VPC27_MYCTO
ID VPC27_MYCTO Reviewed; 137 AA.
AC P9WF82; L0T753; O07780; Q7D9K3;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Ribonuclease VapC27 {ECO:0000255|HAMAP-Rule:MF_00265};
DE Short=RNase VapC27 {ECO:0000255|HAMAP-Rule:MF_00265};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_00265};
DE AltName: Full=Toxin VapC27 {ECO:0000255|HAMAP-Rule:MF_00265};
GN Name=vapC27 {ECO:0000255|HAMAP-Rule:MF_00265}; Synonyms=vapC-mt24;
GN OrderedLocusNames=MT0628;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
CC -!- FUNCTION: Probably the toxic component of a type II toxin-antitoxin
CC (TA) system. An RNase. Its cognate antitoxin is VapB27 (By similarity).
CC {ECO:0000250}.
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 -!- CAUTION: Bioinformatics programs predicts this could have a signal
CC sequence. {ECO:0000305}.
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; AE000516; AAK44852.1; -; Genomic_DNA.
DR PIR; A70909; A70909.
DR RefSeq; WP_003403137.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WF82; -.
DR SMR; P9WF82; -.
DR EnsemblBacteria; AAK44852; AAK44852; MT0628.
DR GeneID; 45424566; -.
DR KEGG; mtc:MT0628; -.
DR PATRIC; fig|83331.31.peg.661; -.
DR HOGENOM; CLU_150004_0_0_11; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004540; F:ribonuclease activity; IEA:InterPro.
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 3: Inferred from homology;
KW Hydrolase; Magnesium; Metal-binding; Nuclease; Toxin-antitoxin system.
FT CHAIN 1..137
FT /note="Ribonuclease VapC27"
FT /id="PRO_0000428584"
FT DOMAIN 7..125
FT /note="PINc"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00265"
FT BINDING 8
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00265"
FT BINDING 101
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00265"
SQ SEQUENCE 137 AA; 14818 MW; 12975B4555CA4402 CRC64;
MKPPLAVDTS VAIPLLVRTH TAHAAVVAWW AHREAALCGH ALAETYSVLT RLPRDLRLAP
MDAARLLTER FAAPLLLSSR TTEHLPRVLA QFEITGGAVY DALVALAAAE HRAELATRDA
RAKDTYEKIG VHVVVAA