Rv0295c (-)

Current annotations:
- TBCAP: (community-based annotations - see table at bottom of page)
- TBDB: hypothetical protein
- REFSEQ: hypothetical protein
- PATRIC: Sulfotransferase
- TUBERCULIST: Conserved protein
- NCBI: hypothetical protein
- updated information (H37Rv4):
  - gene name: stf0
  - function: sulfotransferase
  - reference: Mougous (2002) PMID: 12144918
Type: Not Target
Start: 358945
End: 359748
Operon:

Trans-membrane region:
Role: VI - Unknowns
GO terms:
- GO:0050656 - 3'-phosphoadenosine 5'-phosphosulfate binding (Uniprot)
- GO:0050427 - 3'-phosphoadenosine 5'-phosphosulfate metabolic process (Uniprot)
- GO:0046506 - sulfolipid biosynthetic process (Uniprot)
- GO:0042803 - protein homodimerization activity (Uniprot)
- GO:0016740 - transferase activity (Uniprot)
- GO:0008146 - sulfotransferase activity (Uniprot)
- GO:0005991 - trehalose metabolic process (Uniprot)
- GO:0005975 - carbohydrate metabolic process (Uniprot)
- GO:0005886 - plasma membrane (Uniprot)
- GO:0005618 - cell wall (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:
Search for Homologs in PDB
Top 10 Homologs in PDB (as of Nov 2020):

PDB aa ident species PDB title

1TEX 72% Mycobacterium smegmatis Mycobacterium smegmatis Stf0 Sulfotransferase with Trehalose
Links to additional information on Rv0295c:
- TBDB (updated)
- Phyre2 structure prediction, model: final.casp.pdb (from Mao et al, 2013)
- UniProt
- AlphaFold model
- Vulnerability = 1.315 (from Jeremy Rock's lab)
- KEGG - nucleotide and amino acid sequences of gene
- Mycobrowser
- PATRIC
- BioCyc
- Systems Biology

PDB	aa ident	species	PDB title
1TEX	72%	Mycobacterium smegmatis	Mycobacterium smegmatis Stf0 Sulfotransferase with Trehalose

Amino Acid Sequence

MSRAVRPYLVLATQRSGSTLLVESLRATGCAGEPQEFFQYLPSTGMAPQPREWFAGVDDDTILQLLDPLDPGTPDTATPVAWREHVRTSGRTPNGVWGGK
LMWNQTALLQQRAAQLPDRSGDGLRAAIRDVIGNEPVFVHVHRPDVVSQAVSFWRAVQTQVWRGHPDPKRDSQAVYHAGAIAHIIRNLRDQENGWRAWFA
EEGIDPIDIAYPVLWRNLTAIVASVLDAIGQDPKLAPAPMLERQANQRSDEWVDRYRAEAPRLGLPT

(Nucleotide sequence available on KEGG)

Additional Information

sft0

Mougous...Bertozzi (2004) NSMB
http://www.nature.com/nsmb/journal/v11/n8/full/nsmb802.html

Sulfotransferases and Sulfatases in Mycobacteria
http://www.sciencedirect.com/science/article/pii/S1074552102001758

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
Non-Essential	Sodium Oleate	H37RvMA	Gumbel	Subhalaxmi Nambi	Probability of Essentiality: 0.000000; 2 non-insertions in a row out of 10 sites
Non-Essential	Lignoceric Acid	H37RvMA	Gumbel	Subhalaxmi Nambi	Probability of Essentiality: 0.000000; 2 non-insertions in a row out of 10 sites
Non-Essential	Phosphatidylcholine	H37RvMA	Gumbel	Subhalaxmi Nambi	Probability of Essentiality: 0.000000; 2 non-insertions in a row out of 10 sites
Non-Essential	minimal media + 0.1% glycerol	H37RvMA	Gumbel	Griffin et al. (2011)	Probability of Essentiality: 0.000000; 2 non-insertions in a row out of 9 sites
Non-Essential	minimal media + 0.01% cholesterol	H37RvMA	Gumbel	Griffin et al. (2011)	Probability of Essentiality: 0.005500; 5 non-insertions in a row out of 9 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: 4.13
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

RNA processing and modification

Energy production and conversion

Chromatin structure and dynamics

Amino acid transport and metabolism

Cell cycle control, cell division, chromosome partitioning

Carbohydrate transport and metabolism

Nucleotide transport and metabolism

Lipid transport and metabolism

Coenzyme transport and metabolism

Transcription

Translation, ribosomal structure and biogenesis

Cell wall/membrane/envelope biogenesis

Replication, recombination and repair

Posttranslational modification, protein turnover, chaperones

Cell motility

Secondary metabolites biosynthesis, transport and catabolism

Inorganic ion transport and metabolism

Function unknown

General function prediction only

Intracellular trafficking, secretion, and vesicular transport

Signal transduction mechanisms

Extracellular structures

Defense mechanisms

Nuclear structure

Cytoskeleton

BioCyc Co-regulated genes based on gene expression profiling (Systems Biology, Inferelator Network)

Differentially expressed as result of RNASeq in glycerol environment (Only top 20 genes shown sorted by log fold change with p_adj 0.05).

