VPC37_MYCTU
ID VPC37_MYCTU Reviewed; 144 AA.
AC O53501; L0TA81;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 3.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Ribonuclease VapC37 {ECO:0000255|HAMAP-Rule:MF_00265};
DE Short=RNase VapC37 {ECO:0000255|HAMAP-Rule:MF_00265};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_00265};
DE AltName: Full=Toxin VapC37 {ECO:0000255|HAMAP-Rule:MF_00265};
GN Name=vapC37 {ECO:0000255|HAMAP-Rule:MF_00265}; OrderedLocusNames=Rv2103c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP EXPRESSION IN M.SMEGMATIS, AND FUNCTION AS A TOXIN.
RC STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX PubMed=20011113; DOI=10.1371/journal.pgen.1000767;
RA Ramage H.R., Connolly L.E., Cox J.S.;
RT "Comprehensive functional analysis of Mycobacterium tuberculosis toxin-
RT antitoxin systems: implications for pathogenesis, stress responses, and
RT evolution.";
RL PLoS Genet. 5:E1000767-E1000767(2009).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 27294 / TMC 102 / H37Rv;
RX PubMed=23345537; DOI=10.1074/mcp.m112.018846;
RA Albrethsen J., Agner J., Piersma S.R., Hoejrup P., Pham T.V., Weldingh K.,
RA Jimenez C.R., Andersen P., Rosenkrands I.;
RT "Proteomic profiling of Mycobacterium tuberculosis identifies nutrient-
RT starvation-responsive toxin-antitoxin systems.";
RL Mol. Cell. Proteomics 12:1180-1191(2013).
CC -!- FUNCTION: Probable toxic component of a type II toxin-antitoxin (TA)
CC system. An RNase. Upon expression in M.smegmatis inhibits colony
CC formation. The putative cognate antitoxin is VapB37.
CC {ECO:0000269|PubMed:20011113}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00265};
CC -!- SUBCELLULAR LOCATION: Secreted. Note=Following 6 weeks of nutrient
CC starvation. {ECO:0000269|PubMed:23345537}.
CC -!- SIMILARITY: Belongs to the PINc/VapC protein family.
CC {ECO:0000255|HAMAP-Rule:MF_00265}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL123456; CCP44878.1; -; Genomic_DNA.
DR PIR; D70841; D70841.
DR RefSeq; NP_216619.1; NC_000962.3.
DR RefSeq; WP_003410811.1; NZ_NVQJ01000084.1.
DR AlphaFoldDB; O53501; -.
DR SMR; O53501; -.
DR STRING; 83332.Rv2103c; -.
DR PaxDb; O53501; -.
DR DNASU; 888003; -.
DR GeneID; 888003; -.
DR KEGG; mtu:Rv2103c; -.
DR TubercuList; Rv2103c; -.
DR eggNOG; COG1848; Bacteria.
DR OMA; WVPMLAF; -.
DR PhylomeDB; O53501; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004540; F:ribonuclease activity; IEA:InterPro.
DR GO; GO:0045926; P:negative regulation of growth; IEA:UniProt.
DR HAMAP; MF_00265; VapC_Nob1; 1.
DR InterPro; IPR006226; Mtu_PIN.
DR InterPro; IPR029060; PIN-like_dom_sf.
DR InterPro; IPR002716; PIN_dom.
DR InterPro; IPR022907; VapC_family.
DR Pfam; PF01850; PIN; 1.
DR SUPFAM; SSF88723; SSF88723; 1.
DR TIGRFAMs; TIGR00028; Mtu_PIN_fam; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Magnesium; Metal-binding; Nuclease; Reference proteome;
KW Secreted; Toxin-antitoxin system.
FT CHAIN 1..144
FT /note="Ribonuclease VapC37"
FT /id="PRO_0000407892"
FT DOMAIN 3..137
FT /note="PINc"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00265"
FT BINDING 5
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00265"
FT BINDING 90
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00265"
SQ SEQUENCE 144 AA; 15662 MW; 1AD0B16C8E6FAD53 CRC64;
MKIVDANVLL YAVNTTSEHH KPSLRWLDGA LSGADRVGFA WVPLLAFVRL ATKVGLFPRP
LPREAAITQV ADWLAAPSAV LVNPTVRHAD ILARMLTYVG TGANLVNDAH LAALAVEHRA
SIVSYDSDFG RFEGVRWDQP PALL
