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CSGB_ECOLI
ID   CSGB_ECOLI              Reviewed;         151 AA.
AC   P0ABK7; P39828;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Minor curlin subunit;
DE   Flags: Precursor;
GN   Name=csgB; OrderedLocusNames=b1041, JW1024;
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 / MC4100 / ATCC 35695 / DSM 6574;
RX   PubMed=8817489; DOI=10.1111/j.1365-2958.1995.mmi_18040661.x.;
RA   Hammar M., Arnqvist A., Bian Z., Olsen A., Normark S.;
RT   "Expression of two csg operons is required for production of
RT   fibronectin- and congo red-binding curli polymers in Escherichia coli K-
RT   12.";
RL   Mol. Microbiol. 18:661-670(1995).
RN   [2]
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   [3]
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   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
RC   STRAIN=K12;
RX   PubMed=7854117; DOI=10.1111/j.1365-2958.1994.tb00493.x;
RA   Arnqvist A., Olsen A., Normark S.;
RT   "Sigma S-dependent growth-phase induction of the csgBA promoter in
RT   Escherichia coli can be achieved in vivo by sigma 70 in the absence of the
RT   nucleoid-associated protein H-NS.";
RL   Mol. Microbiol. 13:1021-1032(1994).
RN   [6]
RP   INDUCTION, AND OPERON STRUCTURE.
RC   STRAIN=K12 / MC4100;
RX   PubMed=17010156; DOI=10.1111/j.1365-2958.2006.05440.x;
RA   Weber H., Pesavento C., Possling A., Tischendorf G., Hengge R.;
RT   "Cyclic-di-GMP-mediated signalling within the sigma network of Escherichia
RT   coli.";
RL   Mol. Microbiol. 62:1014-1034(2006).
RN   [7]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=24097954; DOI=10.1128/jb.00946-13;
RA   Serra D.O., Richter A.M., Hengge R.;
RT   "Cellulose as an architectural element in spatially structured Escherichia
RT   coli biofilms.";
RL   J. Bacteriol. 195:5540-5554(2013).
CC   -!- FUNCTION: Curlin is the structural subunit of the curli fimbriae. Curli
CC       are coiled surface structures that assemble preferentially at growth
CC       temperatures below 37 degrees Celsius. Curli can bind to fibronectin.
CC       The minor subunit is the nucleation component of curlin monomers.
CC       Coexpression of cellulose and thin aggregative fimbriae (curli fimbrae
CC       or fibers) leads to a hydrophobic network with tightly packed cells
CC       embedded in a highly inert matrix that confers cohesion, elasticity and
CC       tissue-like properties to colonies (PubMed:24097954).
CC       {ECO:0000269|PubMed:24097954}.
CC   -!- INTERACTION:
CC       P0ABK7; P0ABK7: csgB; NbExp=3; IntAct=EBI-15647688, EBI-15647688;
CC   -!- SUBCELLULAR LOCATION: Fimbrium. Note=Part of the curli surface
CC       structure.
CC   -!- INDUCTION: Under control of the CsgD transcription factor, part of the
CC       csgBAC/ymdA operon. {ECO:0000269|PubMed:17010156}.
CC   -!- DISRUPTION PHENOTYPE: When disrupted in a cellulose-synthesizing strain
CC       (with a functional bcsQ gene), cellulose is made but colony morphology
CC       indicates no curli are made. {ECO:0000269|PubMed:24097954}.
CC   -!- MISCELLANEOUS: Cellulose production is abolished in E.coli K12 / MG1655
CC       and W3110 due to a premature stop codon in bcsQ (PubMed:24097954).
CC       {ECO:0000305|PubMed:24097954}.
CC   -!- SIMILARITY: Belongs to the CsgA/CsgB family. {ECO:0000305}.
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DR   EMBL; X90754; CAA62281.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC74125.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA35831.1; -; Genomic_DNA.
DR   PIR; S70787; S70787.
DR   RefSeq; NP_415559.1; NC_000913.3.
DR   RefSeq; WP_000791650.1; NZ_STEB01000016.1.
DR   AlphaFoldDB; P0ABK7; -.
DR   BioGRID; 4259358; 11.
DR   DIP; DIP-46504N; -.
DR   IntAct; P0ABK7; 1.
DR   STRING; 511145.b1041; -.
DR   PaxDb; P0ABK7; -.
DR   PRIDE; P0ABK7; -.
DR   EnsemblBacteria; AAC74125; AAC74125; b1041.
DR   EnsemblBacteria; BAA35831; BAA35831; BAA35831.
DR   GeneID; 66670691; -.
DR   GeneID; 947391; -.
DR   KEGG; ecj:JW1024; -.
DR   KEGG; eco:b1041; -.
DR   PATRIC; fig|1411691.4.peg.1228; -.
DR   EchoBASE; EB2505; -.
DR   eggNOG; ENOG5033BC9; Bacteria.
DR   HOGENOM; CLU_116264_1_0_6; -.
DR   InParanoid; P0ABK7; -.
DR   OMA; INIVQGR; -.
DR   PhylomeDB; P0ABK7; -.
DR   BioCyc; EcoCyc:G6547-MON; -.
DR   PRO; PR:P0ABK7; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0009279; C:cell outer membrane; IDA:EcoCyc.
DR   GO; GO:0009289; C:pilus; IDA:EcoCyc.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:1990000; P:amyloid fibril formation; IDA:EcoCyc.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   GO; GO:0098775; P:curli assembly; IMP:EcoCyc.
DR   GO; GO:0044010; P:single-species biofilm formation; IMP:EcoCyc.
DR   InterPro; IPR009742; Curlin_rpt.
DR   Pfam; PF07012; Curlin_rpt; 3.
PE   1: Evidence at protein level;
KW   Fimbrium; Reference proteome; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..151
FT                   /note="Minor curlin subunit"
FT                   /id="PRO_0000006374"
SQ   SEQUENCE   151 AA;  15882 MW;  B18D266B964014B8 CRC64;
     MKNKLLFMML TILGAPGIAA AAGYDLANSE YNFAVNELSK SSFNQAAIIG QAGTNNSAQL
     RQGGSKLLAV VAQEGSSNRA KIDQTGDYNL AYIDQAGSAN DASISQGAYG NTAMIIQKGS
     GNKANITQYG TQKTAIVVQR QSQMAIRVTQ R
 
 
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