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HDEA_BRUO2
ID   HDEA_BRUO2              Reviewed;         114 AA.
AC   A5VU57;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Probable acid stress chaperone HdeA {ECO:0000255|HAMAP-Rule:MF_00946};
DE   Flags: Precursor;
GN   Name=hdeA {ECO:0000255|HAMAP-Rule:MF_00946}; OrderedLocusNames=BOV_A0312;
OS   Brucella ovis (strain ATCC 25840 / 63/290 / NCTC 10512).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=444178;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25840 / 63/290 / NCTC 10512;
RX   PubMed=19436743; DOI=10.1371/journal.pone.0005519;
RA   Tsolis R.M., Seshadri R., Santos R.L., Sangari F.J., Lobo J.M.,
RA   de Jong M.F., Ren Q., Myers G., Brinkac L.M., Nelson W.C., Deboy R.T.,
RA   Angiuoli S., Khouri H., Dimitrov G., Robinson J.R., Mulligan S.,
RA   Walker R.L., Elzer P.E., Hassan K.A., Paulsen I.T.;
RT   "Genome degradation in Brucella ovis corresponds with narrowing of its host
RT   range and tissue tropism.";
RL   PLoS ONE 4:E5519-E5519(2009).
CC   -!- FUNCTION: Required for optimal acid stress protection. Exhibits a
CC       chaperone-like activity only at low pH by suppressing non-specifically
CC       the aggregation of denaturated periplasmic proteins.
CC       {ECO:0000255|HAMAP-Rule:MF_00946}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_00946}.
CC   -!- SIMILARITY: Belongs to the HdeA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00946}.
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DR   EMBL; CP000709; ABQ62812.1; -; Genomic_DNA.
DR   RefSeq; WP_006015518.1; NC_009504.1.
DR   AlphaFoldDB; A5VU57; -.
DR   SMR; A5VU57; -.
DR   EnsemblBacteria; ABQ62812; ABQ62812; BOV_A0312.
DR   GeneID; 45125720; -.
DR   KEGG; bov:BOV_A0312; -.
DR   HOGENOM; CLU_170142_0_0_5; -.
DR   OMA; ACTENKK; -.
DR   PhylomeDB; A5VU57; -.
DR   PRO; PR:A5VU57; -.
DR   Proteomes; UP000006383; Chromosome II.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR   GO; GO:1990451; P:cellular stress response to acidic pH; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.890.10; -; 1.
DR   HAMAP; MF_00946; HdeA; 1.
DR   InterPro; IPR024972; HdeA.
DR   InterPro; IPR038303; HdeA/HdeB_sf.
DR   InterPro; IPR036831; HdeA_sf.
DR   InterPro; IPR010486; HNS-dep_expression_A/B.
DR   Pfam; PF06411; HdeA; 1.
DR   PIRSF; PIRSF009564; HNS-dep_expression_A; 1.
DR   SUPFAM; SSF47752; SSF47752; 1.
PE   3: Inferred from homology;
KW   Chaperone; Disulfide bond; Periplasm; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00946"
FT   CHAIN           27..114
FT                   /note="Probable acid stress chaperone HdeA"
FT                   /id="PRO_0000338635"
FT   DISULFID        46..94
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00946"
SQ   SEQUENCE   114 AA;  12392 MW;  175BE9971DF98C16 CRC64;
     MIKTLFNKNT ALAAVAILAL SGSAMAESAK THKTDMAKKK VSELTCEDFN GLEESFKPTV
     VGWVVGFNKK GKEEDAVIDV DGIETVTPAI IEACKQEPKA SFWKKAEAEL KKVF
 
 
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