ID   FIMA1_SALTY             Reviewed;         185 AA.
AC   P37921;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2002, sequence version 2.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Type-1 fimbrial protein, A chain;
DE   AltName: Full=Type-1A pilin;
DE   Flags: Precursor;
GN   Name=fimA; OrderedLocusNames=STM0543;
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).
RN   [3]
RP   PROTEIN SEQUENCE OF 23-50.
RC   STRAIN=LT2 / SH6749;
RA   Waalen K., Sletten K., Froeholm L.O., Vaeisaenen V., Korhonen T.K.;
RT   "The N-terminal amino acid sequence of type 1 fimbria (pili) of Salmonella
RT   typhimurium LT2.";
RL   FEMS Microbiol. Lett. 16:149-151(1983).
CC   -!- FUNCTION: Fimbriae (also called pili), polar filaments radiating from
CC       the surface of the bacterium to a length of 0.5-1.5 micrometers and
CC       numbering 100-300 per cell, enable bacteria to colonize the epithelium
CC       of specific host organs.
CC   -!- SUBCELLULAR LOCATION: Fimbrium.
CC   -!- SIMILARITY: Belongs to the fimbrial protein family. {ECO:0000305}.
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DR   EMBL; L19338; AAA75416.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL19497.1; -; Genomic_DNA.
DR   PIR; B28393; B28393.
DR   RefSeq; NP_459538.3; NC_003197.2.
DR   RefSeq; WP_000681030.1; NC_003197.2.
DR   AlphaFoldDB; P37921; -.
DR   SMR; P37921; -.
DR   STRING; 99287.STM0543; -.
DR   PaxDb; P37921; -.
DR   EnsemblBacteria; AAL19497; AAL19497; STM0543.
DR   GeneID; 1252063; -.
DR   KEGG; stm:STM0543; -.
DR   PATRIC; fig|99287.12.peg.576; -.
DR   HOGENOM; CLU_088965_0_0_6; -.
DR   OMA; ATFVMKY; -.
DR   PhylomeDB; P37921; -.
DR   BioCyc; SENT99287:STM0543-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   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Fimbrium; Reference proteome;
KW   Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000269|Ref.3"
FT   CHAIN           23..185
FT                   /note="Type-1 fimbrial protein, A chain"
FT                   /id="PRO_0000009172"
FT   DISULFID        46..86
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2
FT                   /note="K -> R (in Ref. 1; AAA75416)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   185 AA;  18869 MW;  B59249AC43D107B8 CRC64;
     MKHKLMTSTI ASLMFVAGAA VAADPTPVSV SGGTIHFEGK LVNAACAVST KSADQTVTLG
     QYRTASFTAI GNTTAQVPFS IVLNDCDPKV AANAAVAFSG QADNTNPNLL AVSSADNSTT
     ATGVGIEILD NTSSPLKPDG ATFSAKQSLV EGTNTLRFTA RYKATAAATT PGQANADATF
     IMKYE