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VPC23_MYCTU
ID   VPC23_MYCTU             Reviewed;         126 AA.
AC   P9WF89; L0TAV5; O33345; Q7D6F8;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 34.
DE   RecName: Full=Ribonuclease VapC23 {ECO:0000255|HAMAP-Rule:MF_00265};
DE            Short=RNase VapC23 {ECO:0000255|HAMAP-Rule:MF_00265};
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_00265};
DE   AltName: Full=Toxin VapC23 {ECO:0000255|HAMAP-Rule:MF_00265};
GN   Name=vapC23 {ECO:0000255|HAMAP-Rule:MF_00265}; OrderedLocusNames=Rv2863;
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   POSSIBLE FUNCTION.
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=15718296; DOI=10.1093/nar/gki201;
RA   Pandey D.P., Gerdes K.;
RT   "Toxin-antitoxin loci are highly abundant in free-living but lost from
RT   host-associated prokaryotes.";
RL   Nucleic Acids Res. 33:966-976(2005).
CC   -!- FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system. An
CC       RNase. The cognate antitoxin is VapB23 (By similarity).
CC       {ECO:0000255|HAMAP-Rule:MF_00265}.
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; CCP45665.1; -; Genomic_DNA.
DR   PIR; A70886; A70886.
DR   RefSeq; NP_217379.1; NC_000962.3.
DR   RefSeq; WP_003414592.1; NZ_NVQJ01000006.1.
DR   AlphaFoldDB; P9WF89; -.
DR   SMR; P9WF89; -.
DR   STRING; 83332.Rv2863; -.
DR   PaxDb; P9WF89; -.
DR   DNASU; 888195; -.
DR   GeneID; 888195; -.
DR   KEGG; mtu:Rv2863; -.
DR   TubercuList; Rv2863; -.
DR   eggNOG; COG1848; Bacteria.
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   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; Reference proteome;
KW   Toxin-antitoxin system.
FT   CHAIN           1..126
FT                   /note="Ribonuclease VapC23"
FT                   /id="PRO_0000407882"
FT   DOMAIN          2..118
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         98
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00265"
SQ   SEQUENCE   126 AA;  14237 MW;  63D0DFF851BF7778 CRC64;
     MIFVDTNVFM YAVGRDHPLR MPAREFLEHS LEHQDRLVTS AEAMQELLNA YVPVGRNSTL
     DSALTLVRAL TEIWPVEAAD VAHARTLHHR HPGLGARDLL HLACCQRRGV TRIKTFDHTL
     ASAFRS
 
 
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