ID   ASR_ECO8A               Reviewed;         102 AA.
AC   B7LZY9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 46.
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=ECIAI1_1647;
OS   Escherichia coli O8 (strain IAI1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585034;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IAI1;
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; CU928160; CAQ98504.1; -; Genomic_DNA.
DR   RefSeq; WP_001342195.1; NC_011741.1.
DR   AlphaFoldDB; B7LZY9; -.
DR   KEGG; ecr:ECIAI1_1647; -.
DR   HOGENOM; CLU_102486_2_0_6; -.
DR   OMA; TTHVKKH; -.
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_1000128925"
FT   CHAIN           59..102
FT                   /note="Acid shock protein"
FT                   /id="PRO_1000128926"
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"
FT   COMPBIAS        68..82
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   102 AA;  10490 MW;  2C3E5B586D2964AE CRC64;
     MKKVLALVVA AAMGLSSAAF AAETATTPAP TATTTKAAPA KTTHHKKQHK AAPAQKAQAA
     KKHHKNTKAE QKAPEQKAQA AKKHAGKHSH QQPAKPAAQP AA