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FIMA1_ECOLI
ID   FIMA1_ECOLI             Reviewed;         182 AA.
AC   P04128; Q2M5Z9;
DT   01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 2.
DT   03-AUG-2022, entry version 153.
DE   RecName: Full=Type-1 fimbrial protein, A chain;
DE   AltName: Full=Type-1A pilin;
DE   Flags: Precursor;
GN   Name=fimA; Synonyms=pilA; OrderedLocusNames=b4314, JW4277;
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=2858471; DOI=10.1128/jb.162.1.454-457.1985;
RA   Orndorff P.E., Falkow S.;
RT   "Nucleotide sequence of pilA, the gene encoding the structural component of
RT   type 1 pili in Escherichia coli.";
RL   J. Bacteriol. 162:454-457(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6147250; DOI=10.1111/j.1432-1033.1984.tb08386.x;
RA   Klemm P.;
RT   "The fimA gene encoding the type-1 fimbrial subunit of Escherichia coli.
RT   Nucleotide sequence and primary structure of the protein.";
RL   Eur. J. Biochem. 143:395-399(1984).
RN   [3]
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   [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).
CC   -!- FUNCTION: Fimbriae (also called pili), polar filaments radiating from
CC       the surface of the bacterium to a length of 0.5-1.5 micrometers and
CC       numbering 100-300 per cell, enable bacteria to colonize the epithelium
CC       of specific host organs.
CC   -!- INTERACTION:
CC       P04128; P04128: fimA; NbExp=2; IntAct=EBI-15697528, EBI-15697528;
CC   -!- SUBCELLULAR LOCATION: Fimbrium.
CC   -!- SIMILARITY: Belongs to the fimbrial protein family. {ECO:0000305}.
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DR   EMBL; X00981; CAA25489.1; -; Genomic_DNA.
DR   EMBL; M27603; AAA24389.1; -; Genomic_DNA.
DR   EMBL; U14003; AAA97210.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC77270.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE78307.1; -; Genomic_DNA.
DR   PIR; S56539; YQECT1.
DR   RefSeq; NP_418734.1; NC_000913.3.
DR   RefSeq; WP_000695564.1; NZ_LN832404.1.
DR   PDB; 2JTY; NMR; -; A=24-182.
DR   PDB; 2M5G; NMR; -; A=24-182.
DR   PDB; 2N7H; NMR; -; A/B/C/D/E/F=24-182.
DR   PDB; 3SQB; X-ray; 3.20 A; B/D/F/H=37-182.
DR   PDB; 4DWH; X-ray; 2.50 A; B/D=41-182.
DR   PDB; 5NKT; X-ray; 1.50 A; A=24-182.
DR   PDB; 5OH0; EM; 4.20 A; A/B/C/D/E/F=24-182.
DR   PDB; 6C53; EM; 4.20 A; A/B/C/D/E/F/G/H/I/J/K=24-182.
DR   PDB; 6R74; X-ray; 1.81 A; A=42-182.
DR   PDB; 6R7E; X-ray; 1.79 A; A=31-182.
DR   PDB; 6S09; X-ray; 1.50 A; A/B/C/D/E/F/G/H=42-182.
DR   PDB; 6SWH; X-ray; 2.80 A; C/F=37-182.
DR   PDB; 6Y7S; EM; 2.80 A; A/B/C/D/E/F=1-182.
DR   PDBsum; 2JTY; -.
DR   PDBsum; 2M5G; -.
DR   PDBsum; 2N7H; -.
DR   PDBsum; 3SQB; -.
DR   PDBsum; 4DWH; -.
DR   PDBsum; 5NKT; -.
DR   PDBsum; 5OH0; -.
DR   PDBsum; 6C53; -.
DR   PDBsum; 6R74; -.
DR   PDBsum; 6R7E; -.
DR   PDBsum; 6S09; -.
DR   PDBsum; 6SWH; -.
DR   PDBsum; 6Y7S; -.
DR   AlphaFoldDB; P04128; -.
DR   BMRB; P04128; -.
DR   SMR; P04128; -.
DR   BioGRID; 4262746; 9.
DR   DIP; DIP-9609N; -.
DR   IntAct; P04128; 2.
DR   STRING; 511145.b4314; -.
DR   jPOST; P04128; -.
DR   PaxDb; P04128; -.