Conditionally essential as result of TNSeq (Only top 20 genes shown sorted by log fold change with p_adj 0.05).

BioCyc Transcription factor binding based on ChIP-Seq (Systems Biology)

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

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

Binds To:
- No bindings to other targets were found.
Bound By:
- Rv0967 (csoR) (Direct binding)

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

Upregulates:
- Does not upregulate other genes.
Upregulated by:
- Not upregulated by other genes.
Downregulates:
- Does not downregulate other genes.
Downregulated by:
- Not downregulated by other genes.

TBCAP

Tubculosis Community Annotation Project (

Slayden et al., 2013

Rv0295c (-)

Property	Value	Creator	Evidence	PMID	Comment
Term	EC:2.8.2.2 Alcohol sulfotransferase. - IDA	njamshidi	IDA	15258569	PMID: 15258569 show biochemically that paps is the sulfate donor. see also PMID: 11882713 CA. Rivera-Marrero, JD. Ritzenthaler et al. Molecular cloning and expression of a novel glycolipid sulfotransferase in Mycobacterium tuberculosis. Microbiology (Reading, Engl.) 2002
Term	TBRXN:TRESULT trehalose sulfotransferase - IDA	njamshidi	IDA	15258569	PMID: 15258569 show biochemically that paps is the sulfate donor. see also PMID: 11882713 CA. Rivera-Marrero, JD. Ritzenthaler et al. Molecular cloning and expression of a novel glycolipid sulfotransferase in Mycobacterium tuberculosis. Microbiology (Reading, Engl.) 2002
Citation	Identification, function and structure of the mycobacterial sulfotransferase that initiates sulfolipid-1 biosynthesis. authors,JD. Mougous,CJ. Petzold,RH. Senaratne,DH. Lee,DL. Akey,FL. Lin,SE. Munchel,MR. Pratt,LW. Riley,JA. Leary,JM. Berger,CR. Bertozzi Nat. Struct. Mol. Biol. 2004	njamshidi	ISS	15258569	PMID: 15258569 show biochemically that paps is the sulfate donor. see also PMID: 11882713
Term	EC:2.8.2.2 Alcohol sulfotransferase. - ISS	njamshidi	ISS	15258569	PMID: 15258569 show biochemically that paps is the sulfate donor. see also PMID: 11882713 authors,JD. Mougous,CJ. Petzold,RH. Senaratne,DH. Lee,DL. Akey,FL. Lin,SE. Munchel,MR. Pratt,LW. Riley,JA. Leary,JM. Berger,CR. Bertozzi Identification, function and structure of the mycobacterial sulfotransferase that initiates sulfolipid-1 biosynthesis. Nat. Struct. Mol. Biol. 2004
Term	TBRXN:TRESULT trehalose sulfotransferase - ISS	njamshidi	ISS	15258569	PMID: 15258569 show biochemically that paps is the sulfate donor. see also PMID: 11882713 authors,JD. Mougous,CJ. Petzold,RH. Senaratne,DH. Lee,DL. Akey,FL. Lin,SE. Munchel,MR. Pratt,LW. Riley,JA. Leary,JM. Berger,CR. Bertozzi Identification, function and structure of the mycobacterial sulfotransferase that initiates sulfolipid-1 biosynthesis. Nat. Struct. Mol. Biol. 2004
Citation	Molecular cloning and expression of a novel glycolipid sulfotransferase in Mycobacterium tuberculosis. CA. Rivera-Marrero, JD. Ritzenthaler et al. Microbiology (Reading, Engl.) 2002	njamshidi	ISS	11882713\|15258569	PMID: 15258569 show biochemically that paps is the sulfate donor. see also PMID: 11882713
Term	EC:2.8.2.2 Alcohol sulfotransferase. - ISS	njamshidi	ISS	15258569	PMID: 15258569 show biochemically that paps is the sulfate donor. see also PMID: 11882713 CA. Rivera-Marrero, JD. Ritzenthaler et al. Molecular cloning and expression of a novel glycolipid sulfotransferase in Mycobacterium tuberculosis. Microbiology (Reading, Engl.) 2002
Term	TBRXN:TRESULT trehalose sulfotransferase - ISS	njamshidi	ISS	15258569	PMID: 15258569 show biochemically that paps is the sulfate donor. see also PMID: 11882713 CA. Rivera-Marrero, JD. Ritzenthaler et al. Molecular cloning and expression of a novel glycolipid sulfotransferase in Mycobacterium tuberculosis. Microbiology (Reading, Engl.) 2002
