FIMG_ECOLI
ID FIMG_ECOLI Reviewed; 167 AA.
AC P08190; Q2M5Z4;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Protein FimG;
DE Flags: Precursor;
GN Name=fimG; OrderedLocusNames=b4319, JW4282;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2890081; DOI=10.1007/bf00328136;
RA Klemm P., Christiansen G.;
RT "Three fim genes required for the regulation of length and mediation of
RT adhesion of Escherichia coli type 1 fimbriae.";
RL Mol. Gen. Genet. 208:439-445(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
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).
CC -!- FUNCTION: Involved in regulation of length and mediation of adhesion of
CC type 1 fimbriae (but not necessary for the production of fimbriae).
CC Involved in the integration of FimH in the fimbriae.
CC -!- INTERACTION:
CC P08190; P31697: fimC; NbExp=5; IntAct=EBI-1785843, EBI-1028005;
CC -!- SUBCELLULAR LOCATION: Fimbrium.
CC -!- SIMILARITY: Belongs to the fimbrial protein family. {ECO:0000305}.
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DR EMBL; X05672; CAA29155.1; -; Genomic_DNA.
DR EMBL; U14003; AAA97215.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77275.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78312.1; -; Genomic_DNA.
DR PIR; S56544; S56544.
DR RefSeq; NP_418739.1; NC_000913.3.
DR RefSeq; WP_000870592.1; NZ_SSUV01000012.1.
DR PDB; 3BFQ; X-ray; 1.34 A; G=36-167.
DR PDB; 3BFW; X-ray; 1.80 A; A/C=36-167.
DR PDB; 3JWN; X-ray; 2.69 A; G/M=24-167.
DR PDB; 4J3O; X-ray; 3.80 A; G=24-167.
DR PDB; 4XO9; X-ray; 1.14 A; B=24-37.
DR PDB; 4XOA; X-ray; 2.54 A; B/D/F/H=24-37.
DR PDB; 4XOD; X-ray; 1.14 A; B=24-37.
DR PDB; 5IQM; X-ray; 1.50 A; A/G=36-167.
DR PDB; 5IQN; X-ray; 1.00 A; A/G=36-167.
DR PDB; 5IQO; X-ray; 1.30 A; A/C=36-167.
DR PDB; 6E14; EM; 4.00 A; G=10-167.
DR PDB; 6E15; EM; 6.20 A; G=10-167.
DR PDBsum; 3BFQ; -.
DR PDBsum; 3BFW; -.
DR PDBsum; 3JWN; -.
DR PDBsum; 4J3O; -.
DR PDBsum; 4XO9; -.
DR PDBsum; 4XOA; -.
DR PDBsum; 4XOD; -.
DR PDBsum; 5IQM; -.
DR PDBsum; 5IQN; -.
DR PDBsum; 5IQO; -.
DR PDBsum; 6E14; -.
DR PDBsum; 6E15; -.
DR AlphaFoldDB; P08190; -.
DR SMR; P08190; -.
DR BioGRID; 4262750; 9.
DR ComplexPortal; CPX-2855; Fimbrial Tip Complex FimFGH.
DR DIP; DIP-9615N; -.
DR IntAct; P08190; 1.
DR STRING; 511145.b4319; -.
DR PaxDb; P08190; -.
DR PRIDE; P08190; -.
DR EnsemblBacteria; AAC77275; AAC77275; b4319.
DR EnsemblBacteria; BAE78312; BAE78312; BAE78312.
DR GeneID; 948846; -.
DR KEGG; ecj:JW4282; -.
DR KEGG; eco:b4319; -.
DR PATRIC; fig|1411691.4.peg.2373; -.
DR EchoBASE; EB0310; -.
DR eggNOG; COG3539; Bacteria.
DR HOGENOM; CLU_088965_6_1_6; -.
DR InParanoid; P08190; -.
DR OMA; QAVISVT; -.
DR PhylomeDB; P08190; -.
DR BioCyc; EcoCyc:EG10314-MON; -.
DR EvolutionaryTrace; P08190; -.
DR PRO; PR:P08190; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009289; C:pilus; IBA:GO_Central.
DR GO; GO:0009419; C:pilus tip; IPI:ComplexPortal.
DR GO; GO:0007155; P:cell adhesion; IMP:ComplexPortal.
DR GO; GO:0043709; P:cell adhesion involved in single-species biofilm formation; IBA:GO_Central.
DR GO; GO:0031589; P:cell-substrate adhesion; IMP:ComplexPortal.
DR GO; GO:0007638; P:mechanosensory behavior; IDA:ComplexPortal.
DR Gene3D; 2.60.40.1090; -; 1.
DR InterPro; IPR036937; Adhesion_dom_fimbrial_sf.
DR InterPro; IPR008966; Adhesion_dom_sf.
DR SUPFAM; SSF49401; SSF49401; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Fimbrium; Reference proteome; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..167
FT /note="Protein FimG"
FT /id="PRO_0000009210"
FT SITE 166
FT /note="Required for stability and transport"
FT /evidence="ECO:0000250"
FT DISULFID 39..77
FT /evidence="ECO:0000305"
FT CONFLICT 61
FT /note="A -> S (in Ref. 1; CAA29155)"
FT /evidence="ECO:0000305"
FT CONFLICT 148..149
FT /note="NG -> KV (in Ref. 1; CAA29155)"
FT /evidence="ECO:0000305"
FT STRAND 26..34
FT /evidence="ECO:0007829|PDB:4XO9"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:5IQO"
FT STRAND 44..53
FT /evidence="ECO:0007829|PDB:5IQN"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:5IQN"
FT STRAND 68..75
FT /evidence="ECO:0007829|PDB:5IQN"
FT STRAND 83..89
FT /evidence="ECO:0007829|PDB:5IQN"
FT STRAND 96..99
FT /evidence="ECO:0007829|PDB:5IQN"
FT STRAND 108..112
FT /evidence="ECO:0007829|PDB:5IQN"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:5IQO"
FT STRAND 124..128
FT /evidence="ECO:0007829|PDB:5IQN"
FT TURN 131..134
FT /evidence="ECO:0007829|PDB:5IQN"
FT STRAND 135..145
FT /evidence="ECO:0007829|PDB:5IQN"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:5IQN"
FT STRAND 153..166
FT /evidence="ECO:0007829|PDB:5IQN"
SQ SEQUENCE 167 AA; 17317 MW; 8C3EF95FD442E22C CRC64;
MKWCKRGYVL AAILALASAT IQAADVTITV NGKVVAKPCT VSTTNATVDL GDLYSFSLMS
AGAASAWHDV ALELTNCPVG TSRVTASFSG AADSTGYYKN QGTAQNIQLE LQDDSGNTLN
TGATKTVQVD DSSQSAHFPL QVRALTVNGG ATQGTIQAVI SITYTYS
