ID   ASR_ECO45               Reviewed;         102 AA.
AC   B7M9V0;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, 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=ECS88_1642;
OS   Escherichia coli O45:K1 (strain S88 / ExPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585035;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S88 / ExPEC;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
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}.
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DR   EMBL; CU928161; CAR02957.1; -; Genomic_DNA.
DR   RefSeq; WP_001362115.1; NC_011742.1.
DR   AlphaFoldDB; B7M9V0; -.
DR   EnsemblBacteria; CAR02957; CAR02957; ECS88_1642.
DR   GeneID; 58459793; -.
DR   KEGG; ecz:ECS88_1642; -.
DR   HOGENOM; CLU_102486_2_0_6; -.
DR   OMA; TTHVKKH; -.
DR   Proteomes; UP000000747; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   HAMAP; MF_00546; Asr; 1.
DR   InterPro; IPR023497; Acid_shock.
PE   3: Inferred from homology;
KW   Periplasm; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00546"
FT   PROPEP          22..58
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00546"
FT                   /id="PRO_1000128921"
FT   CHAIN           59..102
FT                   /note="Acid shock protein"
FT                   /id="PRO_1000128922"
FT   REGION          22..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..39
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        40..67
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   102 AA;  10531 MW;  25881B45DBF214AE CRC64;
     MKKVLALVVA AAMGLSSAAF AAETATTPAP TATTTKAAPA KTTHHKKQHK AAPAQKAQAA
     KKHHKNAKAE QKAPEQKAQA AKKHAKKHSH QQPAKPAAQP AA