Citation	Identification, function and structure of the mycobacterial sulfotransferase that initiates sulfolipid-1 biosynthesis. authors,JD. Mougous,CJ. Petzold,RH. Senaratne,DH. Lee,DL. Akey,FL. Lin,SE. Munchel,MR. Pratt,LW. Riley,JA. Leary,JM. Berger,CR. Bertozzi Nat. Struct. Mol. Biol. 2004	njamshidi	IDA	15258569	PMID: 15258569 show biochemically that paps is the sulfate donor. see also PMID: 11882713
Term	EC:2.8.2.2 Alcohol sulfotransferase. - IDA	njamshidi	IDA	15258569	PMID: 15258569 show biochemically that paps is the sulfate donor. see also PMID: 11882713 authors,JD. Mougous,CJ. Petzold,RH. Senaratne,DH. Lee,DL. Akey,FL. Lin,SE. Munchel,MR. Pratt,LW. Riley,JA. Leary,JM. Berger,CR. Bertozzi Identification, function and structure of the mycobacterial sulfotransferase that initiates sulfolipid-1 biosynthesis. Nat. Struct. Mol. Biol. 2004
Term	TBRXN:TRESULT trehalose sulfotransferase - IDA	njamshidi	IDA	15258569	PMID: 15258569 show biochemically that paps is the sulfate donor. see also PMID: 11882713 authors,JD. Mougous,CJ. Petzold,RH. Senaratne,DH. Lee,DL. Akey,FL. Lin,SE. Munchel,MR. Pratt,LW. Riley,JA. Leary,JM. Berger,CR. Bertozzi Identification, function and structure of the mycobacterial sulfotransferase that initiates sulfolipid-1 biosynthesis. Nat. Struct. Mol. Biol. 2004
Citation	Molecular cloning and expression of a novel glycolipid sulfotransferase in Mycobacterium tuberculosis. CA. Rivera-Marrero, JD. Ritzenthaler et al. Microbiology (Reading, Engl.) 2002	njamshidi	IDA	11882713\|15258569	PMID: 15258569 show biochemically that paps is the sulfate donor. see also PMID: 11882713
Symbol	sft0	mjackson	IDA		Polymethyl-branched acyltrehaloses
Name	Sulfotransferase responsible for the formation of the trehalose-2-sulfate moiety of sulfolipid-I	mjackson	IDA		Polymethyl-branched acyltrehaloses
Symbol	sft0	mjackson	IMP		Polymethyl-branched acyltrehaloses
Name	Sulfotransferase responsible for the formation of the trehalose-2-sulfate moiety of sulfolipid-I	mjackson	IMP		Polymethyl-branched acyltrehaloses
Symbol	sft0	mjackson			Sulfotransferase responsible for the formation of the trehalose-2-sulfate moiety of sulfolipid-I (phenotypic [mycobacterial recombinant strains]; enzymatic) authors,JD. Mougous,CJ. Petzold,RH. Senaratne,DH. Lee,DL. Akey,FL. Lin,SE. Munchel,MR. Pratt,LW. Riley,JA. Leary,JM. Berger,CR. Bertozzi Identification, function and structure of the mycobacterial sulfotransferase that initiates sulfolipid-1 biosynthesis. Nat. Struct. Mol. Biol. 2004
Citation	Identification, function and structure of the mycobacterial sulfotransferase that initiates sulfolipid-1 biosynthesis. authors,JD. Mougous,CJ. Petzold,RH. Senaratne,DH. Lee,DL. Akey,FL. Lin,SE. Munchel,MR. Pratt,LW. Riley,JA. Leary,JM. Berger,CR. Bertozzi Nat. Struct. Mol. Biol. 2004	mjackson		15258569	Sulfotransferase responsible for the formation of the trehalose-2-sulfate moiety of sulfolipid-I (phenotypic [mycobacterial recombinant strains]; enzymatic)
Other	TBPWY:Polymethyl-branched acyltrehaloses	mjackson			Sulfotransferase responsible for the formation of the trehalose-2-sulfate moiety of sulfolipid-I (phenotypic [mycobacterial recombinant strains]; enzymatic) authors,JD. Mougous,CJ. Petzold,RH. Senaratne,DH. Lee,DL. Akey,FL. Lin,SE. Munchel,MR. Pratt,LW. Riley,JA. Leary,JM. Berger,CR. Bertozzi Identification, function and structure of the mycobacterial sulfotransferase that initiates sulfolipid-1 biosynthesis. Nat. Struct. Mol. Biol. 2004

