BHSA_ECOLI
ID BHSA_ECOLI Reviewed; 85 AA.
AC P0AB40; P75953;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Multiple stress resistance protein BhsA;
DE AltName: Full=Copper-induced outer membrane component;
DE Flags: Precursor;
GN Name=bhsA; Synonyms=comC, ycfR; OrderedLocusNames=b1112, JW1098;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [2]
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 [3]
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 [4]
RP FUNCTION IN REGULATION OF BIOFILM FORMATION, INDUCTION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=K12 / BW25113;
RX PubMed=17293424; DOI=10.1128/jb.01832-06;
RA Zhang X.-S., Garcia-Contreras R., Wood T.K.;
RT "YcfR (BhsA) influences Escherichia coli biofilm formation through stress
RT response and surface hydrophobicity.";
RL J. Bacteriol. 189:3051-3062(2007).
RN [5]
RP FUNCTION IN COPPER TOLERANCE, SUBCELLULAR LOCATION, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=22089859; DOI=10.1007/s10534-011-9510-x;
RA Mermod M., Magnani D., Solioz M., Stoyanov J.V.;
RT "The copper-inducible ComR (YcfQ) repressor regulates expression of ComC
RT (YcfR), which affects copper permeability of the outer membrane of
RT Escherichia coli.";
RL BioMetals 25:33-43(2012).
CC -!- FUNCTION: Reduces the permeability of the outer membrane to copper.
CC Seems to be involved in the regulation of biofilm formation. May
CC decrease biofilm formation by repressing cell-cell interaction and cell
CC surface interaction. {ECO:0000269|PubMed:17293424,
CC ECO:0000269|PubMed:22089859}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane
CC {ECO:0000269|PubMed:22089859}.
CC -!- INDUCTION: Repressed by ComR. Induced by copper via release of ComR.
CC Induced in biofilms and by several stress conditions.
CC {ECO:0000269|PubMed:17293424, ECO:0000269|PubMed:22089859}.
CC -!- DISRUPTION PHENOTYPE: Disruption of this gene increases copper
CC sensitivity, induces stress response genes in biofilms, increases
CC aggregation and cell surface hydrophobicity, and decreases indole
CC synthesis. {ECO:0000269|PubMed:17293424, ECO:0000269|PubMed:22089859}.
CC -!- SIMILARITY: Belongs to the BhsA/McbA 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; U00096; AAC74196.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35927.1; -; Genomic_DNA.
DR PIR; E64855; E64855.
DR RefSeq; NP_415630.1; NC_000913.3.
DR RefSeq; WP_000800153.1; NZ_STEB01000016.1.
DR AlphaFoldDB; P0AB40; -.
DR SMR; P0AB40; -.
DR BioGRID; 4261348; 15.
DR DIP; DIP-48158N; -.
DR STRING; 511145.b1112; -.
DR PaxDb; P0AB40; -.
DR PRIDE; P0AB40; -.
DR EnsemblBacteria; AAC74196; AAC74196; b1112.
DR EnsemblBacteria; BAA35927; BAA35927; BAA35927.
DR GeneID; 66670622; -.
DR GeneID; 945492; -.
DR KEGG; ecj:JW1098; -.
DR KEGG; eco:b1112; -.
DR PATRIC; fig|1411691.4.peg.1155; -.
DR EchoBASE; EB3210; -.
DR eggNOG; ENOG5032ZBU; Bacteria.
DR HOGENOM; CLU_158602_2_3_6; -.
DR OMA; IQYPQGQ; -.
DR PhylomeDB; P0AB40; -.
DR BioCyc; EcoCyc:G6570-MON; -.
DR PRO; PR:P0AB40; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IDA:EcoCyc.
DR GO; GO:0046688; P:response to copper ion; IMP:EcoCyc.
DR GO; GO:0044010; P:single-species biofilm formation; IMP:EcoCyc.
DR Gene3D; 3.30.1660.10; -; 1.
DR InterPro; IPR025543; Dodecin-like.
DR InterPro; IPR036275; YdgH-like_sf.
DR InterPro; IPR010854; YdgH/BhsA/McbA-like_dom.
DR Pfam; PF07338; DUF1471; 1.
DR SUPFAM; SSF159871; SSF159871; 1.
PE 1: Evidence at protein level;
KW Cell outer membrane; Copper; Membrane; Reference proteome; Signal;
KW Stress response.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..85
FT /note="Multiple stress resistance protein BhsA"
FT /id="PRO_0000013825"
SQ SEQUENCE 85 AA; 8815 MW; BB5122FE73E72181 CRC64;
MKNVKTLIAA AILSSMSFAS FAAVEVQSTP EGQQKVGTIS ANAGTNLGSL EEQLAQKADE
MGAKSFRITS VTGPNTLHGT AVIYK
