VPC20_MYCTU
ID VPC20_MYCTU Reviewed; 131 AA.
AC P95004; L0T9Y5;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=23S rRNA-specific endonuclease VapC20 {ECO:0000305|PubMed:24225902};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_00265};
DE AltName: Full=Ribonuclease VapC20 {ECO:0000255|HAMAP-Rule:MF_00265};
DE Short=RNase VapC20 {ECO:0000255|HAMAP-Rule:MF_00265};
DE AltName: Full=Toxin VapC20 {ECO:0000255|HAMAP-Rule:MF_00265};
GN Name=vapC20 {ECO:0000255|HAMAP-Rule:MF_00265}; OrderedLocusNames=Rv2549c;
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 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 FUNCTION, ACTIVITY REGULATION, EXPRESSION IN E.COLI AND M.SMEGMATIS, AND
RP MUTAGENESIS OF ASP-5.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=24225902; DOI=10.1038/ncomms3796;
RA Winther K.S., Brodersen D.E., Brown A.K., Gerdes K.;
RT "VapC20 of Mycobacterium tuberculosis cleaves the sarcin-ricin loop of 23S
RT rRNA.";
RL Nat. Commun. 4:2796-2796(2013).
CC -!- FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system
CC (PubMed:19016878, PubMed:24225902). An endoribonuclease that cleaves
CC both E.coli and M.smegmatis 23S rRNA between G2661 and A2662 in the
CC sarcin-ricin loop (SRL, E.coli 23S rRNA numbering). The SRL sequence is
CC highly conserved and is implicated in GTP hydrolysis by EF-Tu and EF-G.
CC Acts on purified ribosomes but not on isolated RNA in E.coli, nor on a
CC shortened artificial substrate (PubMed:24225902). Upon expression in
CC E.coli inhibits cell growth, colony formation and translation. Its
CC toxic effect is neutralized by coexpression, or subsequent expression
CC (tested over 2 hours) with cognate antitoxin VapB20 (PubMed:19016878,
CC PubMed:24225902). {ECO:0000255|HAMAP-Rule:MF_00265,
CC ECO:0000269|PubMed:19016878, ECO:0000269|PubMed:24225902}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00265};
CC -!- ACTIVITY REGULATION: Inhibited by EDTA. {ECO:0000269|PubMed:24225902}.
CC -!- SIMILARITY: Belongs to the PINc/VapC protein family.
CC {ECO:0000255|HAMAP-Rule:MF_00265}.
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DR EMBL; AL123456; CCP45345.1; -; Genomic_DNA.
DR PIR; A70660; A70660.
DR RefSeq; NP_217065.1; NC_000962.3.
DR RefSeq; WP_003413180.1; NZ_NVQJ01000032.1.
DR AlphaFoldDB; P95004; -.
DR SMR; P95004; -.
DR STRING; 83332.Rv2549c; -.
DR PaxDb; P95004; -.
DR DNASU; 887193; -.
DR GeneID; 887193; -.
DR KEGG; mtu:Rv2549c; -.
DR TubercuList; Rv2549c; -.
DR eggNOG; COG2402; Bacteria.
DR InParanoid; P95004; -.
DR OMA; CIANDIH; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0004521; F:endoribonuclease activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0044003; P:modulation by symbiont of host process; IMP:MTBBASE.
DR GO; GO:0016075; P:rRNA catabolic process; IDA:UniProtKB.
DR CDD; cd18680; PIN_MtVapC20-like; 1.
DR HAMAP; MF_00265; VapC_Nob1; 1.
DR InterPro; IPR029060; PIN-like_dom_sf.
DR InterPro; IPR002716; PIN_dom.
DR InterPro; IPR039018; VapC20.
DR InterPro; IPR022907; VapC_family.
DR PANTHER; PTHR42188; PTHR42188; 1.
DR Pfam; PF01850; PIN; 1.
DR SUPFAM; SSF88723; SSF88723; 1.
PE 1: Evidence at protein level;
KW Endonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease;
KW Reference proteome; Toxin-antitoxin system.
FT CHAIN 1..131
FT /note="23S rRNA-specific endonuclease VapC20"
FT /id="PRO_0000407879"
FT DOMAIN 2..130
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 MUTAGEN 5
FT /note="D->A: Loss of 23S rRNA cleavage."
FT /evidence="ECO:0000269|PubMed:24225902"
SQ SEQUENCE 131 AA; 14620 MW; 1AF9B15EF70E96A7 CRC64;
MIFVDTSFWA ALGNAGDARH GTAKRLWASK PPVVMTSNHV LGETWTLLNR RCGHRAAVAA
AAIRLSTVVR VEHVTADLEE QAWEWLVRHD EREYSFVDAT SFAVMRKKGI QNAYAFDGDF
SAAGFVEVRP E
