ID   EHPR_ENTAG              Reviewed;         129 AA.
AC   Q8GPH6;
DT   11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 46.
DE   RecName: Full=Phenazine antibiotic resistance protein EhpR;
GN   Name=ehpR {ECO:0000312|EMBL:AAN40889.1};
OS   Enterobacter agglomerans (Erwinia herbicola) (Pantoea agglomerans).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Pantoea; Pantoea agglomerans group.
OX   NCBI_TaxID=549;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAN40889.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], OPERON STRUCTURE, FUNCTION, AND
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=Eh1087 {ECO:0000312|EMBL:AAN40889.1};
RX   PubMed=12139622; DOI=10.1046/j.1365-2958.2002.03048.x;
RA   Giddens S.R., Feng Y., Mahanty H.K.;
RT   "Characterization of a novel phenazine antibiotic gene cluster in Erwinia
RT   herbicola Eh1087.";
RL   Mol. Microbiol. 45:769-783(2002).
RN   [2] {ECO:0000305, ECO:0000312|PDB:3SK1}
RP   X-RAY CRYSTALLOGRAPHY (1.01 ANGSTROMS) OF APOPROTEIN AND IN COMPLEX WITH
RP   GRISEOLUTEIC ACID, FUNCTION, AND SUBUNIT.
RC   STRAIN=Eh1087 {ECO:0000269|PubMed:21849072};
RX   PubMed=21849072; DOI=10.1186/1472-6807-11-33;
RA   Yu S., Vit A., Devenish S., Mahanty H.K., Itzen A., Goody R.S.,
RA   Blankenfeldt W.;
RT   "Atomic resolution structure of EhpR: phenazine resistance in Enterobacter
RT   agglomerans Eh1087 follows principles of bleomycin/mitomycin C resistance
RT   in other bacteria.";
RL   BMC Struct. Biol. 11:33-33(2011).
CC   -!- FUNCTION: Required for resistance to the phenazine antibiotic D-
CC       alanylgriseoluteic acid (AGA), an antibiotic produced by E.agglomerans
CC       itself, and thus protects the bacterium against phenazine toxicity.
CC       Probably binds AGA and acts as a chaperone that works in tandem with a
CC       membrane transporter for subsequent antibiotic secretion.
CC       {ECO:0000269|PubMed:12139622, ECO:0000269|PubMed:21849072}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:21849072}.
CC   -!- DISRUPTION PHENOTYPE: Loss of D-alanylgriseoluteic acid resistance.
CC       {ECO:0000269|PubMed:12139622}.
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DR   EMBL; AF451953; AAN40889.1; -; Genomic_DNA.
DR   PDB; 3SK1; X-ray; 2.15 A; A/B/C/D=1-129.
DR   PDB; 3SK2; X-ray; 1.01 A; A/B=1-129.
DR   PDBsum; 3SK1; -.
DR   PDBsum; 3SK2; -.
DR   AlphaFoldDB; Q8GPH6; -.
DR   SMR; Q8GPH6; -.
DR   GO; GO:0043177; F:organic acid binding; IDA:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:0046677; P:response to antibiotic; IDA:UniProtKB.
DR   InterPro; IPR029068; Glyas_Bleomycin-R_OHBP_Dase.
DR   InterPro; IPR004360; Glyas_Fos-R_dOase_dom.
DR   InterPro; IPR026275; Glyoxalase/dOase/EhpR.
DR   InterPro; IPR037523; VOC.
DR   Pfam; PF00903; Glyoxalase; 1.
DR   PIRSF; PIRSF039020; EhpR; 1.
DR   SUPFAM; SSF54593; SSF54593; 1.
DR   PROSITE; PS51819; VOC; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antibiotic resistance; Chaperone.
FT   CHAIN           1..129
FT                   /note="Phenazine antibiotic resistance protein EhpR"
FT                   /id="PRO_0000429274"
FT   DOMAIN          10..128
FT                   /note="VOC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT   BINDING         42..43
FT                   /ligand="D-alanylgriseoluteate"
FT                   /ligand_id="ChEBI:CHEBI:167053"
FT                   /evidence="ECO:0000305|PubMed:21849072,
FT                   ECO:0007744|PDB:3SK2"
FT   BINDING         57
FT                   /ligand="D-alanylgriseoluteate"
FT                   /ligand_id="ChEBI:CHEBI:167053"
FT                   /evidence="ECO:0000305|PubMed:21849072,
FT                   ECO:0007744|PDB:3SK2"
FT   STRAND          13..17
FT                   /evidence="ECO:0007829|PDB:3SK2"
FT   HELIX           21..32
FT                   /evidence="ECO:0007829|PDB:3SK2"
FT   STRAND          37..39
FT                   /evidence="ECO:0007829|PDB:3SK2"
FT   STRAND          41..47
FT                   /evidence="ECO:0007829|PDB:3SK2"
FT   STRAND          53..60
FT                   /evidence="ECO:0007829|PDB:3SK2"
FT   STRAND          71..79
FT                   /evidence="ECO:0007829|PDB:3SK2"
FT   HELIX           80..92
FT                   /evidence="ECO:0007829|PDB:3SK2"
FT   STRAND          94..96
FT                   /evidence="ECO:0007829|PDB:3SK2"
FT   STRAND          99..107
FT                   /evidence="ECO:0007829|PDB:3SK2"
FT   STRAND          110..116
FT                   /evidence="ECO:0007829|PDB:3SK2"
FT   STRAND          122..127
FT                   /evidence="ECO:0007829|PDB:3SK2"
SQ   SEQUENCE   129 AA;  14626 MW;  7A308F939EB273A3 CRC64;
     MTDLAGPTIT PNLQLVYVSN VERSTDFYRF IFKKEPVFVT PRYVAFPSSG DALFAIWSGG
     EEPVAEIPRF SEIGIMLPTG EDVDKLFNEW TKQKSHQIIV IKEPYTDVFG RTFLISDPDG
     HIIRVCPLD