ID   FIMH_SALTY              Reviewed;         335 AA.
AC   P37925;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2002, sequence version 2.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Type 1 fimbrin D-mannose specific adhesin;
DE   AltName: Full=Protein FimH;
DE   Flags: Precursor;
GN   Name=fimH; OrderedLocusNames=STM0547;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Swenson D.L., Clegg S.;
RL   Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
CC   -!- FUNCTION: Involved in regulation of length and mediation of adhesion of
CC       type 1 fimbriae (but not necessary for the production of fimbriae). A
CC       mannose-binding adhesin (By similarity).
CC       {ECO:0000250|UniProtKB:P08191}.
CC   -!- SUBCELLULAR LOCATION: Fimbrium {ECO:0000250|UniProtKB:P08191}.
CC   -!- SIMILARITY: Belongs to the fimbrial protein family. {ECO:0000305}.
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DR   EMBL; L19338; AAA75420.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL19501.1; -; Genomic_DNA.
DR   RefSeq; NP_459542.1; NC_003197.2.
DR   RefSeq; WP_000708653.1; NC_003197.2.
DR   AlphaFoldDB; P37925; -.
DR   SMR; P37925; -.
DR   STRING; 99287.STM0547; -.
DR   PaxDb; P37925; -.
DR   DNASU; 1252067; -.
DR   EnsemblBacteria; AAL19501; AAL19501; STM0547.
DR   GeneID; 1252067; -.
DR   KEGG; stm:STM0547; -.
DR   PATRIC; fig|99287.12.peg.580; -.
DR   HOGENOM; CLU_066608_1_0_6; -.
DR   OMA; IKCTNVE; -.
DR   PhylomeDB; P37925; -.
DR   BioCyc; SENT99287:STM0547-MON; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0009289; C:pilus; IBA:GO_Central.
DR   GO; GO:0043709; P:cell adhesion involved in single-species biofilm formation; IBA:GO_Central.
DR   Gene3D; 2.60.40.1090; -; 1.
DR   InterPro; IPR000259; Adhesion_dom_fimbrial.
DR   InterPro; IPR036937; Adhesion_dom_fimbrial_sf.
DR   InterPro; IPR008966; Adhesion_dom_sf.
DR   Pfam; PF00419; Fimbrial; 1.
DR   SUPFAM; SSF49401; SSF49401; 1.
PE   3: Inferred from homology;
KW   Fimbrium; Reference proteome; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..335
FT                   /note="Type 1 fimbrin D-mannose specific adhesin"
FT                   /id="PRO_0000009213"
FT   CONFLICT        61
FT                   /note="G -> A (in Ref. 1; AAA75420)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        118
FT                   /note="F -> S (in Ref. 1; AAA75420)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   335 AA;  36102 MW;  31EE8222C041D61D CRC64;
     MKIYSALLLA GTALFFTHPA LATVCRNSNG TATDIFYDLS DVFTSGNNQP GQVVTLPEKS
     GWVGVNATCP AGTTVNYTYR SYVSELPVQS TEGNFKYLKL NDYLLGAMSI TDSVAGVFYP
     PRNYILMGVD YNVSQQKPFG VQDSKLVFKL KVIRPFINMV TIPRQTMFTV YVTTSTGDAL
     STPVYTISYS GKVEVPQNCE VNAGQVVEFD FGDIGASLFS QAGAGNRPQG VTPQTKTIAI
     KCTNVAAQAY LSMRLEAEKA SGQAMVSDNP DLGFVVANSN GTPLTPNNLS SKIPFHLDDN
     AAARVGIRAW PISVTGIKPA EGPFTARGYL RVDYD