VPC12_MYCTU
ID VPC12_MYCTU Reviewed; 129 AA.
AC P9WFA3; L0T7H4; P71978; Q7D832;
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 VapC12 {ECO:0000255|HAMAP-Rule:MF_00265};
DE Short=RNase VapC12 {ECO:0000255|HAMAP-Rule:MF_00265};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_00265};
DE AltName: Full=Toxin VapC12 {ECO:0000255|HAMAP-Rule:MF_00265};
GN Name=vapC12 {ECO:0000255|HAMAP-Rule:MF_00265}; OrderedLocusNames=Rv1720c;
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 VapB12 (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; CCP44486.1; -; Genomic_DNA.
DR PIR; C70686; C70686.
DR RefSeq; NP_216236.1; NC_000962.3.
DR RefSeq; WP_003408465.1; NZ_NVQJ01000010.1.
DR AlphaFoldDB; P9WFA3; -.
DR SMR; P9WFA3; -.
DR STRING; 83332.Rv1720c; -.
DR PaxDb; P9WFA3; -.
DR DNASU; 885180; -.
DR GeneID; 885180; -.
DR KEGG; mtu:Rv1720c; -.
DR TubercuList; Rv1720c; -.
DR eggNOG; COG4113; Bacteria.
DR OMA; RCSHRPL; -.
DR PhylomeDB; P9WFA3; -.
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 CDD; cd09873; PIN_Pae0151-like; 1.
DR HAMAP; MF_00265; VapC_Nob1; 1.
DR InterPro; IPR029060; PIN-like_dom_sf.
DR InterPro; IPR002716; PIN_dom.
DR InterPro; IPR044153; PIN_Pae0151-like.
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..129
FT /note="Ribonuclease VapC12"
FT /id="PRO_0000407873"
FT BINDING 5
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00265"
FT BINDING 94
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00265"
SQ SEQUENCE 129 AA; 13850 MW; D119173F733B06CD CRC64;
MIVLDASAAV ELMLTTPAGA AVARRLRGET VHAPAHFDVE VIGAIRQAVV RQLISDHEGL
VVVVNFLSLP VRRWPLKPFT QRAYQLRSTH TVADGAYVAL AEGLGVPLIT CDGRLAQSHG
HNAEIELVA