ID   ASR_YERPY               Reviewed;         121 AA.
AC   B1JR58;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 48.
DE   RecName: Full=Acid shock protein {ECO:0000255|HAMAP-Rule:MF_00546};
DE   Flags: Precursor;
GN   Name=asr {ECO:0000255|HAMAP-Rule:MF_00546}; OrderedLocusNames=YPK_1120;
OS   Yersinia pseudotuberculosis serotype O:3 (strain YPIII).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=502800;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YPIII;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C.,
RA   Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Challacombe J.F., Green L., Lindler L.E., Nikolich M.P., Richardson P.;
RT   "Complete sequence of Yersinia pseudotuberculosis YPIII.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Required for growth and/or survival at acidic conditions.
CC       {ECO:0000255|HAMAP-Rule:MF_00546}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_00546}.
CC   -!- PTM: Proteolytic processing gives rise to the active protein.
CC       {ECO:0000255|HAMAP-Rule:MF_00546}.
CC   -!- SIMILARITY: Belongs to the Asr family. {ECO:0000255|HAMAP-
CC       Rule:MF_00546}.
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; CP000950; ACA67418.1; -; Genomic_DNA.
DR   RefSeq; WP_011192847.1; NZ_CP009792.1.
DR   AlphaFoldDB; B1JR58; -.
DR   EnsemblBacteria; ACA67418; ACA67418; YPK_1120.
DR   GeneID; 66844622; -.
DR   KEGG; ypy:YPK_1120; -.
DR   PATRIC; fig|502800.11.peg.1750; -.
DR   OMA; KVHHKKA; -.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0010447; P:response to acidic pH; IEA:InterPro.
DR   HAMAP; MF_00546; Asr; 1.
DR   InterPro; IPR023497; Acid_shock.
DR   InterPro; IPR009435; Asr.
DR   Pfam; PF06392; Asr; 1.
PE   3: Inferred from homology;
KW   Periplasm; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00546"
FT   PROPEP          22..63
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00546"
FT                   /id="PRO_1000128939"
FT   CHAIN           64..121
FT                   /note="Acid shock protein"
FT                   /id="PRO_1000128940"
FT   REGION          40..121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        52..75
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   121 AA;  12550 MW;  274939C1AB36F875 CRC64;
     MKKVLALMVA ATLGLSSVAF AADTTATATP AATSTTATVA AQTKATQHQK HKVTKKTTEQ
     KAQAAKKHEK KASVQKAPVQ KAQAAKKHVK KASVQKAPVQ KAQAAKKHHK TAKKPVAAPA
     A