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Database: UniProt
Entry: D2SWN1_ECOLX
LinkDB: D2SWN1_ECOLX
Original site: D2SWN1_ECOLX 
ID   D2SWN1_ECOLX            Unreviewed;       300 AA.
AC   D2SWN1;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Type 1 fimbrial adhesin {ECO:0000313|EMBL:ACZ17766.1};
DE   Flags: Fragment;
GN   Name=fimH {ECO:0000313|EMBL:ACZ17766.1};
OS   Escherichia coli NU14.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=569579 {ECO:0000313|EMBL:ACZ17766.1};
RN   [1] {ECO:0000313|EMBL:ACZ17766.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NU14 {ECO:0000313|EMBL:ACZ17766.1};
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; FJ865715; ACZ17766.1; -; Genomic_DNA.
DR   RefSeq; WP_000832214.1; NZ_CP019777.1.
DR   AlphaFoldDB; D2SWN1; -.
DR   SMR; D2SWN1; -.
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_5030168041"
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:ACZ17766.1"
SQ   SEQUENCE   300 AA;  31429 MW;  D789457A5F5255AE CRC64;
     MKRVITLFAV LLMGWSVNAW SFACKTANGT AIPIGGGSAN VYVNLAPAVN VGQNLVVDLS
     TQIFCHNDYP ETITDYVTLQ RGAAYGGVLS SFSGTVKYNG SSYPFPTTSE TPRVVYNSRT
     DKPWPVALYL TPVSSAGGVA IKAGSLIAVL ILRQTNNYNS DDFQFVWNIY ANNDVVVPTG
     GCDVSARDVT VTLPDYPGSV PIPLTVYCAK SQNLGYYLSG TTADAGNSIF TNTASFSPAQ
     GVGVQLTRNG TIIPANNTVS LGAVGTSAVS LGLTANYART GGQVTAGNVQ SIIGVTFVYQ
//
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