ID YFCV_ECOLI Reviewed; 187 AA. AC P77288; P76940; DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 13-NOV-2019, entry version 121. DE RecName: Full=Uncharacterized fimbrial-like protein YfcV; DE Flags: Precursor; GN Name=yfcV; OrderedLocusNames=b2339, JW2336; 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 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=9205837; DOI=10.1093/dnares/4.2.91; RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., RA Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., RA Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., RA Oshima T., Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., RA Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., RA Yamagata S., Horiuchi T.; RT "Construction of a contiguous 874-kb sequence of the Escherichia coli- RT K12 genome corresponding to 50.0-68.8 min on the linkage map and RT analysis of its sequence features."; RL DNA Res. 4:91-113(1997). 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., RA Mau B., 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 RT MG1655 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 RT chaperone-usher fimbriae with distinct surface specificities."; RL Environ. Microbiol. 12:1957-1977(2010). CC -!- FUNCTION: Part of the yfcOPQRSUV fimbrial operon. Could contribute CC to adhesion to various surfaces in specific environmental niches. CC Increases adhesion to eukaryotic T24 bladder epithelial cells in CC the absence of fim genes. {ECO:0000269|PubMed:20345943}. CC -!- INDUCTION: Expression is negatively regulated by H-NS and CC subjected to cAMP receptor protein (CRP)-mediated catabolite CC repression. {ECO:0000269|PubMed:20345943}. CC -!- DISRUPTION PHENOTYPE: Deletion of the operon under classical CC laboratory conditions does not result in any major effect on CC E.coli capacity to form biofilms compared with the wild-type CC strain. {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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U00096; AAC75399.1; -; Genomic_DNA. DR EMBL; AP009048; BAA16193.1; -; Genomic_DNA. DR PIR; A65007; A65007. DR RefSeq; NP_416841.1; NC_000913.3. DR RefSeq; WP_000033316.1; NZ_LN832404.1. DR SMR; P77288; -. DR BioGrid; 4263168; 8. DR IntAct; P77288; 1. DR STRING; 511145.b2339; -. DR jPOST; P77288; -. DR PaxDb; P77288; -. DR PRIDE; P77288; -. DR EnsemblBacteria; AAC75399; AAC75399; b2339. DR EnsemblBacteria; BAA16193; BAA16193; BAA16193. DR GeneID; 949109; -. DR KEGG; ecj:JW2336; -. DR KEGG; eco:b2339; -. DR PATRIC; fig|1411691.4.peg.4393; -. DR EchoBASE; EB3877; -. DR HOGENOM; HOG000260127; -. DR BioCyc; EcoCyc:G7210-MONOMER; -. DR BioCyc; ECOL316407:JW2336-MONOMER; -. DR PRO; PR:P77288; -. 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 GO; GO:0043711; P:pilus organization; 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 Complete proteome; Reference proteome; Signal. FT SIGNAL 1 25 {ECO:0000255}. FT CHAIN 26 187 Uncharacterized fimbrial-like protein FT YfcV. FT /FTId=PRO_0000013774. SQ SEQUENCE 187 AA; 19851 MW; 9BAE027695988940 CRC64; MSKFVKTAIA AAMVMGAFTS TATIAAGNNG TARFYGTIED SVCSIVPDDH KLEVDMGDIG AEKLKNNGTT TPKNFQIRLQ DCVFDTQETM TTTFTGTVSS ANSGNYYTIF NTDTGAAFNN VSLAIGDSLG TSYKSGMGID QKIVKDTATN KGKAKQTLNF KAWLVGAADA PDLGNFEANT TFQITYL //