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VAPC2_MYCTO
ID   VAPC2_MYCTO             Reviewed;         141 AA.
AC   P9WFB8; L0T386; O07228; Q7DA25;
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 VapC2 {ECO:0000255|HAMAP-Rule:MF_00265};
DE            Short=RNase VapC2 {ECO:0000255|HAMAP-Rule:MF_00265};
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_00265};
DE   AltName: Full=Toxin VapC2 {ECO:0000255|HAMAP-Rule:MF_00265};
GN   Name=vapC2 {ECO:0000255|HAMAP-Rule:MF_00265}; OrderedLocusNames=MT0314;
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: Toxic component of a type II toxin-antitoxin (TA) system.
CC       Acts as an RNase. All its toxic effects are neutralized by coexpression
CC       with cognate antitoxin VapB2 (By similarity). {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) ion per monomer. {ECO:0000250};
CC   -!- SUBUNIT: Probably active as a homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PINc/VapC protein family.
CC       {ECO:0000255|HAMAP-Rule:MF_00265}.
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DR   EMBL; AE000516; AAK44537.1; -; Genomic_DNA.
DR   PIR; F70523; F70523.
DR   RefSeq; WP_003401566.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WFB8; -.
DR   SMR; P9WFB8; -.
DR   EnsemblBacteria; AAK44537; AAK44537; MT0314.
DR   KEGG; mtc:MT0314; -.
DR   PATRIC; fig|83331.31.peg.337; -.
DR   HOGENOM; CLU_118482_4_1_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..141
FT                   /note="Ribonuclease VapC2"
FT                   /id="PRO_0000428566"
FT   DOMAIN          7..129
FT                   /note="PINc"
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   BINDING         117
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00265"
FT   BINDING         119
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00265"
SQ   SEQUENCE   141 AA;  15746 MW;  F371180C7C34F448 CRC64;
     MTDQRWLIDK SALVRLTDSP DMEIWSNRIE RGLVHITGVT RLEVGFSAEC GEIARREFRE
     PPLSAMPVEY LTPRIEDRAL EVQTLLADRG HHRGPSIPDL LIAATAELSG LTVLHVDKDF
     DAIAALTGQK TERLTHRPPS A
 
 
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