Rv2181 (-)

Current annotations:
- TBCAP: (community-based annotations - see table at bottom of page)
- TBDB: alpha-12-mannosyltransferase
- REFSEQ: integral membrane protein
- PATRIC: Possible membrane protein
- TUBERCULIST: Alpha(1->2)mannosyltransferase
- NCBI: Alpha(1->2)mannosyltransferase
- updated information (H37Rv4):
  - gene name: mptC
  - function:
  - reference: Mishra (2011) Rv2181
Type: Not Target
Start: 2443302
End: 2444585
Operon:

Trans-membrane region:
Role: II.C.5 - Other membrane proteins
GO terms:
- GO:0097502 - mannosylation (Uniprot)
- GO:0046488 - phosphatidylinositol metabolic process (Uniprot)
- GO:0016758 - transferase activity, transferring hexosyl groups (Uniprot)
- GO:0016757 - transferase activity, transferring glycosyl groups (Uniprot)
- GO:0016740 - transferase activity (Uniprot)
- GO:0016021 - integral component of membrane (Uniprot)
- GO:0016020 - membrane (Uniprot)
- GO:0009405 - pathogenesis (Uniprot)
- GO:0009247 - glycolipid biosynthetic process (Uniprot)
- GO:0008654 - phospholipid biosynthetic process (Uniprot)
- GO:0006629 - lipid metabolic process (Uniprot)
- GO:0005886 - plasma membrane (Uniprot)
- GO:0000026 - alpha-1,2-mannosyltransferase activity (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): (none with >35% aa id)
Links to additional information on Rv2181:
- TBDB (updated)
- Phyre2 structure prediction, model: final.casp.pdb (from Mao et al, 2013)
- UniProt
- AlphaFold model
- Vulnerability = 1.032 (from Jeremy Rock's lab)
- KEGG - nucleotide and amino acid sequences of gene
- Mycobrowser
- PATRIC
- BioCyc
- Systems Biology

Amino Acid Sequence

MSAWRAPEVGSRLGRRVLWCLLWLLAGVALGYVAWRLFGHTPYRIDIDIYQMGARAWLDGRPLYGGGVLFHTPIGLNLPFTYPPLAAVLFSPFAWLQMPA
ASVAITVLTLVLLIASTAIVLTGLDAWPTSRLVPAPARLRRLWLAVLIVAPATIWLEPISSNFAFGQINVVLMTLVIVDCFPRRTPWPRGLMLGLGIALK
LTPAVFLLYFLLRRDGRAALTALASFAVATLLGFVLAWRDSWEYWTHTLHHTDRIGAAALNTDQNIAGALARLTIGDDERFALWVAGSLLVLAATIWAMR
RVLRAGEPTLAVICVALFGLVVSPVSWSHHWVWMLPAVLVIGLLGWRRRNVALAMLSLAGVVLMRWTPIDLLPQHRETTAVWWRQLAGMSYVWWALAVIV
VAGLTVTARMTPQRSLTRGLTPAPTAS

(Nucleotide sequence available on KEGG)

Additional Information

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 20 sites
Non-Essential	Lignoceric Acid	H37RvMA	Gumbel	Subhalaxmi Nambi	Probability of Essentiality: 0.000000; 2 non-insertions in a row out of 20 sites
Non-Essential	Phosphatidylcholine	H37RvMA	Gumbel	Subhalaxmi Nambi	Probability of Essentiality: 0.000000; 2 non-insertions in a row out of 20 sites
Non-Essential	minimal media + 0.1% glycerol	H37RvMA	Gumbel	Griffin et al. (2011)	Probability of Essentiality: 0.000000; 3 non-insertions in a row out of 20 sites
Non-Essential	minimal media + 0.01% cholesterol	H37RvMA	Gumbel	Griffin et al. (2011)	Probability of Essentiality: 0.000000; 2 non-insertions in a row out of 20 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: 0.61
Growth-Advantage	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:
- Rv1990c (-) (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.

