VPC25_MYCTU
ID VPC25_MYCTU Reviewed; 142 AA.
AC P9WF85; L0T672; O53683; Q7DA40;
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 VapC25 {ECO:0000255|HAMAP-Rule:MF_00265};
DE Short=RNase VapC25 {ECO:0000255|HAMAP-Rule:MF_00265};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_00265};
DE AltName: Full=Toxin VapC25 {ECO:0000255|HAMAP-Rule:MF_00265};
GN Name=vapC25 {ECO:0000255|HAMAP-Rule:MF_00265}; OrderedLocusNames=Rv0277c;
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).
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 VapB25. {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}.
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DR EMBL; AL123456; CCP43006.1; -; Genomic_DNA.
DR PIR; C70835; C70835.
DR RefSeq; NP_214791.1; NC_000962.3.
DR RefSeq; WP_003401406.1; NZ_NVQJ01000055.1.
DR AlphaFoldDB; P9WF85; -.
DR SMR; P9WF85; -.
DR STRING; 83332.Rv0277c; -.
DR PaxDb; P9WF85; -.
DR DNASU; 886625; -.
DR GeneID; 886625; -.
DR KEGG; mtu:Rv0277c; -.
DR TubercuList; Rv0277c; -.
DR eggNOG; COG1848; Bacteria.
DR PhylomeDB; P9WF85; -.
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; 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 Toxin-antitoxin system.
FT CHAIN 1..142
FT /note="Ribonuclease VapC25"
FT /id="PRO_0000407884"
FT DOMAIN 3..139
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 108
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00265"
SQ SEQUENCE 142 AA; 15887 MW; 0A941F32472DE135 CRC64;
MFLIDVNVLL AAHRGDHPNH RTVRPWFDRL LAADDPFTVP NLVWASFLRL TTNRRIFEIP
SPRADAFAFV EAVNAQPHHL PTSPGPRHLV LLRKLCDEAD ASGDLIPDAV LGAIAVEHHC
AVVSLDRDFA RFASVRHIRP PI