DR   PRIDE; P04128; -.
DR   EnsemblBacteria; AAC77270; AAC77270; b4314.
DR   EnsemblBacteria; BAE78307; BAE78307; BAE78307.
DR   GeneID; 948838; -.
DR   KEGG; ecj:JW4277; -.
DR   KEGG; eco:b4314; -.
DR   PATRIC; fig|1411691.4.peg.2378; -.
DR   EchoBASE; EB0304; -.
DR   eggNOG; COG3539; Bacteria.
DR   HOGENOM; CLU_088965_0_0_6; -.
DR   InParanoid; P04128; -.
DR   OMA; QLNDCDS; -.
DR   PhylomeDB; P04128; -.
DR   BioCyc; EcoCyc:EG10308-MON; -.
DR   EvolutionaryTrace; P04128; -.
DR   PRO; PR:P04128; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0009289; C:pilus; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0007155; P:cell adhesion; IDA:EcoCyc.
DR   GO; GO:0043709; P:cell adhesion involved in single-species biofilm formation; IBA:GO_Central.
DR   Gene3D; 2.60.40.1090; -; 1.
DR   InterPro; IPR000259; Adhesion_dom_fimbrial.
DR   InterPro; IPR036937; Adhesion_dom_fimbrial_sf.
DR   InterPro; IPR008966; Adhesion_dom_sf.
DR   Pfam; PF00419; Fimbrial; 1.
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   CHAIN           24..182
FT                   /note="Type-1 fimbrial protein, A chain"
FT                   /id="PRO_0000009170"
FT   DISULFID        44..84
FT                   /evidence="ECO:0000305"
FT   CONFLICT        20
FT                   /note="A -> T (in Ref. 1; AAA24389)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        163
FT                   /note="Missing (in Ref. 2; CAA25489)"
FT                   /evidence="ECO:0000305"
FT   STRAND          31..37
FT                   /evidence="ECO:0007829|PDB:5NKT"
FT   STRAND          42..46
FT                   /evidence="ECO:0007829|PDB:5NKT"
FT   TURN            48..51
FT                   /evidence="ECO:0007829|PDB:5NKT"
FT   STRAND          52..58
FT                   /evidence="ECO:0007829|PDB:5NKT"
FT   STRAND          59..61
FT                   /evidence="ECO:0007829|PDB:6S09"
FT   HELIX           62..65
FT                   /evidence="ECO:0007829|PDB:5NKT"
FT   STRAND          67..71
FT                   /evidence="ECO:0007829|PDB:4DWH"
FT   STRAND          75..84
FT                   /evidence="ECO:0007829|PDB:5NKT"
FT   TURN            86..88
FT                   /evidence="ECO:0007829|PDB:5NKT"
FT   STRAND          90..97
FT                   /evidence="ECO:0007829|PDB:5NKT"
FT   STRAND          100..102
FT                   /evidence="ECO:0007829|PDB:5NKT"
FT   STRAND          105..109
FT                   /evidence="ECO:0007829|PDB:6S09"
FT   TURN            115..117
FT                   /evidence="ECO:0007829|PDB:6Y7S"
FT   STRAND          120..127
FT                   /evidence="ECO:0007829|PDB:5NKT"
FT   STRAND          131..134
FT                   /evidence="ECO:0007829|PDB:2N7H"
FT   STRAND          137..141
FT                   /evidence="ECO:0007829|PDB:5NKT"
FT   STRAND          149..167
FT                   /evidence="ECO:0007829|PDB:5NKT"
FT   STRAND          168..170
FT                   /evidence="ECO:0007829|PDB:6SWH"
FT   STRAND          172..181
FT                   /evidence="ECO:0007829|PDB:5NKT"
SQ   SEQUENCE   182 AA;  18111 MW;  35B2016BDD21A2C1 CRC64;
     MKIKTLAIVV LSALSLSSTA ALAAATTVNG GTVHFKGEVV NAACAVDAGS VDQTVQLGQV
     RTASLAQEGA TSSAVGFNIQ LNDCDTNVAS KAAVAFLGTA IDAGHTNVLA LQSSAAGSAT
     NVGVQILDRT GAALTLDGAT FSSETTLNNG TNTIPFQARY FATGAATPGA ANADATFKVQ
     YQ
 
 
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