ID   YRAH_ECOLI              Reviewed;         194 AA.
AC   P42913; Q2M968;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Uncharacterized fimbrial-like protein YraH;
DE   Flags: Precursor;
GN   Name=yraH; OrderedLocusNames=b3142, JW3111;
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;
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   [2]
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   [3]
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 yraHIJK 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 operon. {ECO:0000269|PubMed:20345943}.
CC   -!- SUBCELLULAR LOCATION: Fimbrium {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 fimbrial protein family. {ECO:0000305}.
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DR   EMBL; U18997; AAA57945.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76176.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77188.1; -; Genomic_DNA.
DR   PIR; B65104; B65104.
DR   RefSeq; NP_417611.1; NC_000913.3.
DR   RefSeq; WP_001045432.1; NZ_LN832404.1.
DR   AlphaFoldDB; P42913; -.
DR   SMR; P42913; -.
DR   BioGRID; 4261995; 13.
DR   STRING; 511145.b3142; -.
DR   PaxDb; P42913; -.
DR   PRIDE; P42913; -.
DR   EnsemblBacteria; AAC76176; AAC76176; b3142.
DR   EnsemblBacteria; BAE77188; BAE77188; BAE77188.
DR   GeneID; 947658; -.
DR   KEGG; ecj:JW3111; -.
DR   KEGG; eco:b3142; -.
DR   PATRIC; fig|1411691.4.peg.3588; -.
DR   EchoBASE; EB2626; -.
DR   eggNOG; COG3539; Bacteria.
DR   HOGENOM; CLU_088965_0_3_6; -.
DR   OMA; QACEIDD; -.
DR   PhylomeDB; P42913; -.
DR   BioCyc; EcoCyc:G7637-MON; -.
DR   PRO; PR:P42913; -.
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..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..194
FT                   /note="Uncharacterized fimbrial-like protein YraH"
FT                   /id="PRO_0000009261"
FT   DISULFID        38..78
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   194 AA;  20744 MW;  02B10A946D45C4C6 CRC64;
     MNKVTKTAIA GLLALFAGNA AATDGEIVFD GEILKSACEI NDSDKKIEVA LGHYNAEQFR
     NIGERSPKIP FTIPLVNCPM TGWEHDNGNV EASFRLWLET RDNGTVPNFP NLAKVGSFAG
     IAATGVGIRI DDAESGNIMP LNAMGNDNTV YQIPAESNGI VNVDLIAYYV STVVPSEITP
     GEADAIVNVT LDYR