
Symbol	relK	jlew			Overexpression of Mtb relE, relG and relK induces growth arrest in Msmeg; reversed by expression of relB, relF and relJ SB. Korch, H. Contreras et al. Three Mycobacterium tuberculosis Rel toxin:antitoxin modules inhibit mycobacterial growth and are expressed in human-infected macrophages. J. Bacteriol. 2008
Citation	Three Mycobacterium tuberculosis Rel toxin:antitoxin modules inhibit mycobacterial growth and are expressed in human-infected macrophages. SB. Korch, H. Contreras et al. J. Bacteriol. 2008	jlew		19114484	Overexpression of Mtb relE, relG and relK induces growth arrest in Msmeg; reversed by expression of relB, relF and relJ
Symbol	RelE3	jlew			We report the heterologous toxicity of these TA loci in Escherichia coli and show that only a few of the M. tuberculosis-encoded toxins can inhibit E. coli growth and have a killing effect. This killing effect can be suppressed by coexpression of the cognate antitoxin. authors,A. Gupta Killing activity and rescue function of genome-wide toxin-antitoxin loci of Mycobacterium tuberculosis. FEMS Microbiol. Lett. 2009
Citation	Killing activity and rescue function of genome-wide toxin-antitoxin loci of Mycobacterium tuberculosis. authors,A. Gupta FEMS Microbiol. Lett. 2009	jlew		19016878	We report the heterologous toxicity of these TA loci in Escherichia coli and show that only a few of the M. tuberculosis-encoded toxins can inhibit E. coli growth and have a killing effect. This killing effect can be suppressed by coexpression of the cognate antitoxin.
Other	start:3771045	rslayden			SAV2407 from Staphylococcus aureus subsp. aureus Mu50 (88 aa), FASTA scores: opt: 250, E(): 2e-11, (40.5% identity in 84 aa overlap); etc.
Other	stop:3771302	rslayden			SAV2407 from Staphylococcus aureus subsp. aureus Mu50 (88 aa), FASTA scores: opt: 250, E(): 2e-11, (40.5% identity in 84 aa overlap); etc.
Other	strand:+	rslayden			SAV2407 from Staphylococcus aureus subsp. aureus Mu50 (88 aa), FASTA scores: opt: 250, E(): 2e-11, (40.5% identity in 84 aa overlap); etc.
Other	start:3771045	rslayden			Conserved hypohetical protein, highly similar to other hypohetical proteins e.g. Q9Z4V8
Other	stop:3771302	rslayden			Conserved hypohetical protein, highly similar to other hypohetical proteins e.g. Q9Z4V8
Other	strand:+	rslayden			Conserved hypohetical protein, highly similar to other hypohetical proteins e.g. Q9Z4V8
Other	start:3771045	rslayden			SCBAC17D6.03 from Streptomyces coelicolor (84 aa), FASTA scores: opt: 393, E(): 1.1e-21, (59.75% identity in 82 aa overlap); P56605
Other	stop:3771302	rslayden			SCBAC17D6.03 from Streptomyces coelicolor (84 aa), FASTA scores: opt: 393, E(): 1.1e-21, (59.75% identity in 82 aa overlap); P56605
Other	strand:+	rslayden			SCBAC17D6.03 from Streptomyces coelicolor (84 aa), FASTA scores: opt: 393, E(): 1.1e-21, (59.75% identity in 82 aa overlap); P56605
Other	start:3771045	rslayden			YOEB_ECOLI from Escherichia coli (84 aa), FASTA scores: opt: 305, E(): 2.2e-15, (49.35% identity in 77 aa overlap); Q9Z5W7 PUTATIVE DOC PROTEIN from Francisella novicida (68 aa), FASTA scores: opt: 253, E(): 9.6e-12, (51.6% identity in 62 aa overlap); BAB58569
Other	stop:3771302	rslayden			YOEB_ECOLI from Escherichia coli (84 aa), FASTA scores: opt: 305, E(): 2.2e-15, (49.35% identity in 77 aa overlap); Q9Z5W7 PUTATIVE DOC PROTEIN from Francisella novicida (68 aa), FASTA scores: opt: 253, E(): 9.6e-12, (51.6% identity in 62 aa overlap); BAB58569
Other	strand:+	rslayden			YOEB_ECOLI from Escherichia coli (84 aa), FASTA scores: opt: 305, E(): 2.2e-15, (49.35% identity in 77 aa overlap); Q9Z5W7 PUTATIVE DOC PROTEIN from Francisella novicida (68 aa), FASTA scores: opt: 253, E(): 9.6e-12, (51.6% identity in 62 aa overlap); BAB58569

