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Protein

Protein FimG

Gene

fimG

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Involved in regulation of length and mediation of adhesion of type 1 fimbriae (but not necessary for the production of fimbriae). Involved in the integration of FimH in the fimbriae.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei166 – 1661Required for stability and transportBy similarity

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

BioCyciEcoCyc:EG10314-MONOMER.
ECOL316407:JW4282-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein FimG
Gene namesi
Name:fimG
Ordered Locus Names:b4319, JW4282
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10314. fimG.

Subcellular locationi

GO - Cellular componenti

  • pilus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Fimbrium

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence analysisAdd
BLAST
Chaini24 – 167144Protein FimGPRO_0000009210Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi39 ↔ 77Curated

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP08190.

Interactioni

Protein-protein interaction databases

BioGridi4262750. 9 interactions.
DIPiDIP-9615N.
IntActiP08190. 1 interaction.
STRINGi511145.b4319.

Structurei

Secondary structure

1
167
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi26 – 349Combined sources
Beta strandi40 – 423Combined sources
Beta strandi44 – 5411Combined sources
Helixi56 – 583Combined sources
Beta strandi68 – 758Combined sources
Beta strandi83 – 897Combined sources
Beta strandi96 – 994Combined sources
Beta strandi108 – 1136Combined sources
Beta strandi114 – 1163Combined sources
Beta strandi124 – 1285Combined sources
Turni131 – 1344Combined sources
Beta strandi135 – 14511Combined sources
Beta strandi147 – 1493Combined sources
Beta strandi153 – 16715Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BFQX-ray1.34G36-167[»]
3BFWX-ray1.80A/C36-167[»]
3JWNX-ray2.69G/M24-167[»]
4J3OX-ray3.80G24-167[»]
4XO9X-ray1.14B24-37[»]
4XOAX-ray2.54B/D/F/H24-37[»]
4XODX-ray1.14B24-37[»]
ProteinModelPortaliP08190.
SMRiP08190. Positions 24-167.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08190.

Family & Domainsi

Sequence similaritiesi

Belongs to the fimbrial protein family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4108T65. Bacteria.
ENOG4111FMS. LUCA.
HOGENOMiHOG000260127.
InParanoidiP08190.
KOiK07349.
OMAiFTHEAKF.
OrthoDBiEOG6QP11B.
PhylomeDBiP08190.

Family and domain databases

Gene3Di2.60.40.1090. 1 hit.
InterProiIPR008966. Adhesion_dom.
IPR000259. Adhesion_dom_fimbrial.
[Graphical view]
SUPFAMiSSF49401. SSF49401. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P08190-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKWCKRGYVL AAILALASAT IQAADVTITV NGKVVAKPCT VSTTNATVDL
60 70 80 90 100
GDLYSFSLMS AGAASAWHDV ALELTNCPVG TSRVTASFSG AADSTGYYKN
110 120 130 140 150
QGTAQNIQLE LQDDSGNTLN TGATKTVQVD DSSQSAHFPL QVRALTVNGG
160
ATQGTIQAVI SITYTYS
Length:167
Mass (Da):17,317
Last modified:February 1, 1995 - v2
Checksum:i8C3EF95FD442E22C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti61 – 611A → S in CAA29155 (PubMed:2890081).Curated
Sequence conflicti148 – 1492NG → KV in CAA29155 (PubMed:2890081).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05672 Genomic DNA. Translation: CAA29155.1.
U14003 Genomic DNA. Translation: AAA97215.1.
U00096 Genomic DNA. Translation: AAC77275.1.
AP009048 Genomic DNA. Translation: BAE78312.1.
PIRiS56544.
RefSeqiNP_418739.1. NC_000913.3.
WP_000870592.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC77275; AAC77275; b4319.
BAE78312; BAE78312; BAE78312.
GeneIDi948846.
KEGGiecj:JW4282.
eco:b4319.
PATRICi32124234. VBIEscCol129921_4460.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05672 Genomic DNA. Translation: CAA29155.1.
U14003 Genomic DNA. Translation: AAA97215.1.
U00096 Genomic DNA. Translation: AAC77275.1.
AP009048 Genomic DNA. Translation: BAE78312.1.
PIRiS56544.
RefSeqiNP_418739.1. NC_000913.3.
WP_000870592.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BFQX-ray1.34G36-167[»]
3BFWX-ray1.80A/C36-167[»]
3JWNX-ray2.69G/M24-167[»]
4J3OX-ray3.80G24-167[»]
4XO9X-ray1.14B24-37[»]
4XOAX-ray2.54B/D/F/H24-37[»]
4XODX-ray1.14B24-37[»]
ProteinModelPortaliP08190.
SMRiP08190. Positions 24-167.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262750. 9 interactions.
DIPiDIP-9615N.
IntActiP08190. 1 interaction.
STRINGi511145.b4319.

Proteomic databases

PaxDbiP08190.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77275; AAC77275; b4319.
BAE78312; BAE78312; BAE78312.
GeneIDi948846.
KEGGiecj:JW4282.
eco:b4319.
PATRICi32124234. VBIEscCol129921_4460.

Organism-specific databases

EchoBASEiEB0310.
EcoGeneiEG10314. fimG.

Phylogenomic databases

eggNOGiENOG4108T65. Bacteria.
ENOG4111FMS. LUCA.
HOGENOMiHOG000260127.
InParanoidiP08190.
KOiK07349.
OMAiFTHEAKF.
OrthoDBiEOG6QP11B.
PhylomeDBiP08190.

Enzyme and pathway databases

BioCyciEcoCyc:EG10314-MONOMER.
ECOL316407:JW4282-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP08190.
PROiP08190.

Family and domain databases

Gene3Di2.60.40.1090. 1 hit.
InterProiIPR008966. Adhesion_dom.
IPR000259. Adhesion_dom_fimbrial.
[Graphical view]
SUPFAMiSSF49401. SSF49401. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Three fim genes required for the regulation of length and mediation of adhesion of Escherichia coli type 1 fimbriae."
    Klemm P., Christiansen G.
    Mol. Gen. Genet. 208:439-445(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
    Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
    Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.

Entry informationi

Entry nameiFIMG_ECOLI
AccessioniPrimary (citable) accession number: P08190
Secondary accession number(s): Q2M5Z4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: February 1, 1995
Last modified: May 11, 2016
This is version 121 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.