SFMD_ECOLI
ID SFMD_ECOLI Reviewed; 867 AA.
AC P77468; P77133; Q2MBP7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Outer membrane usher protein SfmD;
DE Flags: Precursor;
GN Name=sfmD; OrderedLocusNames=b0532, JW0521;
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. Probably involved in the export and assembly of
CC fimbrial subunits across the outer membrane.
CC {ECO:0000269|PubMed:20345943}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250}; Multi-pass
CC membrane protein {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 export usher family. {ECO:0000305}.
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DR EMBL; U82598; AAB40730.1; -; Genomic_DNA.
DR EMBL; U82664; AAB40285.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73634.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76309.1; -; Genomic_DNA.
DR PIR; C64785; C64785.
DR RefSeq; NP_415065.1; NC_000913.3.
DR RefSeq; WP_001333622.1; NZ_SSZK01000024.1.
DR AlphaFoldDB; P77468; -.
DR SMR; P77468; -.
DR BioGRID; 4263216; 173.
DR IntAct; P77468; 2.
DR STRING; 511145.b0532; -.
DR PaxDb; P77468; -.
DR PRIDE; P77468; -.
DR EnsemblBacteria; AAC73634; AAC73634; b0532.
DR EnsemblBacteria; BAE76309; BAE76309; BAE76309.
DR GeneID; 945160; -.
DR KEGG; ecj:JW0521; -.
DR KEGG; eco:b0532; -.
DR PATRIC; fig|1411691.4.peg.1746; -.
DR EchoBASE; EB3642; -.
DR eggNOG; COG3188; Bacteria.
DR HOGENOM; CLU_009120_3_1_6; -.
DR InParanoid; P77468; -.
DR OMA; GELLIQW; -.
DR PhylomeDB; P77468; -.
DR BioCyc; EcoCyc:G6292-MON; -.
DR PRO; PR:P77468; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015473; F:fimbrial usher porin activity; IBA:GO_Central.
DR GO; GO:0009297; P:pilus assembly; IBA:GO_Central.
DR Gene3D; 2.60.40.2070; -; 1.
DR Gene3D; 2.60.40.2610; -; 1.
DR Gene3D; 3.10.20.410; -; 1.
DR InterPro; IPR000015; Fimb_usher.
DR InterPro; IPR018030; Fimbrial_membr_usher_CS.
DR InterPro; IPR042186; FimD_plug_dom.
DR InterPro; IPR025949; PapC-like_C.
DR InterPro; IPR043142; PapC-like_C_sf.
DR InterPro; IPR025885; PapC_N.
DR InterPro; IPR037224; PapC_N_sf.
DR PANTHER; PTHR30451; PTHR30451; 1.
DR Pfam; PF13953; PapC_C; 1.
DR Pfam; PF13954; PapC_N; 1.
DR Pfam; PF00577; Usher; 1.
DR SUPFAM; SSF141729; SSF141729; 1.
DR PROSITE; PS01151; FIMBRIAL_USHER; 1.
PE 2: Evidence at transcript level;
KW Cell outer membrane; Disulfide bond; Fimbrium biogenesis; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane beta strand;
KW Transport.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..867
FT /note="Outer membrane usher protein SfmD"
FT /id="PRO_0000009313"
FT DISULFID 840..862
FT /evidence="ECO:0000255"
SQ SEQUENCE 867 AA; 95677 MW; DF8591D0E6C4205A CRC64;
MKIPTTTDIP QRYTWCLAGI CYSSLAILPS FLSYAESYFN PAFLLENGTS VADLSRFERG
NHQPAGVYRV DLWRNDEFIG SQDIVFESTT ENTGDKSGGL MPCFNQVLLE RIGLNSSAFP
ELAQQQNNKC INLLKAVPDA TINFDFAAMR LNITIPQIAL LSSAHGYIPP EEWDEGIPAL
LLNYNFTGNR GNGNDSYFFS ELSGINIGPW RLRNNGSWNY FRGNGYHSEQ WNNIGTWVQR
AIIPLKSELV MGDGNTGSDI FDGVGFRGVR LYSSDNMYPD SQQGFAPTVR GIARTAAQLT
IRQNGFIIYQ SYVSPGAFEI TDLHPTSSNG DLDVTIDERD GNQQNYTIPY STVPILQREG
RFKFDLTAGD FRSGNSQQSS PFFFQGTALG GLPQEFTAYG GTQLSANYTA FLLGLGRNLG
NWGAVSLDVT HARSQLADAS RHEGDSIRFL YAKSMNTFGT NFQLMGYRYS TQGFYTLDDV
AYRRMEGYEY DYDGEHRDEP IIVNYHNLRF SRKDRLQLNV SQSLNDFGSL YISGTHQKYW
NTSDSDTWYQ VGYTSSWVGI SYSLSFSWNE SVGIPDNERI VGLNVSVPFN VLTKRRYTRE
NALDRAYASF NANRNSNGQN SWLAGVGGTL LEGHNLSYHV SQGDTSNNGY TGSATANWQA
AYGTLGGGYN YDRDQHDVNW QLSGGVVGHE NGITLSQPLG DTNVLIKAPG AGGVRIENQT
GILTDWRGYA VMLYATVYRY NRIALDTNTM GNSIDVEKNI SSVVPTQGAL VRANFDTRIG
VRALITVTQG GKPVPFGSLV RENSTGITSM VGDDGQVYLS GAPLSGELLV QWGDGANSRC
IAHYVLPKQS LQQAVTVISA VCTHPGS