Property

Value

Creator

Evidence

PMID

Comment

Citation

The three RelE homologs of Mycobacterium tuberculosis have individual, drug-specific effects on bacterial antibiotic tolerance. authors,R. Singh,CE. Barry,HI. Boshoff J. Bacteriol. 2010

shahanup86

IPI

20061486

Affinity purification (Physical interaction)

Interaction

PhysicalInteraction Rv3357

shahanup86

IPI

Affinity purification (Physical interaction)
authors,R. Singh,CE. Barry,HI. Boshoff The three RelE homologs of Mycobacterium tuberculosis have individual, drug-specific effects on bacterial antibiotic tolerance. J. Bacteriol. 2010

Citation

Crystal structure of Mycobacterium tuberculosis YefM antitoxin reveals that it is not an intrinsically unstructured protein. authors,P. Kumar,B. Issac,EJ. Dodson,JP. Turkenburg,SC. Mande J. Mol. Biol. 2008

vashishtrv

IPI

18793646

Affinity purification (Physical interaction)

Interaction

PhysicalInteraction Rv3357

vashishtrv

IPI

Affinity purification (Physical interaction)
authors,P. Kumar,B. Issac,EJ. Dodson,JP. Turkenburg,SC. Mande Crystal structure of Mycobacterium tuberculosis YefM antitoxin reveals that it is not an intrinsically unstructured protein. J. Mol. Biol. 2008

Citation

Three Mycobacterium tuberculosis Rel toxin:antitoxin modules inhibit mycobacterial growth and are expressed in human-infected macrophages. SB. Korch, H. Contreras et al. J. Bacteriol. 2008

vashishtrv

IPI

19114484

Affinity purification (Physical interaction)

Interaction

PhysicalInteraction Rv3357

vashishtrv

IPI

Affinity purification (Physical interaction)
SB. Korch, H. Contreras et al. Three Mycobacterium tuberculosis Rel toxin:antitoxin modules inhibit mycobacterial growth and are expressed in human-infected macrophages. J. Bacteriol. 2008

Citation

The three RelE homologs of Mycobacterium tuberculosis have individual, drug-specific effects on bacterial antibiotic tolerance. authors,R. Singh,CE. Barry,HI. Boshoff J. Bacteriol. 2010

vashishtrv

IPI

20061486

Affinity purification (Physical interaction)

Interaction

PhysicalInteraction Rv3357

vashishtrv

IPI

Interaction

PhysicalInteraction Rv3357

vashishtrv

IPI

Interaction

PhysicalInteraction Rv3357

vashishtrv

IPI

Interaction

PhysicalInteraction Rv3357

vashishtrv

IPI

Citation

shahanup86

IPI

18793646

Affinity purification (Physical interaction)

Interaction

PhysicalInteraction Rv3357

shahanup86

IPI

Citation

Three Mycobacterium tuberculosis Rel toxin:antitoxin modules inhibit mycobacterial growth and are expressed in human-infected macrophages. SB. Korch, H. Contreras et al. J. Bacteriol. 2008

shahanup86

IPI

19114484

Affinity purification (Physical interaction)

Interaction

PhysicalInteraction Rv3357

shahanup86

IPI

Interaction

PhysicalInteraction Rv3357

shahanup86

IPI

Interaction

PhysicalInteraction Rv3357

shahanup86

IPI

Interaction

PhysicalInteraction Rv3357

shahanup86

IPI

Citation

Comprehensive functional analysis of Mycobacterium tuberculosis toxin-antitoxin systems: implications for pathogenesis, stress responses, and evolution. authors,HR. Ramage,LE. Connolly,JS. Cox PLoS Genet. 2009

jlew

20011113

RelE homolog, Toxic when expressed in Msmeg, not rescued by antitoxin (Rv3358)

Symbol

relK

jlew

Each pair shows interaction by two-hybrid and GST pulldown. F and B each interact with E, G, K, and itself.
authors,M. Yang,C. Gao,Y. Wang,H. Zhang,ZG. He Characterization of the interaction and cross-regulation of three Mycobacterium tuberculosis RelBE modules. PLoS ONE 2010

Citation

Characterization of the interaction and cross-regulation of three Mycobacterium tuberculosis RelBE modules. authors,M. Yang,C. Gao,Y. Wang,H. Zhang,ZG. He PLoS ONE 2010

jlew

20498855

Each pair shows interaction by two-hybrid and GST pulldown. F and B each interact with E, G, K, and itself.

