VPC27_MYCTU
ID VPC27_MYCTU Reviewed; 137 AA.
AC P9WF83; L0T753; O07780; Q7D9K3;
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 VapC27 {ECO:0000255|HAMAP-Rule:MF_00265};
DE Short=RNase VapC27 {ECO:0000255|HAMAP-Rule:MF_00265};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_00265};
DE AltName: Full=Toxin VapC27 {ECO:0000255|HAMAP-Rule:MF_00265};
GN Name=vapC27 {ECO:0000255|HAMAP-Rule:MF_00265}; Synonyms=vapC-mt24;
GN OrderedLocusNames=Rv0598c;
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 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 [3]
RP INTERACTION WITH ANTITOXIN VAPB27.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=20876537; DOI=10.1074/jbc.m110.163105;
RA Zhu L., Sharp J.D., Kobayashi H., Woychik N.A., Inouye M.;
RT "Noncognate Mycobacterium tuberculosis toxin-antitoxins can physically and
RT functionally interact.";
RL J. Biol. Chem. 285:39732-39738(2010).
RN [4]
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).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 27294 / TMC 102 / H37Rv;
RX PubMed=23345537; DOI=10.1074/mcp.m112.018846;
RA Albrethsen J., Agner J., Piersma S.R., Hoejrup P., Pham T.V., Weldingh K.,
RA Jimenez C.R., Andersen P., Rosenkrands I.;
RT "Proteomic profiling of Mycobacterium tuberculosis identifies nutrient-
RT starvation-responsive toxin-antitoxin systems.";
RL Mol. Cell. Proteomics 12:1180-1191(2013).
CC -!- FUNCTION: Probably the toxic component of a type II toxin-antitoxin
CC (TA) system. An RNase (By similarity). Its cognate antitoxin is VapB27.
CC {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00265};
CC -!- SUBUNIT: Interacts with cognate antitoxin VapB27.
CC {ECO:0000269|PubMed:20876537}.
CC -!- SUBCELLULAR LOCATION: Secreted. Note=Following 6 weeks of nutrient
CC starvation. {ECO:0000269|PubMed:23345537}.
CC -!- SIMILARITY: Belongs to the PINc/VapC protein family.
CC {ECO:0000255|HAMAP-Rule:MF_00265}.
CC -!- CAUTION: Bioinformatics programs predicts this could have a signal
CC sequence. {ECO:0000305}.
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DR EMBL; AL123456; CCP43337.1; -; Genomic_DNA.
DR PIR; A70909; A70909.
DR RefSeq; NP_215112.1; NC_000962.3.
DR RefSeq; WP_003403137.1; NZ_NVQJ01000033.1.
DR AlphaFoldDB; P9WF83; -.
DR SMR; P9WF83; -.
DR STRING; 83332.Rv0598c; -.
DR PaxDb; P9WF83; -.
DR DNASU; 887861; -.
DR GeneID; 45424566; -.
DR GeneID; 887861; -.
DR KEGG; mtu:Rv0598c; -.
DR TubercuList; Rv0598c; -.
DR eggNOG; COG1848; Bacteria.
DR OMA; HENHEIC; -.
DR PhylomeDB; P9WF83; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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 1: Evidence at protein level;
KW Hydrolase; Magnesium; Metal-binding; Nuclease; Reference proteome;
KW Secreted; Toxin-antitoxin system.
FT CHAIN 1..137
FT /note="Ribonuclease VapC27"
FT /id="PRO_0000407886"
FT DOMAIN 7..125
FT /note="PINc"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00265"
FT BINDING 8
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00265"
FT BINDING 101
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00265"
SQ SEQUENCE 137 AA; 14818 MW; 12975B4555CA4402 CRC64;
MKPPLAVDTS VAIPLLVRTH TAHAAVVAWW AHREAALCGH ALAETYSVLT RLPRDLRLAP
MDAARLLTER FAAPLLLSSR TTEHLPRVLA QFEITGGAVY DALVALAAAE HRAELATRDA
RAKDTYEKIG VHVVVAA
