FIMC_ECOLI
ID FIMC_ECOLI Reviewed; 241 AA.
AC P31697; P71220; Q2M5Z7;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 3.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Chaperone protein FimC;
DE Flags: Precursor;
GN Name=fimC; OrderedLocusNames=b4316, JW4279;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 37-51.
RC STRAIN=K12;
RX PubMed=1363735; DOI=10.1016/0923-2508(92)90070-5;
RA Klemm P.;
RT "FimC, a chaperone-like periplasmic protein of Escherichia coli involved in
RT biogenesis of type 1 fimbriae.";
RL Res. Microbiol. 143:831-838(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Clinical isolate 149;
RX PubMed=8104335; DOI=10.1073/pnas.90.18.8397;
RA Jones C.H., Pinkner J.S., Nicholes A.V., Slonim L.N., Abraham S.N.,
RA Hultgren S.J.;
RT "FimC is a periplasmic PapD-like chaperone that directs assembly of type 1
RT pili in bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:8397-8401(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=O2:K1:H+ / MT78;
RX PubMed=8636962; DOI=10.1099/00222615-44-6-444;
RA Marc D., Dho-Moulin M.;
RT "Analysis of the fim cluster of an avian O2 strain of Escherichia coli:
RT serogroup-specific sites within fimA and nucleotide sequence of fimI.";
RL J. Med. Microbiol. 44:444-452(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [7]
RP STRUCTURE BY NMR.
RX PubMed=9783748; DOI=10.1038/2325;
RA Pellecchia M., Guntert P., Glockshuber R., Wuethrich K.;
RT "NMR solution structure of the periplasmic chaperone FimC.";
RL Nat. Struct. Biol. 5:885-890(1998).
CC -!- FUNCTION: Required for the biogenesis of type 1 fimbriae. Binds and
CC interact with FimH.
CC -!- INTERACTION:
CC P31697; P30130: fimD; NbExp=11; IntAct=EBI-1028005, EBI-554889;
CC P31697; P08190: fimG; NbExp=5; IntAct=EBI-1028005, EBI-1785843;
CC P31697; P08191: fimH; NbExp=11; IntAct=EBI-1028005, EBI-1028015;
CC P31697; Q83UM2: fimA; Xeno; NbExp=2; IntAct=EBI-1028005, EBI-8548126;
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- SIMILARITY: Belongs to the periplasmic pilus chaperone family.
CC {ECO:0000305}.
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DR EMBL; X51655; CAA35967.1; -; Genomic_DNA.
DR EMBL; L14598; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z37500; CAA85729.1; -; Genomic_DNA.
DR EMBL; U14003; AAA97212.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77272.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78309.1; -; Genomic_DNA.
DR PIR; S56541; S56541.
DR RefSeq; NP_418736.3; NC_000913.3.
DR RefSeq; WP_000066547.1; NZ_LN832404.1.
DR PDB; 1BF8; NMR; -; A=37-241.
DR PDB; 1KIU; X-ray; 3.00 A; A/C/E/G/I/K/M/O=37-241.
DR PDB; 1KLF; X-ray; 2.79 A; A/C/E/G/I/K/M/O=37-241.
DR PDB; 1QUN; X-ray; 2.80 A; A/C/E/G/I/K/M/O=37-241.
DR PDB; 1ZE3; X-ray; 1.84 A; C=37-241.
DR PDB; 3BWU; X-ray; 1.76 A; C=37-241.
DR PDB; 3JWN; X-ray; 2.69 A; C/I=37-241.
DR PDB; 3RFZ; X-ray; 2.80 A; C/F=37-241.
DR PDB; 3SQB; X-ray; 3.20 A; A/C/E/G=37-241.
DR PDB; 4DWH; X-ray; 2.50 A; A/C=37-241.
DR PDB; 4J3O; X-ray; 3.80 A; C=37-241.
DR PDB; 6E14; EM; 4.00 A; C=1-241.
DR PDB; 6E15; EM; 6.20 A; C=1-241.
DR PDB; 6SWH; X-ray; 2.80 A; A/D=37-241.
DR PDB; 7B0W; X-ray; 1.75 A; C=37-241.
DR PDB; 7B0X; X-ray; 1.70 A; C=37-241.
DR PDB; 7SZO; X-ray; 2.80 A; C/I=37-241.
DR PDBsum; 1BF8; -.
DR PDBsum; 1KIU; -.
DR PDBsum; 1KLF; -.
DR PDBsum; 1QUN; -.
DR PDBsum; 1ZE3; -.
DR PDBsum; 3BWU; -.
DR PDBsum; 3JWN; -.
DR PDBsum; 3RFZ; -.
DR PDBsum; 3SQB; -.
