ID B7MML0_ECO45 Unreviewed; 300 AA.
AC B7MML0;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Minor component of type 1 fimbriae {ECO:0000313|EMBL:CAR06082.1};
GN Name=fimH {ECO:0000313|EMBL:CAR06082.1};
GN OrderedLocusNames=ECS88_4938 {ECO:0000313|EMBL:CAR06082.1};
OS Escherichia coli O45:K1 (strain S88 / ExPEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585035 {ECO:0000313|EMBL:CAR06082.1, ECO:0000313|Proteomes:UP000000747};
RN [1] {ECO:0000313|Proteomes:UP000000747}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S88 / ExPEC {ECO:0000313|Proteomes:UP000000747};
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(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; CU928161; CAR06082.1; -; Genomic_DNA.
DR RefSeq; WP_001338195.1; NC_011742.1.
DR AlphaFoldDB; B7MML0; -.
DR KEGG; ecz:ECS88_4938; -.
DR HOGENOM; CLU_080390_0_0_6; -.
DR Proteomes; UP000000747; Chromosome.
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 Reference proteome {ECO:0000313|Proteomes:UP000000747};
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_5002860579"
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; 31501 MW; 158ABC37835CD564 CRC64;
MKRVINLFAI LLMGWSVNAW SFACKTANGT AIPIGGGSAN VYVNLAPAVN VGQNLVVDLS
TQIFCHNDYP ETITDYVTLQ RGSAYGGVLS NFSGTVKYSG SSYPFPTTSE TPRVVYNSRT
DKPWPVALYL TPVSSAGGVV IKAGSLIAVL ILRQTNNYNS DDFQFVWNIY ANNDVVVPTG
GCDVSARDVT VTLPDYPGSV PIPLTVYCAK SQNLGYYLSG TTADAGNSIF TNTASFSPAQ
GVGVQLTRNG TIIPANNTVS LGAVGTSAVS LGLTANYART GGQVTAGNVQ SIIGVTFVYQ
//
