ASR_ECO81
ID ASR_ECO81 Reviewed; 102 AA.
AC B7MV44;
DT 28-JUL-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=ECED1_1766;
OS Escherichia coli O81 (strain ED1a).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585397;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ED1a;
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; CU928162; CAR07960.2; -; Genomic_DNA.
DR AlphaFoldDB; B7MV44; -.
DR EnsemblBacteria; CAR07960; CAR07960; ECED1_1766.
DR KEGG; ecq:ECED1_1766; -.
DR HOGENOM; CLU_102486_2_0_6; -.
DR OMA; TTHVKKH; -.
DR Proteomes; UP000000748; 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_1000146601"
FT CHAIN 59..102
FT /note="Acid shock protein"
FT /id="PRO_1000146602"
FT REGION 26..102
FT /note="Disordered"
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; 10543 MW; 0A622B45C1C13DB4 CRC64;
MKKVLALVVA AAMGLSSAAF AAETAITPAP TATTTKAAPA KTTHHKKQHK AAPAQKAQAA
KKHHKNAKAE QKAPEQKAQA AKKHAKKHSH QQPAKPAAQP AA