ID Q9S495_ECOLX Unreviewed; 300 AA.
AC Q9S495;
DT 01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=FimH {ECO:0000313|EMBL:AAD44321.1};
GN Name=fimH {ECO:0000313|EMBL:AAD44321.1};
OS Escherichia coli.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562 {ECO:0000313|EMBL:AAD44321.1};
RN [1] {ECO:0000313|EMBL:AAD44321.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=K12 {ECO:0000313|EMBL:AAD44321.1};
RX PubMed=10869080; DOI=10.1128/JB.182.14.4012-4021.2000;
RA Hamrick T.S., Harris S.L., Spears P.A., Havell E.A., Horton J.R.,
RA Russell P.W., Orndorff P.E.;
RT "Genetic characterization of Escherichia coli type 1 pilus adhesin mutants
RT and identification of a novel binding phenotype.";
RL J. Bacteriol. 182:4012-4021(2000).
CC -!- SUBCELLULAR LOCATION: Fimbrium {ECO:0000256|ARBA:ARBA00004561}.
CC -!- SIMILARITY: Belongs to the fimbrial protein family.
CC {ECO:0000256|ARBA:ARBA00006671}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF154927; AAD44321.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9S495; -.
DR GO; GO:0009289; C:pilus; IEA:UniProtKB-SubCell.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR CDD; cd10466; FimH_man-bind; 1.
DR Gene3D; 2.60.40.1090; Fimbrial-type adhesion domain; 2.
DR InterPro; IPR000259; Adhesion_dom_fimbrial.
DR InterPro; IPR036937; Adhesion_dom_fimbrial_sf.
DR InterPro; IPR008966; Adhesion_dom_sf.
DR InterPro; IPR015243; FimH_man-bd.
DR PANTHER; PTHR33420; FIMBRIAL SUBUNIT ELFA-RELATED; 1.
DR PANTHER; PTHR33420:SF11; TYPE 1 FIMBRIN D-MANNOSE SPECIFIC ADHESIN; 1.
DR Pfam; PF00419; Fimbrial; 1.
DR Pfam; PF09160; FimH_man-bind; 1.
DR SUPFAM; SSF49401; Bacterial adhesins; 2.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..300
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004331968"
FT DOMAIN 24..168
FT /note="FimH mannose-binding"
FT /evidence="ECO:0000259|Pfam:PF09160"
FT DOMAIN 178..300
FT /note="Fimbrial-type adhesion"
FT /evidence="ECO:0000259|Pfam:PF00419"
SQ SEQUENCE 300 AA; 31534 MW; 48FFB2795A3CB23D CRC64;
MKRVITLFAV LLMGWSVNAW SFACKTANGT AIPIGGGSAN VYVNLAPVVN VGQNLVVDLS
TQIFYHNDYP ETITDYVTLQ RGSAYGGVLS NFSGTVKYSG SSYPFPTTSE TPRVVYNSRT
DKPWPVALYL TPVSSAGGVA IKAGSLIAVL ILRQTNNYNS DDFQFVWNIY ANNDVVVPTG
GCDVSARDVT VTLPDYPGSV PIPLTVYCAK SQNLGYYLSG TTADAGNSIF TNTASFSPAQ
GVGVQLTRNG TIIPANNTVS LGAVGTSAVS LGLTANYART GGQVTAGNVQ SIIGVTFVYQ
//
