ID   CSGA_ECOLI              Reviewed;         151 AA.
AC   P28307;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 3.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=Major curlin subunit;
DE   Flags: Precursor;
GN   Name=csgA; OrderedLocusNames=b1042, JW1025;
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 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=8459772; DOI=10.1111/j.1365-2958.1993.tb01143.x;
RA   Olsen A., Arnqvist A.;
RT   "The RpoS sigma factor relieves H-NS-mediated transcriptional repression of
RT   csgA, the subunit gene of fibronectin-binding curli in Escherichia coli.";
RL   Mol. Microbiol. 7:523-536(1993).
RN   [2]
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   [3]
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   [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 21-40.
RC   STRAIN=K12 / YMEL;
RX   PubMed=1357528; DOI=10.1111/j.1365-2958.1992.tb01420.x;
RA   Arnqvist A., Olsen A., Pfeifer J., Russell D.G., Normark S.;
RT   "The Crl protein activates cryptic genes for curli formation and
RT   fibronectin binding in Escherichia coli HB101.";
RL   Mol. Microbiol. 6:2443-2452(1992).
RN   [7]
RP   PROTEIN SEQUENCE OF 21-31.
RX   PubMed=1677357; DOI=10.1128/jb.173.15.4773-4781.1991;
RA   Collinson S.K., Emoedy L., Mueller K.-H., Trust T.J., Kay W.W.;
RT   "Purification and characterization of thin, aggregative fimbriae from
RT   Salmonella enteritidis.";
RL   J. Bacteriol. 173:4773-4781(1991).
RN   [8]
RP   INDUCTION.
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).
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   -!- INTERACTION:
CC       P28307; P28307: csgA; NbExp=3; IntAct=EBI-15647673, EBI-15647673;
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   -!- SIMILARITY: Belongs to the CsgA/CsgB family. {ECO:0000305}.
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DR   EMBL; L04979; AAA23616.1; -; Genomic_DNA.
DR   EMBL; X90754; CAA62282.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC74126.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA35832.1; -; Genomic_DNA.
DR   PIR; S70788; S70788.
DR   RefSeq; NP_415560.1; NC_000913.3.
DR   RefSeq; WP_000771437.1; NZ_STEB01000016.1.
DR   PDB; 6G8C; X-ray; 1.65 A; B=47-52.
DR   PDB; 6G8D; X-ray; 1.85 A; A=45-50.
DR   PDB; 6G8E; X-ray; 1.70 A; A/B=137-142.
DR   PDB; 6G9G; X-ray; 1.60 A; B=129-134.
DR   PDB; 6L7C; EM; 3.34 A; S/T/U/V/W/X/Y/Z/a=21-42.
DR   PDBsum; 6G8C; -.
DR   PDBsum; 6G8D; -.
DR   PDBsum; 6G8E; -.
DR   PDBsum; 6G9G; -.
DR   PDBsum; 6L7C; -.
DR   AlphaFoldDB; P28307; -.
DR   SMR; P28307; -.
DR   BioGRID; 4260065; 16.
DR   DIP; DIP-9325N; -.
DR   IntAct; P28307; 1.
DR   STRING; 511145.b1042; -.
DR   ChEMBL; CHEMBL3309018; -.
DR   PaxDb; P28307; -.
DR   DNASU; 949055; -.
DR   EnsemblBacteria; AAC74126; AAC74126; b1042.
DR   EnsemblBacteria; BAA35832; BAA35832; BAA35832.
DR   GeneID; 66670690; -.
DR   GeneID; 949055; -.
DR   KEGG; ecj:JW1025; -.
DR   KEGG; eco:b1042; -.
DR   PATRIC; fig|1411691.4.peg.1227; -.
DR   EchoBASE; EB1452; -.
DR   eggNOG; ENOG5030M63; Bacteria.
DR   HOGENOM; CLU_1861613_0_0_6; -.
DR   InParanoid; P28307; -.
DR   OMA; NSEIQIY; -.
DR   PhylomeDB; P28307; -.
DR   BioCyc; EcoCyc:EG11489-MON; -.
DR   PRO; PR:P28307; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0009289; C:pilus; IEA:UniProtKB-SubCell.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
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   3D-structure; Direct protein sequencing; Fimbrium; Reference proteome;
KW   Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000269|PubMed:1357528,
FT                   ECO:0000269|PubMed:1677357"
FT   CHAIN           21..151
FT                   /note="Major curlin subunit"
FT                   /id="PRO_0000006369"
FT   REGION          71..90
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        7
FT                   /note="A -> E (in Ref. 1; AAA23616)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   151 AA;  15049 MW;  C003470D208D395F CRC64;
     MKLLKVAAIA AIVFSGSALA GVVPQYGGGG NHGGGGNNSG PNSELNIYQY GGGNSALALQ
     TDARNSDLTI TQHGGGNGAD VGQGSDDSSI DLTQRGFGNS ATLDQWNGKN SEMTVKQFGG
     GNGAAVDQTA SNSSVNVTQV GFGNNATAHQ Y