VPC11_MYCTU
ID VPC11_MYCTU Reviewed; 134 AA.
AC P9WFA5; L0T8M0; P64879; Q10770;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Ribonuclease VapC11 {ECO:0000255|HAMAP-Rule:MF_00265};
DE Short=RNase VapC11 {ECO:0000255|HAMAP-Rule:MF_00265};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_00265};
DE AltName: Full=Toxin VapC11 {ECO:0000255|HAMAP-Rule:MF_00265};
GN Name=vapC11 {ECO:0000255|HAMAP-Rule:MF_00265}; OrderedLocusNames=Rv1561;
GN ORFNames=MTCY48.04c;
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 E.COLI, AND FUNCTION AS A TOXIN.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=19016878; DOI=10.1111/j.1574-6968.2008.01400.x;
RA Gupta A.;
RT "Killing activity and rescue function of genome-wide toxin-antitoxin loci
RT of Mycobacterium tuberculosis.";
RL FEMS Microbiol. Lett. 290:45-53(2009).
RN [4]
RP EXPRESSION IN M.SMEGMATIS, FUNCTION AS A TOXIN, FUNCTION AS AN RNASE, AND
RP INDUCTION DURING 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 [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.
CC Acts as an RNase. Upon expression in E.coli and M.smegmatis inhibits
CC translation, cell growth and colony formation. Its toxic effects on
CC cell growth and colony formation are neutralized by coexpression with
CC cognate antitoxin VapB11; the effect on translation has not been tested
CC but is probably also neutralized. {ECO:0000269|PubMed:19016878,
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 {ECO:0000269|PubMed:20011113}.
CC -!- SIMILARITY: Belongs to the PINc/VapC protein family.
CC {ECO:0000255|HAMAP-Rule:MF_00265}.
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DR EMBL; AL123456; CCP44325.1; -; Genomic_DNA.
DR PIR; F70763; F70763.
DR RefSeq; NP_216077.1; NC_000962.3.
DR RefSeq; WP_003407786.1; NZ_NVQJ01000004.1.
DR PDB; 6A7V; X-ray; 1.67 A; A/C/E/G=2-134.
DR PDBsum; 6A7V; -.
DR AlphaFoldDB; P9WFA5; -.
DR SMR; P9WFA5; -.
DR STRING; 83332.Rv1561; -.
DR PaxDb; P9WFA5; -.
DR DNASU; 886361; -.
DR GeneID; 886361; -.
DR KEGG; mtu:Rv1561; -.
DR TubercuList; Rv1561; -.
DR eggNOG; COG1487; Bacteria.
DR OMA; SSVWIDF; -.
DR PhylomeDB; P9WFA5; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004540; F:ribonuclease activity; IDA:MTBBASE.
DR GO; GO:0044003; P:modulation by symbiont of host process; IMP:MTBBASE.
DR GO; GO:0017148; P:negative regulation of translation; IMP:MTBBASE.
DR GO; GO:0075136; P:response to host; IEP:MTBBASE.
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 3D-structure; Hydrolase; Magnesium; Metal-binding; Nuclease;
KW Reference proteome; Toxin-antitoxin system.
FT CHAIN 1..134
FT /note="Ribonuclease VapC11"
FT /id="PRO_0000103883"
FT DOMAIN 2..126
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"
FT STRAND 2..4
FT /evidence="ECO:0007829|PDB:6A7V"
FT HELIX 6..13
FT /evidence="ECO:0007829|PDB:6A7V"
FT HELIX 19..30
FT /evidence="ECO:0007829|PDB:6A7V"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:6A7V"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:6A7V"
FT HELIX 39..47
FT /evidence="ECO:0007829|PDB:6A7V"
FT HELIX 52..64
FT /evidence="ECO:0007829|PDB:6A7V"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:6A7V"
FT HELIX 75..88
FT /evidence="ECO:0007829|PDB:6A7V"
FT HELIX 96..108
FT /evidence="ECO:0007829|PDB:6A7V"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:6A7V"
FT HELIX 117..125
FT /evidence="ECO:0007829|PDB:6A7V"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:6A7V"
SQ SEQUENCE 134 AA; 14651 MW; 7D22BA3A94DE0FEB CRC64;
MILIDTSAWV EYFRATGSIA AVEVRRLLSE EAARIAMCEP IAMEILSGAL DDNTHTTLER
LVNGLPSLNV DDAIDFRAAA GIYRAARRAG ETVRSINDCL IAALAIRHGA RIVHRDADFD
VIARITNLQA ASFR
