SFMC_ECOLI
ID SFMC_ECOLI Reviewed; 230 AA.
AC P77249; P77077; Q2MBP8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Probable fimbrial chaperone SfmC;
DE Flags: Precursor;
GN Name=sfmC; OrderedLocusNames=b0531, JW0520;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
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 [4]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=20345943; DOI=10.1111/j.1462-2920.2010.02202.x;
RA Korea C.G., Badouraly R., Prevost M.C., Ghigo J.M., Beloin C.;
RT "Escherichia coli K-12 possesses multiple cryptic but functional chaperone-
RT usher fimbriae with distinct surface specificities.";
RL Environ. Microbiol. 12:1957-1977(2010).
CC -!- FUNCTION: Part of the sfmACDHF fimbrial operon. Could contribute to
CC adhesion to various surfaces in specific environmental niches.
CC Increases adhesion to eukaryotic T24 bladder epithelial cells in the
CC absence of fim genes. {ECO:0000269|PubMed:20345943}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CC -!- INDUCTION: Expression is negatively regulated by H-NS and subjected to
CC cAMP receptor protein (CRP)-mediated catabolite repression.
CC {ECO:0000269|PubMed:20345943}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the operon under classical laboratory
CC conditions does not result in any major effect on E.coli capacity to
CC form biofilms compared with the wild-type strain.
CC {ECO:0000269|PubMed:20345943}.
CC -!- MISCELLANEOUS: The operon is cryptic under classical laboratory
CC conditions, but is functional when constitutively expressed.
CC {ECO:0000305|PubMed:20345943}.
CC -!- SIMILARITY: Belongs to the periplasmic pilus chaperone family.
CC {ECO:0000305}.
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DR EMBL; U82664; AAB40284.1; -; Genomic_DNA.
DR EMBL; U82598; AAB40729.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73633.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76308.1; -; Genomic_DNA.
DR PIR; B64785; B64785.
DR RefSeq; NP_415064.1; NC_000913.3.
DR RefSeq; WP_000988364.1; NZ_SSZK01000024.1.
DR AlphaFoldDB; P77249; -.
DR SMR; P77249; -.
DR BioGRID; 4263219; 114.
DR IntAct; P77249; 3.
DR STRING; 511145.b0531; -.
DR PaxDb; P77249; -.
DR PRIDE; P77249; -.
DR EnsemblBacteria; AAC73633; AAC73633; b0531.
DR EnsemblBacteria; BAE76308; BAE76308; BAE76308.
DR GeneID; 945367; -.
DR KEGG; ecj:JW0520; -.
DR KEGG; eco:b0531; -.
DR PATRIC; fig|1411691.4.peg.1747; -.
DR EchoBASE; EB3641; -.
DR eggNOG; COG3121; Bacteria.
DR HOGENOM; CLU_070768_2_1_6; -.
DR OMA; YLINAWI; -.
DR PhylomeDB; P77249; -.
DR BioCyc; EcoCyc:G6291-MON; -.
DR PRO; PR:P77249; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; 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 2: Evidence at transcript level;
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="Probable fimbrial chaperone SfmC"
FT /id="PRO_0000009275"
SQ SEQUENCE 230 AA; 25458 MW; D9B0CEEBB66C10D3 CRC64;
MMTKIKLLML IIFYLIISAS AHAAGGIALG ATRIIYPADA KQTAVWIRNS HTNERFLVNS
WIENSSGVKE KSFIITPPLF VSEPKSENTL RIIYTGPPLA ADRESLFWMN VKTIPSVDKN
ALNGRNVLQL AILSRMKLFL RPIQLQELPA EAPDTLKFSR SGNYINVHNP SPFYVTLVNL
QVGSQKLGNA MAAPRVNSQI PLPSGVQGKL KFQTVNDYGS VTPVREVNLN
