ID   HDEA_SHIFL              Reviewed;         110 AA.
AC   P0AET1; P26604;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=Acid stress chaperone HdeA {ECO:0000255|HAMAP-Rule:MF_00946};
DE   Flags: Precursor;
GN   Name=hdeA {ECO:0000255|HAMAP-Rule:MF_00946};
GN   OrderedLocusNames=SF3544, S4223;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
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; AE005674; AAN44999.1; -; Genomic_DNA.
DR   EMBL; AE014073; AAP19187.1; -; Genomic_DNA.
DR   RefSeq; NP_709292.1; NC_004337.2.
DR   RefSeq; WP_000756550.1; NZ_WPGW01000225.1.
DR   AlphaFoldDB; P0AET1; -.
DR   BMRB; P0AET1; -.
DR   SMR; P0AET1; -.
DR   STRING; 198214.SF3544; -.
DR   EnsemblBacteria; AAN44999; AAN44999; SF3544.
DR   EnsemblBacteria; AAP19187; AAP19187; S4223.
DR   GeneID; 1026387; -.
DR   GeneID; 66672606; -.
DR   KEGG; sfl:SF3544; -.
DR   KEGG; sfx:S4223; -.
DR   PATRIC; fig|198214.7.peg.4174; -.
DR   HOGENOM; CLU_170142_1_0_6; -.
DR   OMA; ACTENKK; -.
DR   OrthoDB; 1861283at2; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; Chromosome.
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; Reference proteome; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00946"
FT   CHAIN           22..110
FT                   /note="Acid stress chaperone HdeA"
FT                   /id="PRO_0000045101"
FT   DISULFID        39..87
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00946"
SQ   SEQUENCE   110 AA;  11858 MW;  063262C4863FA2E9 CRC64;
     MKKVLGVILG GLLLLPVVSN AADAQKAADN KKPVNSWTCE DFLAVDESFQ PTAVGFAEAL
     NNKDKPEDAV LDVQGIATVT PAIVQACTQD KQANFKDKVK GEWDKIKKDM