SFMF_ECOLI
ID SFMF_ECOLI Reviewed; 171 AA.
AC P38052; P75716; P77079; Q2MBP5;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Uncharacterized fimbrial-like protein SfmF;
DE Flags: Precursor;
GN Name=sfmF; Synonyms=ybcG; OrderedLocusNames=b0534, JW5072;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 119-171.
RC STRAIN=K12;
RX PubMed=2183007; DOI=10.1007/bf00260503;
RA Muramatsu S., Mizuno T.;
RT "Nucleotide sequence of the region encompassing the int gene of a cryptic
RT prophage and the DNA Y gene flanked by a curved DNA sequence of Escherichia
RT coli K12.";
RL Mol. Gen. Genet. 220:325-328(1990).
RN [5]
RP IDENTIFICATION.
RX PubMed=7984428; DOI=10.1093/nar/22.22.4756;
RA Borodovsky M., Rudd K.E., Koonin E.V.;
RT "Intrinsic and extrinsic approaches for detecting genes in a bacterial
RT genome.";
RL Nucleic Acids Res. 22:4756-4767(1994).
RN [6]
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: Fimbrium {ECO:0000250}.
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 fimbrial protein family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB40732.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U82598; AAB40732.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC73636.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76311.1; -; Genomic_DNA.
DR EMBL; X51662; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; E64785; E64785.
DR RefSeq; NP_415067.1; NC_000913.3.
DR RefSeq; WP_001255230.1; NZ_SSZK01000024.1.
DR AlphaFoldDB; P38052; -.
DR SMR; P38052; -.
DR BioGRID; 4263147; 12.
DR STRING; 511145.b0534; -.
DR PaxDb; P38052; -.
DR EnsemblBacteria; AAC73636; AAC73636; b0534.
DR EnsemblBacteria; BAE76311; BAE76311; BAE76311.
DR GeneID; 944977; -.
DR KEGG; ecj:JW5072; -.
DR KEGG; eco:b0534; -.
DR PATRIC; fig|1411691.4.peg.1744; -.
DR EchoBASE; EB2289; -.
DR eggNOG; COG3539; Bacteria.
DR HOGENOM; CLU_088965_0_2_6; -.
DR InParanoid; P38052; -.
DR OMA; ATFMINY; -.
DR PhylomeDB; P38052; -.
DR BioCyc; EcoCyc:EG12388-MON; -.
DR PRO; PR:P38052; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009289; C:pilus; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IMP:EcoCyc.
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 2: Evidence at transcript level;
KW Disulfide bond; Fimbrium; Reference proteome; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..171
FT /note="Uncharacterized fimbrial-like protein SfmF"
FT /id="PRO_0000009208"
FT DISULFID 40..80
FT /evidence="ECO:0000255"
SQ SEQUENCE 171 AA; 18223 MW; 59230981242A1DCA CRC64;
MRRVLFSCFC GLLWSSSGWA VDPLGTININ LHGNVVDFSC TVNTADIDKT VDLGRWPTTQ
LLNAGDTTAL VPFSLRLEGC PPGSVAILFT GTPASDTNLL ALDDPAMAQT VAIELRNSDR
SRLALGEASP TEEVDANGNV TLNFFANYRA LASGVRPGVA KADAIFMINY N
