ID   VPC15_MYCTO             Reviewed;         132 AA.
AC   P9WF96; L0T8D0; P64925; Q10847;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 37.
DE   RecName: Full=Ribonuclease VapC15 {ECO:0000255|HAMAP-Rule:MF_00265};
DE            Short=RNase VapC15 {ECO:0000255|HAMAP-Rule:MF_00265};
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_00265};
DE   AltName: Full=Toxin VapC15 {ECO:0000255|HAMAP-Rule:MF_00265};
GN   Name=vapC15 {ECO:0000255|HAMAP-Rule:MF_00265}; OrderedLocusNames=MT2065;
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. An
CC       RNase. Its toxic effect is neutralized by cognate antitoxin VapB15 (By
CC       similarity). {ECO:0000250|UniProtKB:P9WF97, ECO:0000255|HAMAP-
CC       Rule:MF_00265}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P9WF97,
CC         ECO:0000255|HAMAP-Rule:MF_00265};
CC       Note=The heterotrimer binds 1 Mg(2+)-Mn(2+) pair while the
CC       heterotetramer binds 2 pairs. Both metals are shared by the toxin-
CC       antitoxin pair. {ECO:0000250|UniProtKB:P9WF97};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:P9WF97};
CC       Note=The heterotrimer binds 1 Mg(2+)-Mn(2+) pair while the
CC       heterotetramer binds 2 pairs. Both metals are shared by the toxin-
CC       antitoxin pair. {ECO:0000250|UniProtKB:P9WF97};
CC   -!- SUBUNIT: Forms a VapB15-VapC15(2) heterotrimer and a VapB15(2)-
CC       VapC15(2) heterotetramer; each toxin pair forms a homodimer which
CC       creates a channel in which the antitoxin binds.
CC       {ECO:0000250|UniProtKB:P9WF97}.
CC   -!- SIMILARITY: Belongs to the PINc/VapC protein family.
CC       {ECO:0000255|HAMAP-Rule:MF_00265}.
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DR   EMBL; AE000516; AAK46343.1; -; Genomic_DNA.
DR   PIR; H70759; H70759.
DR   RefSeq; WP_003410075.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WF96; -.
DR   SMR; P9WF96; -.
DR   EnsemblBacteria; AAK46343; AAK46343; MT2065.
DR   KEGG; mtc:MT2065; -.
DR   PATRIC; fig|83331.31.peg.2224; -.
DR   HOGENOM; CLU_118482_1_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; Manganese; Metal-binding; Nuclease;
KW   Toxin-antitoxin system.
FT   CHAIN           1..132
FT                   /note="Ribonuclease VapC15"
FT                   /id="PRO_0000428577"
FT   DOMAIN          1..121
FT                   /note="PINc"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00265"
FT   BINDING         96
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="ligand shared with antitoxin"
FT                   /evidence="ECO:0000250|UniProtKB:P9WF97, ECO:0000255|HAMAP-
FT                   Rule:MF_00265"
FT   BINDING         96
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_note="ligand shared with antitoxin"
FT                   /evidence="ECO:0000250|UniProtKB:P9WF97"
FT   BINDING         114
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_note="ligand shared with antitoxin"
FT                   /evidence="ECO:0000250|UniProtKB:P9WF97"
FT   BINDING         116
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_note="ligand shared with antitoxin"
FT                   /evidence="ECO:0000250|UniProtKB:P9WF97"
SQ   SEQUENCE   132 AA;  14731 MW;  CEBE78B1A25BDEFC CRC64;
     MIVDTSVWIA YLSTSESLAS RWLADRIAAD STVIVPEVVM MELLIGKTDE DTAALRRRLL
     QRFAIEPLAP VRDAEDAAAI HRRCRRGGDT VRSLIDCQVA AMALRIGVAV AHRDRDYEAI
     RTHCGLRTEP LF