VPC21_MYCTU
ID VPC21_MYCTU Reviewed; 138 AA.
AC P9WF91; L0TAS8; O33299; Q7D6M9;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=Ribonuclease VapC21 {ECO:0000255|HAMAP-Rule:MF_00265};
DE Short=RNase VapC21 {ECO:0000255|HAMAP-Rule:MF_00265};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_00265};
DE AltName: Full=Toxin VapC21 {ECO:0000255|HAMAP-Rule:MF_00265};
GN Name=vapC21 {ECO:0000255|HAMAP-Rule:MF_00265}; OrderedLocusNames=Rv2757c;
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, AND FUNCTION AS A TOXIN.
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).
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 VapB21. {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 -!- SIMILARITY: Belongs to the PINc/VapC protein family.
CC {ECO:0000255|HAMAP-Rule:MF_00265}.
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DR EMBL; AL123456; CCP45556.1; -; Genomic_DNA.
DR PIR; D70880; D70880.
DR RefSeq; NP_217273.1; NC_000962.3.
DR RefSeq; WP_003414059.1; NZ_NVQJ01000020.1.
DR PDB; 5SV2; X-ray; 1.31 A; A=1-138.
DR PDBsum; 5SV2; -.
DR AlphaFoldDB; P9WF91; -.
DR SMR; P9WF91; -.
DR STRING; 83332.Rv2757c; -.
DR PaxDb; P9WF91; -.
DR DNASU; 888249; -.
DR GeneID; 888249; -.
DR KEGG; mtu:Rv2757c; -.
DR TubercuList; Rv2757c; -.
DR eggNOG; COG1487; Bacteria.
DR OMA; LHYDGDF; -.
DR PhylomeDB; P9WF91; -.
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:0045926; P:negative regulation of growth; IMP: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..138
FT /note="Ribonuclease VapC21"
FT /id="PRO_0000407880"
FT DOMAIN 6..128
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 97
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00265"
FT STRAND 5..7
FT /evidence="ECO:0007829|PDB:5SV2"
FT HELIX 9..12
FT /evidence="ECO:0007829|PDB:5SV2"
FT TURN 13..16
FT /evidence="ECO:0007829|PDB:5SV2"
FT HELIX 18..29
FT /evidence="ECO:0007829|PDB:5SV2"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:5SV2"
FT HELIX 37..44
FT /evidence="ECO:0007829|PDB:5SV2"
FT HELIX 50..63
FT /evidence="ECO:0007829|PDB:5SV2"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:5SV2"
FT HELIX 73..85
FT /evidence="ECO:0007829|PDB:5SV2"
FT TURN 86..88
FT /evidence="ECO:0007829|PDB:5SV2"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:5SV2"
FT HELIX 95..107
FT /evidence="ECO:0007829|PDB:5SV2"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:5SV2"
FT HELIX 117..125
FT /evidence="ECO:0007829|PDB:5SV2"
FT STRAND 129..133
FT /evidence="ECO:0007829|PDB:5SV2"
SQ SEQUENCE 138 AA; 15773 MW; CCCCA89F9B308FFE CRC64;
MTTRYLLDKS AAYRAHLPAV RHRLEPLMER GLLARCGITD LEFGVSARSR EDHRTLGTYR
RDALEYVNTP DTVWVRAWEI QEALTDKGFH RSVKIPDLII AAVAEHHGIP VMHYDQDFER
IAAITRQPVE WVVAPGTA
