ASR_ECOL5
ID ASR_ECOL5 Reviewed; 102 AA.
AC Q0THN1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 25-MAY-2022, entry version 59.
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=ECP_1541;
OS Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=362663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=536 / UPEC;
RX PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT "Role of pathogenicity island-associated integrases in the genome
RT plasticity of uropathogenic Escherichia coli strain 536.";
RL Mol. Microbiol. 61:584-595(2006).
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; CP000247; ABG69548.1; -; Genomic_DNA.
DR RefSeq; WP_001362115.1; NC_008253.1.
DR AlphaFoldDB; Q0THN1; -.
DR STRING; 362663.ECP_1541; -.
DR EnsemblBacteria; ABG69548; ABG69548; ECP_1541.
DR GeneID; 58459793; -.
DR KEGG; ecp:ECP_1541; -.
DR HOGENOM; CLU_102486_2_0_6; -.
DR OMA; TTHVKKH; -.
DR Proteomes; UP000009182; 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_0000316043"
FT CHAIN 59..102
FT /note="Acid shock protein"
FT /id="PRO_1000017750"
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