ID D2SWA2_ECOLX Unreviewed; 300 AA.
AC D2SWA2;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Type 1 fimbrial adhesin {ECO:0000313|EMBL:ACZ17637.1};
DE Flags: Fragment;
GN Name=fimH {ECO:0000313|EMBL:ACZ17637.1};
OS Escherichia coli.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562 {ECO:0000313|EMBL:ACZ17637.1};
RN [1] {ECO:0000313|EMBL:ACZ17637.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ASB941 {ECO:0000313|EMBL:ACZ17637.1}, ASB950
RC {ECO:0000313|EMBL:ACZ17666.1}, ASB951 {ECO:0000313|EMBL:ACZ17712.1},
RC and ECOR11 {ECO:0000313|EMBL:ACZ17727.1};
RX PubMed=20018753; DOI=10.1073/pnas.0902179106;
RA Chen S.L., Hung C.S., Pinkner J.S., Walker J.N., Cusumano C.K., Li Z.,
RA Bouckaert J., Gordon J.I., Hultgren S.J.;
RT "Positive selection identifies an in vivo role for FimH during urinary
RT tract infection in addition to mannose binding.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:22439-22444(2009).
CC -!- SUBCELLULAR LOCATION: Fimbrium {ECO:0000256|ARBA:ARBA00004561}.
CC -!- SIMILARITY: Belongs to the fimbrial protein family.
CC {ECO:0000256|ARBA:ARBA00006671}.
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DR EMBL; FJ865586; ACZ17637.1; -; Genomic_DNA.
DR EMBL; FJ865615; ACZ17666.1; -; Genomic_DNA.
DR EMBL; FJ865661; ACZ17712.1; -; Genomic_DNA.
DR EMBL; FJ865676; ACZ17727.1; -; Genomic_DNA.
DR RefSeq; WP_001702522.1; NZ_WNUB01000033.1.
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_5011937156"
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"
FT NON_TER 300
FT /evidence="ECO:0000313|EMBL:ACZ17637.1"
SQ SEQUENCE 300 AA; 31573 MW; 82920802D08FAF0D CRC64;
MKRVITLFAV LLMGWSVNAW SFACKTANGT AIPIGGGSAN VYVNLAPVVN VGQNLVVDLS
TQIFCHNDYP ETITDYVTLQ RGSAYGGVLS NFSGTVKYSG SSYPFPTTSE TPRVVYNSRT
DKPWPVALYL TPVSSAGRVA IKAGSLIAVL ILRQTNNYNS DDFQFVWNIY ANNDVVVPTG
GCDVSARDVT VTLPDYPGSV PIPLTVYCAK SQNLGYYLSG TTADAGNSIF TNTASFSPAQ
GVGVQLTRNG TIIPANNTVS LGAVGTSAVS LGLTANYART GGQVTAGNVQ SIIGVTFVYQ
//