Property	Value	Creator	Evidence	PMID	Comment
Symbol	mptC	mjackson	IMP		PIM, LM and LAM biosynthesis
Name	Polyprenol phosphomannose-dependent alpha-1,2-mannosyltransferase involved in LM branching and ManLAM capping	mjackson	IMP		PIM, LM and LAM biosynthesis
Symbol	mptC	mjackson	IDA		PIM, LM and LAM biosynthesis
Name	Polyprenol phosphomannose-dependent alpha-1,2-mannosyltransferase involved in LM branching and ManLAM capping	mjackson	IDA		PIM, LM and LAM biosynthesis
Symbol	mptC	mjackson			Polyprenol phosphomannose-dependent alpha-1,2-mannosyltransferase involved in LM branching and ManLAM capping (phenotypic [mycobacterial recombinant strains]; enzymatic) authors,AK. Mishra,K. Krumbach,D. Rittmann,B. Appelmelk,V. Pathak,AK. Pathak,J. Nigou,J. Geurtsen,L. Eggeling,GS. Besra Lipoarabinomannan biosynthesis in Corynebacterineae: the interplay of two (12)-mannopyranosyltransferases MptC and MptD in mannan branching. Mol. Microbiol. 2011
Citation	Lipoarabinomannan biosynthesis in Corynebacterineae: the interplay of two (12)-mannopyranosyltransferases MptC and MptD in mannan branching. authors,AK. Mishra,K. Krumbach,D. Rittmann,B. Appelmelk,V. Pathak,AK. Pathak,J. Nigou,J. Geurtsen,L. Eggeling,GS. Besra Mol. Microbiol. 2011	mjackson		21435038	Polyprenol phosphomannose-dependent alpha-1,2-mannosyltransferase involved in LM branching and ManLAM capping (phenotypic [mycobacterial recombinant strains]; enzymatic)
Other	TBPWY:PIM, LM and LAM biosynthesis	mjackson			Polyprenol phosphomannose-dependent alpha-1,2-mannosyltransferase involved in LM branching and ManLAM capping (phenotypic [mycobacterial recombinant strains]; enzymatic) authors,AK. Mishra,K. Krumbach,D. Rittmann,B. Appelmelk,V. Pathak,AK. Pathak,J. Nigou,J. Geurtsen,L. Eggeling,GS. Besra Lipoarabinomannan biosynthesis in Corynebacterineae: the interplay of two (12)-mannopyranosyltransferases MptC and MptD in mannan branching. Mol. Microbiol. 2011
Symbol	mptC	mjackson			Polyprenol phosphomannose-dependent alpha-1,2-mannosyltransferase involved in LM branching and ManLAM capping (phenotypic [mycobacterial recombinant strains]; enzymatic) D. Kaur, S. Berg et al. Biosynthesis of mycobacterial lipoarabinomannan: role of a branching mannosyltransferase. Proc. Natl. Acad. Sci. U.S.A. 2006
Citation	Biosynthesis of mycobacterial lipoarabinomannan: role of a branching mannosyltransferase. D. Kaur, S. Berg et al. Proc. Natl. Acad. Sci. U.S.A. 2006	mjackson		16945913	Polyprenol phosphomannose-dependent alpha-1,2-mannosyltransferase involved in LM branching and ManLAM capping (phenotypic [mycobacterial recombinant strains]; enzymatic)
Other	TBPWY:PIM, LM and LAM biosynthesis	mjackson			Polyprenol phosphomannose-dependent alpha-1,2-mannosyltransferase involved in LM branching and ManLAM capping (phenotypic [mycobacterial recombinant strains]; enzymatic) D. Kaur, S. Berg et al. Biosynthesis of mycobacterial lipoarabinomannan: role of a branching mannosyltransferase. Proc. Natl. Acad. Sci. U.S.A. 2006
Symbol	mptC	mjackson			Polyprenol phosphomannose-dependent alpha-1,2-mannosyltransferase involved in LM branching and ManLAM capping (phenotypic [mycobacterial recombinant strains]; enzymatic) D. Kaur, A. Obregn-Henao et al. Lipoarabinomannan of Mycobacterium: mannose capping by a multifunctional terminal mannosyltransferase. Proc. Natl. Acad. Sci. U.S.A. 2008
Citation	Lipoarabinomannan of Mycobacterium: mannose capping by a multifunctional terminal mannosyltransferase. D. Kaur, A. Obregn-Henao et al. Proc. Natl. Acad. Sci. U.S.A. 2008	mjackson		19004785	Polyprenol phosphomannose-dependent alpha-1,2-mannosyltransferase involved in LM branching and ManLAM capping (phenotypic [mycobacterial recombinant strains]; enzymatic)
Other	TBPWY:PIM, LM and LAM biosynthesis	mjackson			Polyprenol phosphomannose-dependent alpha-1,2-mannosyltransferase involved in LM branching and ManLAM capping (phenotypic [mycobacterial recombinant strains]; enzymatic) D. Kaur, A. Obregn-Henao et al. Lipoarabinomannan of Mycobacterium: mannose capping by a multifunctional terminal mannosyltransferase. Proc. Natl. Acad. Sci. U.S.A. 2008

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