Symbol

relE3

jlew

Each toxin individually arrests growth of both M. tuberculosis and E. coli, an effect that is neutralized by coexpression of the cognate antitoxin.
authors,R. Singh,CE. Barry,HI. Boshoff The three RelE homologs of Mycobacterium tuberculosis have individual, drug-specific effects on bacterial antibiotic tolerance. J. Bacteriol. 2010

Citation

The three RelE homologs of Mycobacterium tuberculosis have individual, drug-specific effects on bacterial antibiotic tolerance. authors,R. Singh,CE. Barry,HI. Boshoff J. Bacteriol. 2010

jlew

20061486

Each toxin individually arrests growth of both M. tuberculosis and E. coli, an effect that is neutralized by coexpression of the cognate antitoxin.

Symbol

relK

jlew

Overexpression of Mtb relE, relG and relK induces growth arrest in Msmeg; reversed by expression of relB, relF and relJ
SB. Korch, H. Contreras et al. Three Mycobacterium tuberculosis Rel toxin:antitoxin modules inhibit mycobacterial growth and are expressed in human-infected macrophages. J. Bacteriol. 2008

Citation

Three Mycobacterium tuberculosis Rel toxin:antitoxin modules inhibit mycobacterial growth and are expressed in human-infected macrophages. SB. Korch, H. Contreras et al. J. Bacteriol. 2008

jlew

19114484

Overexpression of Mtb relE, relG and relK induces growth arrest in Msmeg; reversed by expression of relB, relF and relJ

Symbol

RelE3

jlew

We report the heterologous toxicity of these TA loci in Escherichia coli and show that only a few of the M. tuberculosis-encoded toxins can inhibit E. coli growth and have a killing effect. This killing effect can be suppressed by coexpression of the cognate antitoxin.
authors,A. Gupta Killing activity and rescue function of genome-wide toxin-antitoxin loci of Mycobacterium tuberculosis. FEMS Microbiol. Lett. 2009

Citation

Killing activity and rescue function of genome-wide toxin-antitoxin loci of Mycobacterium tuberculosis. authors,A. Gupta FEMS Microbiol. Lett. 2009

jlew

19016878

Other

start:3771045

rslayden

SAV2407 from Staphylococcus aureus subsp. aureus Mu50 (88 aa), FASTA scores: opt: 250, E(): 2e-11, (40.5% identity in 84 aa overlap); etc.

Other

stop:3771302

rslayden

SAV2407 from Staphylococcus aureus subsp. aureus Mu50 (88 aa), FASTA scores: opt: 250, E(): 2e-11, (40.5% identity in 84 aa overlap); etc.

Other

strand:+

rslayden

SAV2407 from Staphylococcus aureus subsp. aureus Mu50 (88 aa), FASTA scores: opt: 250, E(): 2e-11, (40.5% identity in 84 aa overlap); etc.

Other

start:3771045

rslayden

Conserved hypohetical protein, highly similar to other hypohetical proteins e.g. Q9Z4V8

Other

stop:3771302

rslayden

Conserved hypohetical protein, highly similar to other hypohetical proteins e.g. Q9Z4V8

Other

strand:+

rslayden

Conserved hypohetical protein, highly similar to other hypohetical proteins e.g. Q9Z4V8

Other

start:3771045

rslayden

SCBAC17D6.03 from Streptomyces coelicolor (84 aa), FASTA scores: opt: 393, E(): 1.1e-21, (59.75% identity in 82 aa overlap); P56605

Other

stop:3771302

rslayden

SCBAC17D6.03 from Streptomyces coelicolor (84 aa), FASTA scores: opt: 393, E(): 1.1e-21, (59.75% identity in 82 aa overlap); P56605

Other

strand:+

rslayden

SCBAC17D6.03 from Streptomyces coelicolor (84 aa), FASTA scores: opt: 393, E(): 1.1e-21, (59.75% identity in 82 aa overlap); P56605

Other

start:3771045

rslayden

YOEB_ECOLI from Escherichia coli (84 aa), FASTA scores: opt: 305, E(): 2.2e-15, (49.35% identity in 77 aa overlap); Q9Z5W7 PUTATIVE DOC PROTEIN from Francisella novicida (68 aa), FASTA scores: opt: 253, E(): 9.6e-12, (51.6% identity in 62 aa overlap); BAB58569

Other

stop:3771302

rslayden

Other

strand:+

rslayden

Comments