SFMH_ECOLI
ID SFMH_ECOLI Reviewed; 327 AA.
AC P75715; P77078; Q2MBP6;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Uncharacterized fimbrial-like protein SfmH;
DE Flags: Precursor;
GN Name=sfmH; OrderedLocusNames=b0533, JW5071;
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: 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=AAB40731.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE76310.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U82598; AAB40731.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC73635.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE76310.1; ALT_INIT; Genomic_DNA.
DR PIR; D64785; D64785.
DR RefSeq; NP_415066.2; NC_000913.3.
DR AlphaFoldDB; P75715; -.
DR SMR; P75715; -.
DR BioGRID; 4261686; 4.
DR STRING; 511145.b0533; -.
DR PaxDb; P75715; -.
DR PRIDE; P75715; -.
DR EnsemblBacteria; AAC73635; AAC73635; b0533.
DR EnsemblBacteria; BAE76310; BAE76310; BAE76310.
DR GeneID; 945407; -.
DR KEGG; ecj:JW5071; -.
DR KEGG; eco:b0533; -.
DR PATRIC; fig|511145.12.peg.554; -.
DR EchoBASE; EB3643; -.
DR eggNOG; COG3539; Bacteria.
DR HOGENOM; CLU_066608_1_0_6; -.
DR InParanoid; P75715; -.
DR OMA; IKCTNVE; -.
DR PhylomeDB; P75715; -.
DR BioCyc; EcoCyc:G6293-MON; -.
DR PRO; PR:P75715; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009289; C:pilus; IBA:GO_Central.
DR GO; GO:0005537; F:mannose binding; IEA:UniProtKB-KW.
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 Fimbrium; Lectin; Mannose-binding; Reference proteome; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..327
FT /note="Uncharacterized fimbrial-like protein SfmH"
FT /id="PRO_0000009212"
SQ SEQUENCE 327 AA; 35696 MW; 8FAF2EA0E77A4FC5 CRC64;
MAMACLCLAN ISWATVCANS TGVAEDEHYD LSNIFNSTNN QPGQIVVLPE KSGWVGVSAI
CPPGTLVNYT YRSYVTNFIV QETIDNYKYM QLHDYLLGAM SLVDSVMDIQ FPPQNYIRMG
TDPNVSQNLP FGVMDSRLIF RLKVIRPFIN MVEIPRQVMF TVYVTSTPYD PLVTPVYTIS
FGGRVEVPQN CELNAGQIVE FDFGDIGASL FSAAGPGNRP AGVMPQTKSI AVKCTNVAAQ
AYLTMRLEAS AVSGQAMVSD NQDLGFIVAD QNDTPITPND LNSVIPFRLD AAAAANVTLR
AWPISITGQK PTEGPFSALG YLRVDYQ