VPC30_MYCTU
ID VPC30_MYCTU Reviewed; 131 AA.
AC P9WF77; L0T4A1; P67240; P96914;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Ribonuclease VapC30 {ECO:0000255|HAMAP-Rule:MF_00265};
DE Short=RNase VapC30 {ECO:0000255|HAMAP-Rule:MF_00265};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_00265};
DE AltName: Full=Toxin VapC30 {ECO:0000255|HAMAP-Rule:MF_00265};
GN Name=vapC30 {ECO:0000255|HAMAP-Rule:MF_00265}; OrderedLocusNames=Rv0624;
GN ORFNames=MTCY20H10.05;
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).
CC -!- FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system. An
CC RNase (By similarity). Upon expression in M.smegmatis inhibits colony
CC formation. Its toxic effect is neutralized by coexpression with cognate
CC antitoxin VapB30. {ECO:0000255|HAMAP-Rule:MF_00265,
CC ECO:0000269|PubMed:20011113}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00265};
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; CCP43365.1; -; Genomic_DNA.
DR PIR; E70611; E70611.
DR RefSeq; NP_215138.1; NC_000962.3.
DR RefSeq; WP_003403236.1; NZ_NVQJ01000033.1.
DR PDB; 4XGQ; X-ray; 2.70 A; A/C/E/G=1-131.
DR PDB; 4XGR; X-ray; 2.70 A; A/C/E/G=1-131.
DR PDBsum; 4XGQ; -.
DR PDBsum; 4XGR; -.
DR AlphaFoldDB; P9WF77; -.
DR SMR; P9WF77; -.
DR STRING; 83332.Rv0624; -.
DR PaxDb; P9WF77; -.
DR DNASU; 887951; -.
DR GeneID; 887951; -.
DR KEGG; mtu:Rv0624; -.
DR TubercuList; Rv0624; -.
DR eggNOG; COG3742; Bacteria.
DR OMA; AFNEPEA; -.
DR PhylomeDB; P9WF77; -.
DR Proteomes; UP000001584; Chromosome.
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; IMP:MTBBASE.
DR HAMAP; MF_00265; VapC_Nob1; 1.
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.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Magnesium; Metal-binding; Nuclease;
KW Reference proteome; Toxin-antitoxin system.
FT CHAIN 1..131
FT /note="Ribonuclease VapC30"
FT /id="PRO_0000221199"
FT DOMAIN 1..129
FT /note="PINc"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00265"
FT BINDING 4
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00265"
FT BINDING 99
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00265"
FT STRAND 1..3
FT /evidence="ECO:0007829|PDB:4XGQ"
FT HELIX 5..13
FT /evidence="ECO:0007829|PDB:4XGQ"
FT HELIX 18..27
FT /evidence="ECO:0007829|PDB:4XGQ"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:4XGQ"
FT HELIX 35..48
FT /evidence="ECO:0007829|PDB:4XGQ"
FT HELIX 50..63
FT /evidence="ECO:0007829|PDB:4XGQ"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:4XGQ"
FT HELIX 73..86
FT /evidence="ECO:0007829|PDB:4XGQ"
FT HELIX 99..109
FT /evidence="ECO:0007829|PDB:4XGQ"
FT STRAND 121..125
FT /evidence="ECO:0007829|PDB:4XGQ"
SQ SEQUENCE 131 AA; 14250 MW; 777FCE0A5BB640E3 CRC64;
MVIDTSALVA MLSDEPDAER FEAAVEADHI RLMSTASYLE TALVIEARFG EPGGRELDLW
LHRAAVDLVA VHADQADAAR AAYRTYGKGR HRAGLNYGDC FSYGLAKISG QPLLFKGEDF
QHTDIATVAL P
