ID   FIMC_SALTY              Reviewed;         230 AA.
AC   P37923;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Chaperone protein FimC;
DE   Flags: Precursor;
GN   Name=fimC; OrderedLocusNames=STM0545;
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: Required for the biogenesis of type 1 fimbriae. Binds and
CC       interact with FimH.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the periplasmic pilus chaperone family.
CC       {ECO:0000305}.
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DR   EMBL; L19338; AAA75418.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL19499.1; -; Genomic_DNA.
DR   RefSeq; NP_459540.1; NC_003197.2.
DR   RefSeq; WP_000935025.1; NC_003197.2.
DR   AlphaFoldDB; P37923; -.
DR   SMR; P37923; -.
DR   STRING; 99287.STM0545; -.
DR   PaxDb; P37923; -.
DR   EnsemblBacteria; AAL19499; AAL19499; STM0545.
DR   GeneID; 1252065; -.
DR   KEGG; stm:STM0545; -.
DR   PATRIC; fig|99287.12.peg.578; -.
DR   HOGENOM; CLU_070768_2_1_6; -.
DR   OMA; YLINAWI; -.
DR   PhylomeDB; P37923; -.
DR   BioCyc; SENT99287:STM0545-MON; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:InterPro.
DR   GO; GO:0061077; P:chaperone-mediated protein folding; IEA:InterPro.
DR   Gene3D; 2.60.40.10; -; 2.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR008962; PapD-like_sf.
DR   InterPro; IPR036316; Pili_assmbl_chap_C_dom_sf.
DR   InterPro; IPR001829; Pili_assmbl_chaperone_bac.
DR   InterPro; IPR016148; Pili_assmbl_chaperone_C.
DR   InterPro; IPR018046; Pili_assmbl_chaperone_CS.
DR   InterPro; IPR016147; Pili_assmbl_chaperone_N.
DR   Pfam; PF02753; PapD_C; 1.
DR   Pfam; PF00345; PapD_N; 1.
DR   PRINTS; PR00969; CHAPERONPILI.
DR   SUPFAM; SSF49354; SSF49354; 1.
DR   SUPFAM; SSF49584; SSF49584; 1.
DR   PROSITE; PS00635; PILI_CHAPERONE; 1.
PE   3: Inferred from homology;
KW   Chaperone; Fimbrium biogenesis; Immunoglobulin domain; Periplasm;
KW   Reference proteome; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..230
FT                   /note="Chaperone protein FimC"
FT                   /id="PRO_0000009276"
SQ   SEQUENCE   230 AA;  24868 MW;  9CC193826E92A712 CRC64;
     MLNSIKVGFI VLLTLFTSLN VQAAGGIALG ATRVIYPSAA KQTSLAISNS DTQERYLVNS
     WIENNAGQKE KTFIVTPPLF VSEPKSENTL RIIYAGQPLP GDRESLFWMN VKAIPSVDKS
     HIEGKNVLQL AILSRIKLFV RPANLPQTPE DAPTLLKFSR VGNHLKITNP SAYYLTLVNI
     SVGAKKIDNV MIAPKSDMQI PLPTGAQGNV TFQSVNDYGA LTSATTASLG