ID   VIBE_VIBCH              Reviewed;         543 AA.
AC   O07899; Q9JQ10;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Vibriobactin-specific 2,3-dihydroxybenzoate-AMP ligase;
DE            EC=6.2.1.71 {ECO:0000250|UniProtKB:P10378};
DE   AltName: Full=Dihydroxybenzoic acid-activating enzyme;
GN   Name=vibE; OrderedLocusNames=VC_0772;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=El Tor Lou15;
RX   PubMed=9371453; DOI=10.1128/jb.179.22.7055-7062.1997;
RA   Wyckoff E.E., Stoebner J.A., Reed K.E., Payne S.M.;
RT   "Cloning of a Vibrio cholerae vibriobactin gene cluster: identification of
RT   genes required for early steps in siderophore biosynthesis.";
RL   J. Bacteriol. 179:7055-7062(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
CC   -!- FUNCTION: Activation of the carboxylate group of 2,3-dihydroxy-benzoate
CC       (DHB), via ATP-dependent PPi exchange reactions, to the acyladenylate,
CC       preparing that molecule for the final stages of vibriobactin synthesis.
CC       {ECO:0000250|UniProtKB:P10378}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2,3-dihydroxybenzoate + ATP + holo-[aryl-carrier protein] =
CC         2,3-dihydroxybenzoyl-[aryl-carrier protein] + AMP + diphosphate;
CC         Xref=Rhea:RHEA:61652, Rhea:RHEA-COMP:15903, Rhea:RHEA-COMP:17559,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:36654,
CC         ChEBI:CHEBI:64479, ChEBI:CHEBI:90610, ChEBI:CHEBI:456215;
CC         EC=6.2.1.71; Evidence={ECO:0000250|UniProtKB:P10378};
CC   -!- PATHWAY: Siderophore biosynthesis; vibriobactin biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Single-pass
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U52150; AAC45927.1; -; Genomic_DNA.
DR   EMBL; AE003852; AAF93937.1; -; Genomic_DNA.
DR   PIR; H82282; H82282.
DR   RefSeq; NP_230421.1; NC_002505.1.
DR   RefSeq; WP_000205544.1; NZ_LT906614.1.
DR   AlphaFoldDB; O07899; -.
DR   SMR; O07899; -.
DR   STRING; 243277.VC_0772; -.
DR   DNASU; 2615315; -.
DR   EnsemblBacteria; AAF93937; AAF93937; VC_0772.
DR   GeneID; 57739482; -.
DR   KEGG; vch:VC_0772; -.
DR   PATRIC; fig|243277.26.peg.736; -.
DR   eggNOG; COG1021; Bacteria.
DR   HOGENOM; CLU_000022_59_7_6; -.
DR   OMA; PNIRFIR; -.
DR   BioCyc; MetaCyc:VC0772-MON; -.
DR   BioCyc; VCHO:VC0772-MON; -.
DR   BRENDA; 6.2.1.71; 15862.
DR   UniPathway; UPA00022; -.
DR   Proteomes; UP000000584; Chromosome 1.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008668; F:(2,3-dihydroxybenzoyl)adenylate synthase activity; IEA:InterPro.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0019290; P:siderophore biosynthetic process; IEA:InterPro.
DR   GO; GO:0019537; P:vibriobactin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.30.300.30; -; 1.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR011963; DHB_AMP_lig.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   TIGRFAMs; TIGR02275; DHB_AMP_lig; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Ligase; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..543
FT                   /note="Vibriobactin-specific 2,3-dihydroxybenzoate-AMP
FT                   ligase"
FT                   /id="PRO_0000193080"
FT   TRANSMEM        240..259
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   543 AA;  60065 MW;  1532583565B8C647 CRC64;
     MTTDFTPWPE ALAAQYRQLG YWQDKTLLDY LQQSAERTPN ALALVGDNQQ WRYQAMLERI
     EQLAAGFTEL GLGCGDNVVL QLGNVAEFYL CFFALLRQGI RPILALPAHR LAEIRYFCQH
     SQAKAYLIDG AQRPFDYQAL AQELLACCPT LQTVIVRGQT RVTDPKFIEL ASCYSASSCQ
     ANADPNQIAF FQLSGGTTGT PKLIPRTHND YAYSVTASVE ICRFDQHTRY LCVLPAAHNF
     PLSSPGALGV FWAGGCVVLS QDASPQHAFK LIEQHKITVT ALVPPLALLW MDHAEKSTYD
     LSSLHFVQVG GAKFSEAAAR RLPKALGCQL QQVFGMAEGL VNYTRLDDSA ELIATTQGRP
     ISAHDQLLVV DEQGQPVASG EEGYLLTQGP YTIRGYYRAD QHNQRAFNAQ GFYITGDKVK
     LSSEGYVIVT GRAKDQINRG GEKIAAEEVE NQLLHHPAVH DAALIAISDE YLGERSCAVI
     VLKPEQSVNT IQLKRFLHQA GLADYKIPDQ IQFIDQLPKT SVGKIDKNAL RRRFDTLGLA
     LMS