VAPC3_MYCTU
ID VAPC3_MYCTU Reviewed; 137 AA.
AC P9WFB7; L0T708; O06415; Q7D9N6;
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 VapC3 {ECO:0000255|HAMAP-Rule:MF_00265};
DE Short=RNase VapC3 {ECO:0000255|HAMAP-Rule:MF_00265};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_00265};
DE AltName: Full=Toxin VapC3 {ECO:0000255|HAMAP-Rule:MF_00265};
GN Name=vapC3 {ECO:0000255|HAMAP-Rule:MF_00265}; OrderedLocusNames=Rv0549c;
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).
RN [3]
RP EXPRESSION IN M.SMEGMATIS, FUNCTION AS A TOXIN, AND INDUCTION DURING
RP MACROPHAGE INFECTION.
RC STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX PubMed=20011113; DOI=10.1371/journal.pgen.1000767;
RA Ramage H.R., Connolly L.E., Cox J.S.;
RT "Comprehensive functional analysis of Mycobacterium tuberculosis toxin-
RT antitoxin systems: implications for pathogenesis, stress responses, and
RT evolution.";
RL PLoS Genet. 5:E1000767-E1000767(2009).
RN [4]
RP INDUCTION IN PERSISTER CELLS.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21673191; DOI=10.1128/mbio.00100-11;
RA Keren I., Minami S., Rubin E., Lewis K.;
RT "Characterization and transcriptome analysis of Mycobacterium tuberculosis
RT persisters.";
RL MBio 2:E00100-E00111(2011).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system. An
CC RNase (By similarity). Upon expression in M.smegmatis inhibits colony
CC formation. Its toxic effect is neutralized by coexpression with cognate
CC antitoxin VapB3. {ECO:0000255|HAMAP-Rule:MF_00265,
CC ECO:0000269|PubMed:20011113}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00265};
CC -!- INDUCTION: Induced during infection of mouse macrophages
CC (PubMed:20011113). Induced in persister cells in response to D-
CC cycloserine (PubMed:21673191). {ECO:0000269|PubMed:20011113,
CC ECO:0000269|PubMed:21673191}.
CC -!- SIMILARITY: Belongs to the PINc/VapC protein family.
CC {ECO:0000255|HAMAP-Rule:MF_00265}.
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DR EMBL; AL123456; CCP43287.1; -; Genomic_DNA.
DR PIR; H70547; H70547.
DR RefSeq; NP_215063.1; NC_000962.3.
DR RefSeq; WP_003898500.1; NZ_NVQJ01000036.1.
DR AlphaFoldDB; P9WFB7; -.
DR SMR; P9WFB7; -.
DR STRING; 83332.Rv0549c; -.
DR PaxDb; P9WFB7; -.
DR DNASU; 887534; -.
DR GeneID; 45424513; -.
DR GeneID; 887534; -.
DR KEGG; mtu:Rv0549c; -.
DR TubercuList; Rv0549c; -.
DR eggNOG; COG4113; Bacteria.
DR OMA; LANDVME; -.
DR PhylomeDB; P9WFB7; -.
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 GO; GO:0045927; P:positive regulation of growth; IMP:MTBBASE.
DR GO; GO:0075136; P:response to host; IEP:MTBBASE.
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 1: Evidence at protein level;
KW Hydrolase; Magnesium; Metal-binding; Nuclease; Reference proteome;
KW Toxin-antitoxin system.
FT CHAIN 1..137
FT /note="Ribonuclease VapC3"
FT /id="PRO_0000407866"
FT DOMAIN 12..129
FT /note="PINc"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00265"
FT BINDING 15
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00265"
FT BINDING 105
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00265"
SQ SEQUENCE 137 AA; 14700 MW; 16A91120CA498A7E CRC64;
MRASPTSPPE QVVVDASAMV DLLARTSDRC SAVRARLART AMHAPAHFDA EVLSALGRMQ
RAGALTVAYV DAALEELRQV PVTRHGLSSL LAGAWSRRDT LRLTDALYVE LAETAGLVLL
TTDERLARAW PSAHAIG
