ID   HDEA_BRUA2              Reviewed;         114 AA.
AC   Q2YK18;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   25-MAY-2022, entry version 81.
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=BAB2_0862;
OS   Brucella abortus (strain 2308).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=359391;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2308;
RX   PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005;
RA   Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
RA   Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT   "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL   Infect. Immun. 73:8353-8361(2005).
RN   [2]
RP   PROTEIN SEQUENCE OF 27-41, AND FUNCTION IN ACID RESISTANCE AND VIRULENCE.
RX   PubMed=15863292; DOI=10.1016/j.vetmic.2005.01.018;
RA   Valderas M.W., Alcantara R.B., Baumgartner J.E., Bellaire B.H.,
RA   Robertson G.T., Ng W.-L., Richardson J.M., Winkler M.E., Roop R.M. II;
RT   "Role of HdeA in acid resistance and virulence in Brucella abortus 2308.";
RL   Vet. Microbiol. 107:307-312(2005).
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 (By similarity).
CC       Contributes to acid resistance. Not required for wild-type virulence in
CC       the BALB/c mouse model. {ECO:0000255|HAMAP-Rule:MF_00946,
CC       ECO:0000269|PubMed:15863292}.
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; AM040265; CAJ13028.1; -; Genomic_DNA.
DR   RefSeq; WP_002966248.1; NZ_KN046823.1.
DR   AlphaFoldDB; Q2YK18; -.
DR   SMR; Q2YK18; -.
DR   STRING; 359391.BAB2_0862; -.
DR   EnsemblBacteria; CAJ13028; CAJ13028; BAB2_0862.
DR   GeneID; 3828246; -.
DR   GeneID; 55592038; -.
DR   KEGG; bmf:BAB2_0862; -.
DR   PATRIC; fig|359391.11.peg.550; -.
DR   HOGENOM; CLU_170142_0_0_5; -.
DR   OMA; ACTENKK; -.
DR   PhylomeDB; Q2YK18; -.
DR   PRO; PR:Q2YK18; -.
DR   Proteomes; UP000002719; 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   1: Evidence at protein level;
KW   Chaperone; Direct protein sequencing; Disulfide bond; Periplasm;
KW   Reference proteome; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00946,
FT                   ECO:0000269|PubMed:15863292"
FT   CHAIN           27..114
FT                   /note="Probable acid stress chaperone HdeA"
FT                   /id="PRO_0000338631"
FT   DISULFID        46..94
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00946"
SQ   SEQUENCE   114 AA;  12332 MW;  0B5A298253466C53 CRC64;
     MIKALFNKNT ALAAVAILAL SGGAMAESAK THKTDMAKKK VSELTCEDFN GLEESFKPTV
     VGWVVGFNKK GKEEDAVIDV DGIETVTPAI IEACKQEPKA SFWKKAEAEL KKVF