ID   VBHA_BARSR              Reviewed;          62 AA.
AC   E6Z0R4;
DT   16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT   08-MAR-2011, sequence version 1.
DT   03-AUG-2022, entry version 24.
DE   RecName: Full=Antitoxin VbhA;
GN   ORFNames=B11C_100027;
OS   Bartonella schoenbuchensis (strain DSM 13525 / NCTC 13165 / R1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=687861;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13525 / NCTC 13165 / R1;
RX   PubMed=21347280; DOI=10.1371/journal.pgen.1001296;
RA   Engel P., Salzburger W., Liesch M., Chang C.C., Maruyama S., Lanz C.,
RA   Calteau A., Lajus A., Medigue C., Schuster S.C., Dehio C.;
RT   "Parallel evolution of a type IV secretion system in radiating lineages of
RT   the host-restricted bacterial pathogen Bartonella.";
RL   PLoS Genet. 7:E1001296-E1001296(2011).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 2-61 IN COMPLEX WITH VBHT,
RP   FUNCTION, INTERACTION WITH VBHT, AND MUTAGENESIS OF GLU-24.
RC   STRAIN=DSM 13525 / NCTC 13165 / R1;
RX   PubMed=22266942; DOI=10.1038/nature10729;
RA   Engel P., Goepfert A., Stanger F.V., Harms A., Schmidt A., Schirmer T.,
RA   Dehio C.;
RT   "Adenylylation control by intra- or intermolecular active-site obstruction
RT   in Fic proteins.";
RL   Nature 482:107-110(2012).
CC   -!- FUNCTION: Antitoxin component of type II toxin-antitoxin (TA) system
CC       VbhT-VbhA. Acts by inhibiting the adenylyltransferase activity of VbhT;
CC       competes with ATP-binding and prevents productive ATP-binding to VbhT.
CC       {ECO:0000269|PubMed:22266942}.
CC   -!- SUBUNIT: Interacts with VbhT. {ECO:0000269|PubMed:22266942}.
CC   -!- INTERACTION:
CC       E6Z0R4; E6Z0R3: vbhT; NbExp=2; IntAct=EBI-15965363, EBI-15965345;
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DR   EMBL; FN645515; CBI82702.1; -; Genomic_DNA.
DR   PDB; 3SHG; X-ray; 1.50 A; B=2-61.
DR   PDB; 3ZC7; X-ray; 2.10 A; B=2-62.
DR   PDB; 3ZCB; X-ray; 1.94 A; B=1-62.
DR   PDBsum; 3SHG; -.
DR   PDBsum; 3ZC7; -.
DR   PDBsum; 3ZCB; -.
DR   AlphaFoldDB; E6Z0R4; -.
DR   SMR; E6Z0R4; -.
DR   DIP; DIP-60137N; -.
DR   IntAct; E6Z0R4; 1.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:1900723; P:negative regulation of protein adenylylation; IDA:UniProtKB.
DR   CDD; cd11586; VbhA_like; 1.
DR   Gene3D; 1.10.8.1050; -; 1.
DR   InterPro; IPR041535; VbhA.
DR   InterPro; IPR033788; VbhA-like.
DR   InterPro; IPR043038; VbhA_sf.
DR   Pfam; PF18495; VbhA; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Nucleotide-binding; Toxin-antitoxin system.
FT   CHAIN           1..62
FT                   /note="Antitoxin VbhA"
FT                   /id="PRO_0000417550"
FT   MOTIF           20..25
FT                   /note="Inhibitory (S/T)XXXE(G/N) motif"
FT   BINDING         24
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000305"
FT   MUTAGEN         24
FT                   /note="E->G: Loss of antitoxin activity when transfected
FT                   into E.Coli cells."
FT                   /evidence="ECO:0000269|PubMed:22266942"
FT   HELIX           4..22
FT                   /evidence="ECO:0007829|PDB:3SHG"
FT   TURN            23..25
FT                   /evidence="ECO:0007829|PDB:3SHG"
FT   HELIX           30..40
FT                   /evidence="ECO:0007829|PDB:3SHG"
FT   HELIX           46..58
FT                   /evidence="ECO:0007829|PDB:3SHG"
SQ   SEQUENCE   62 AA;  7270 MW;  FD80CC67A913A5AF CRC64;
     MLSEEEIEYR RRDARNALAS QRLEGLEPDP QVVAQMERVV VGELETSDVI KDLMERIKRE
     EI