VPB15_MYCTU
ID VPB15_MYCTU Reviewed; 80 AA.
AC P9WLM7; L0T9X2; Q10848;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 32.
DE RecName: Full=Antitoxin VapB15 {ECO:0000303|PubMed:20011113};
GN Name=vapB15; OrderedLocusNames=Rv2009; ORFNames=MTCY39.08c;
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 AN ANTITOXIN, AND INDUCTION BY
RP HYPOXIA.
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 X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH VAPC15; MAGNESIUM AND
RP MANGANESE, FUNCTION, COFACTOR, AND SUBUNIT.
RC STRAIN=H37Rv;
RX PubMed=25450593; DOI=10.1016/j.jsb.2014.10.002;
RA Das U., Pogenberg V., Subhramanyam U.K., Wilmanns M., Gourinath S.,
RA Srinivasan A.;
RT "Crystal structure of the VapBC-15 complex from Mycobacterium tuberculosis
RT reveals a two-metal ion dependent PIN-domain ribonuclease and a variable
RT mode of toxin-antitoxin assembly.";
RL J. Struct. Biol. 188:249-258(2014).
CC -!- FUNCTION: Antitoxin component of a type II toxin-antitoxin (TA) system.
CC Upon expression in M.smegmatis neutralizes the effect of cognate toxin
CC VapC15 (PubMed:20011113). Partially inhibits the RNase activity of
CC VapC15 (PubMed:25450593). {ECO:0000269|PubMed:20011113,
CC ECO:0000269|PubMed:25450593, ECO:0000305|PubMed:15718296}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:25450593};
CC Note=The heterotrimer binds 1 Mg(2+)-Mn(2+) pair while the
CC heterotetramer binds 2 pairs. Both metals are shared by the toxin-
CC antitoxin pair. {ECO:0000269|PubMed:25450593};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:25450593};
CC Note=The heterotrimer binds 1 Mg(2+)-Mn(2+) pair while the
CC heterotetramer binds 2 pairs. Both metals are shared by the toxin-
CC antitoxin pair. {ECO:0000269|PubMed:25450593};
CC -!- SUBUNIT: Crystallizes as a VapB15-VapC15(2) heterotrimer and as a
CC VapB15(2)-VapC15(2) heterotetramer; each toxin pair forms a homodimer
CC which creates a channel in which the antitoxin binds.
CC {ECO:0000269|PubMed:25450593}.
CC -!- INDUCTION: Induced by hypoxia. {ECO:0000269|PubMed:20011113}.
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DR EMBL; AL123456; CCP44781.1; -; Genomic_DNA.
DR PIR; G70759; G70759.
DR RefSeq; NP_216525.1; NC_000962.3.
DR RefSeq; WP_003899127.1; NC_000962.3.
DR PDB; 4CHG; X-ray; 2.10 A; G/H/I/J=1-80.
DR PDBsum; 4CHG; -.
DR AlphaFoldDB; P9WLM7; -.
DR SMR; P9WLM7; -.
DR STRING; 83332.Rv2009; -.
DR PaxDb; P9WLM7; -.
DR DNASU; 888925; -.
DR GeneID; 888925; -.
DR KEGG; mtu:Rv2009; -.
DR TubercuList; Rv2009; -.
DR eggNOG; COG5450; Bacteria.
DR OMA; MTAREMH; -.
DR PhylomeDB; P9WLM7; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045927; P:positive regulation of growth; IMP:MTBBASE.
DR GO; GO:0001666; P:response to hypoxia; IEP:MTBBASE.
DR InterPro; IPR019239; VapB_antitoxin.
DR Pfam; PF09957; VapB_antitoxin; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Magnesium; Manganese; Metal-binding; Reference proteome;
KW Toxin-antitoxin system.
FT CHAIN 1..80
FT /note="Antitoxin VapB15"
FT /id="PRO_0000103938"
FT REGION 60..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 67
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="ligand shared with toxin"
FT /evidence="ECO:0000269|PubMed:25450593"
FT BINDING 67
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="ligand shared with toxin"
FT /evidence="ECO:0000269|PubMed:25450593"
FT HELIX 48..52
FT /evidence="ECO:0007829|PDB:4CHG"
FT TURN 53..56
FT /evidence="ECO:0007829|PDB:4CHG"
FT HELIX 63..67
FT /evidence="ECO:0007829|PDB:4CHG"
SQ SEQUENCE 80 AA; 8884 MW; 524F4A764E722AEB CRC64;
MYSGVVSRTN IEIDDELVAA AQRMYRLDSK RSAVDLALRR LVGEPLGRDE ALALQGSGFD
FSNDEIESFS DTDRKLADES