DR PDBsum; 4DWH; -.
DR PDBsum; 4J3O; -.
DR PDBsum; 6E14; -.
DR PDBsum; 6E15; -.
DR PDBsum; 6SWH; -.
DR PDBsum; 7B0W; -.
DR PDBsum; 7B0X; -.
DR PDBsum; 7SZO; -.
DR AlphaFoldDB; P31697; -.
DR BMRB; P31697; -.
DR SMR; P31697; -.
DR BioGRID; 4262754; 253.
DR DIP; DIP-9611N; -.
DR IntAct; P31697; 8.
DR MINT; P31697; -.
DR STRING; 511145.b4316; -.
DR UniLectin; P31697; -.
DR jPOST; P31697; -.
DR PaxDb; P31697; -.
DR PRIDE; P31697; -.
DR EnsemblBacteria; AAC77272; AAC77272; b4316.
DR EnsemblBacteria; BAE78309; BAE78309; BAE78309.
DR GeneID; 948843; -.
DR KEGG; ecj:JW4279; -.
DR KEGG; eco:b4316; -.
DR PATRIC; fig|1411691.4.peg.2376; -.
DR EchoBASE; EB0306; -.
DR eggNOG; COG3121; Bacteria.
DR HOGENOM; CLU_070768_2_1_6; -.
DR InParanoid; P31697; -.
DR OMA; LFAMQGK; -.
DR PhylomeDB; P31697; -.
DR BioCyc; EcoCyc:EG10310-MON; -.
DR EvolutionaryTrace; P31697; -.
DR PRO; PR:P31697; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0044183; F:protein folding chaperone; IDA:EcoCyc.
DR GO; GO:0071555; P:cell wall organization; IEA:InterPro.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IDA:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Chaperone; Direct protein sequencing; Fimbrium biogenesis;
KW Immunoglobulin domain; Periplasm; Reference proteome; Signal.
FT SIGNAL 1..36
FT /evidence="ECO:0000269|PubMed:1363735"
FT CHAIN 37..241
FT /note="Chaperone protein FimC"
FT /id="PRO_0000009273"
FT VARIANT 29
FT /note="M -> V (in strain: Clinical isolate 149 and O2:K1:H+
FT / MT78)"
FT VARIANT 54
FT /note="E -> V (in strain: Clinical isolate 149 and O2:K1:H+
FT / MT78)"
FT VARIANT 210
FT /note="T -> A (in strain: Clinical isolate 149 and O2:K1:H+
FT / MT78)"
FT CONFLICT 81
FT /note="D -> G (in Ref. 1; CAA35967)"
FT /evidence="ECO:0000305"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:7B0X"
FT STRAND 43..48
FT /evidence="ECO:0007829|PDB:7B0X"
FT STRAND 52..60
FT /evidence="ECO:0007829|PDB:7B0X"
FT STRAND 66..74
FT /evidence="ECO:0007829|PDB:7B0X"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:1BF8"
FT STRAND 84..105
FT /evidence="ECO:0007829|PDB:7B0X"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:7B0X"
FT STRAND 117..127
FT /evidence="ECO:0007829|PDB:7B0X"
FT HELIX 131..135
FT /evidence="ECO:0007829|PDB:7B0X"
FT STRAND 138..152
FT /evidence="ECO:0007829|PDB:7B0X"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:1BF8"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:7B0X"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:7B0X"
FT STRAND 168..171
FT /evidence="ECO:0007829|PDB:7B0X"
FT STRAND 173..180
FT /evidence="ECO:0007829|PDB:7B0X"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:7B0X"
FT STRAND 186..193
FT /evidence="ECO:0007829|PDB:7B0X"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:1KIU"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:7B0X"
FT STRAND 207..212
FT /evidence="ECO:0007829|PDB:7B0X"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:3JWN"
FT STRAND 221..226
FT /evidence="ECO:0007829|PDB:7B0X"
FT STRAND 236..239
FT /evidence="ECO:0007829|PDB:4DWH"
SQ SEQUENCE 241 AA; 26689 MW; B1AD63C33C8FACB4 CRC64;
MSNKNVNVRK SQEITFCLLA GILMFMAMMV AGRAEAGVAL GATRVIYPAG QKQEQLAVTN
NDENSTYLIQ SWVENADGVK DGRFIVTPPL FAMKGKKENT LRILDATNNQ LPQDRESLFW
MNVKAIPSMD KSKLTENTLQ LAIISRIKLY YRPAKLALPP DQAAEKLRFR RSANSLTLIN
PTPYYLTVTE LNAGTRVLEN ALVPPMGEST VKLPSDAGSN ITYRTINDYG ALTPKMTGVM
E