Property

Value

Creator

Evidence

PMID

Comment

Term

EC:2.8.2.2 Alcohol sulfotransferase. - IDA

njamshidi

IDA

15258569

PMID: 15258569 show biochemically that paps is the sulfate donor. see also PMID: 11882713
CA. Rivera-Marrero, JD. Ritzenthaler et al. Molecular cloning and expression of a novel glycolipid sulfotransferase in Mycobacterium tuberculosis. Microbiology (Reading, Engl.) 2002

Term

TBRXN:TRESULT trehalose sulfotransferase - IDA

njamshidi

IDA

15258569

Citation

Identification, function and structure of the mycobacterial sulfotransferase that initiates sulfolipid-1 biosynthesis. authors,JD. Mougous,CJ. Petzold,RH. Senaratne,DH. Lee,DL. Akey,FL. Lin,SE. Munchel,MR. Pratt,LW. Riley,JA. Leary,JM. Berger,CR. Bertozzi Nat. Struct. Mol. Biol. 2004

njamshidi

ISS

15258569

PMID: 15258569 show biochemically that paps is the sulfate donor. see also PMID: 11882713

Term

EC:2.8.2.2 Alcohol sulfotransferase. - ISS

njamshidi

ISS

15258569

PMID: 15258569 show biochemically that paps is the sulfate donor. see also PMID: 11882713
authors,JD. Mougous,CJ. Petzold,RH. Senaratne,DH. Lee,DL. Akey,FL. Lin,SE. Munchel,MR. Pratt,LW. Riley,JA. Leary,JM. Berger,CR. Bertozzi Identification, function and structure of the mycobacterial sulfotransferase that initiates sulfolipid-1 biosynthesis. Nat. Struct. Mol. Biol. 2004

Term

TBRXN:TRESULT trehalose sulfotransferase - ISS

njamshidi

ISS

15258569

Citation

Molecular cloning and expression of a novel glycolipid sulfotransferase in Mycobacterium tuberculosis. CA. Rivera-Marrero, JD. Ritzenthaler et al. Microbiology (Reading, Engl.) 2002

njamshidi

ISS

11882713|15258569

PMID: 15258569 show biochemically that paps is the sulfate donor. see also PMID: 11882713

Term

EC:2.8.2.2 Alcohol sulfotransferase. - ISS

njamshidi

ISS

15258569

Term

TBRXN:TRESULT trehalose sulfotransferase - ISS

njamshidi

ISS

15258569

Citation

njamshidi

IDA

15258569

PMID: 15258569 show biochemically that paps is the sulfate donor. see also PMID: 11882713

Term

EC:2.8.2.2 Alcohol sulfotransferase. - IDA

njamshidi

IDA

15258569

Term

TBRXN:TRESULT trehalose sulfotransferase - IDA

njamshidi

IDA

15258569

Citation

Molecular cloning and expression of a novel glycolipid sulfotransferase in Mycobacterium tuberculosis. CA. Rivera-Marrero, JD. Ritzenthaler et al. Microbiology (Reading, Engl.) 2002

njamshidi

IDA

11882713|15258569

PMID: 15258569 show biochemically that paps is the sulfate donor. see also PMID: 11882713

Symbol

sft0

mjackson

IDA

Polymethyl-branched acyltrehaloses

Name

Sulfotransferase responsible for the formation of the trehalose-2-sulfate moiety of sulfolipid-I

mjackson

IDA

Polymethyl-branched acyltrehaloses

Symbol

sft0

mjackson

IMP

Polymethyl-branched acyltrehaloses

Name

Sulfotransferase responsible for the formation of the trehalose-2-sulfate moiety of sulfolipid-I

mjackson

IMP

Polymethyl-branched acyltrehaloses

Symbol

sft0

mjackson

Sulfotransferase responsible for the formation of the trehalose-2-sulfate moiety of sulfolipid-I (phenotypic [mycobacterial recombinant strains]; enzymatic)
authors,JD. Mougous,CJ. Petzold,RH. Senaratne,DH. Lee,DL. Akey,FL. Lin,SE. Munchel,MR. Pratt,LW. Riley,JA. Leary,JM. Berger,CR. Bertozzi Identification, function and structure of the mycobacterial sulfotransferase that initiates sulfolipid-1 biosynthesis. Nat. Struct. Mol. Biol. 2004

Citation

mjackson

15258569

Sulfotransferase responsible for the formation of the trehalose-2-sulfate moiety of sulfolipid-I (phenotypic [mycobacterial recombinant strains]; enzymatic)

Other

TBPWY:Polymethyl-branched acyltrehaloses

mjackson

Comments