ASR_ECOLI
ID ASR_ECOLI Reviewed; 102 AA.
AC P36560; P77267;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 3.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Acid shock protein;
DE Flags: Precursor;
GN Name=asr; OrderedLocusNames=b1597, JW5826;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / N2212;
RX PubMed=10094685; DOI=10.1128/jb.181.7.2084-2093.1999;
RA Suziedeliene E., Suziedelis K., Garbenciute V., Normark S.;
RT "The acid-inducible asr gene in Escherichia coli: transcriptional control
RT by the phoBR operon.";
RL J. Bacteriol. 181:2084-2093(1999).
RN [2]
RP SEQUENCE REVISION.
RA Suziedeliene E.;
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP PROTEIN SEQUENCE OF 22-31 AND 59-68, PROTEOLYTIC PROCESSING, FUNCTION, AND
RP IDENTIFICATION OF START CODON.
RX PubMed=12670971; DOI=10.1128/jb.185.8.2475-2484.2003;
RA Seputiene V., Motiejunas D., Suziedelis K., Tomenius H., Normark S.,
RA Melefors O., Suziedeliene E.;
RT "Molecular characterization of the acid-inducible asr gene of Escherichia
RT coli and its role in acid stress response.";
RL J. Bacteriol. 185:2475-2484(2003).
CC -!- FUNCTION: Required for growth and/or survival at acidic conditions (pH
CC 4.5). Needed for the adaptation process at pH 4.5 that enables cells to
CC survive at extremely low pH (pH 2.0). {ECO:0000269|PubMed:12670971}.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- INDUCTION: By high environmental acidity.
CC -!- PTM: Proteolytic processing gives rise to the active protein.
CC {ECO:0000269|PubMed:12670971}.
CC -!- SIMILARITY: Belongs to the Asr family. {ECO:0000305}.
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; AF405541; AAA23500.2; -; Genomic_DNA.
DR EMBL; U00096; AAC74669.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA15331.2; -; Genomic_DNA.
DR PIR; G64915; G64915.
DR RefSeq; NP_416114.2; NC_000913.3.
DR RefSeq; WP_001340364.1; NZ_SSZK01000001.1.
DR AlphaFoldDB; P36560; -.
DR BioGRID; 4259122; 16.
DR BioGRID; 849492; 3.
DR DIP; DIP-9183N; -.
DR IntAct; P36560; 5.
DR STRING; 511145.b1597; -.
DR PaxDb; P36560; -.
DR PRIDE; P36560; -.
DR EnsemblBacteria; AAC74669; AAC74669; b1597.
DR EnsemblBacteria; BAA15331; BAA15331; BAA15331.
DR GeneID; 945103; -.
DR KEGG; ecj:JW5826; -.
DR KEGG; eco:b1597; -.
DR PATRIC; fig|511145.12.peg.1668; -.
DR EchoBASE; EB2069; -.
DR eggNOG; ENOG5032U9T; Bacteria.
DR HOGENOM; CLU_102486_2_0_6; -.
DR OMA; TTHVKKH; -.
DR BioCyc; EcoCyc:G6855-MON; -.
DR PRO; PR:P36560; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0010447; P:response to acidic pH; IMP:EcoCyc.
DR GO; GO:0010043; P:response to zinc ion; IEP:EcoCyc.
DR HAMAP; MF_00546; Asr; 1.
DR InterPro; IPR023497; Acid_shock.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Periplasm; Reference proteome; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:12670971"
FT PROPEP 22..58
FT /evidence="ECO:0000269|PubMed:12670971"
FT /id="PRO_0000269503"
FT CHAIN 59..102
FT /note="Acid shock protein"
FT /id="PRO_0000002402"
FT REGION 21..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..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; 10591 MW; 3E92AAE86D3975AF CRC64;
MKKVLALVVA AAMGLSSAAF AAETTTTPAP TATTTKAAPA KTTHHKKQHK AAPAQKAQAA
KKHHKNTKAE QKAPEQKAQA AKKHAKKHSH QQPAKPAAQP AA
