ID   YRAK_ECOLI              Reviewed;         363 AA.
AC   P43319; Q2M965;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=Uncharacterized fimbrial-like protein YraK;
DE   Flags: Precursor;
GN   Name=yraK; OrderedLocusNames=b3145, JW3114;
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA57948.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; U18997; AAA57948.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U00096; AAC76179.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77191.1; -; Genomic_DNA.
DR   PIR; E65104; E65104.
DR   RefSeq; NP_417614.1; NC_000913.3.
DR   RefSeq; WP_000816992.1; NZ_LN832404.1.
DR   AlphaFoldDB; P43319; -.
DR   SMR; P43319; -.
DR   BioGRID; 4261994; 426.
DR   STRING; 511145.b3145; -.
DR   PaxDb; P43319; -.
DR   PRIDE; P43319; -.
DR   EnsemblBacteria; AAC76179; AAC76179; b3145.
DR   EnsemblBacteria; BAE77191; BAE77191; BAE77191.
DR   GeneID; 947654; -.
DR   KEGG; ecj:JW3114; -.
DR   KEGG; eco:b3145; -.
DR   PATRIC; fig|1411691.4.peg.3585; -.
DR   EchoBASE; EB2629; -.
DR   eggNOG; COG3539; Bacteria.
DR   HOGENOM; CLU_066608_0_0_6; -.
DR   OMA; TIACNCT; -.
DR   PhylomeDB; P43319; -.
DR   BioCyc; EcoCyc:G7640-MON; -.
DR   PRO; PR:P43319; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0009289; C:pilus; IBA:GO_Central.
DR   GO; GO:0043709; P:cell adhesion involved in single-species biofilm formation; IMP:EcoCyc.
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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   2: Evidence at transcript level;
KW   Fimbrium; Reference proteome; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           21..363
FT                   /note="Uncharacterized fimbrial-like protein YraK"
FT                   /id="PRO_0000013908"
SQ   SEQUENCE   363 AA;  38535 MW;  33CAE8050D4088E2 CRC64;
     MKRAPLITGL LLISTSCAYA SSGGCGADST SGATNYSSVV DDVTVNQTDN VTGREFTSAT
     LSSTNWQYAC SCSAGKAVKL VYMVSPVLTT TGHQTGYYKL NDSLDIKTTL QANDIPGLTT
     DQVVSVNTRF TQIKNNTVYS AATQTGVCQG DTSRYGPVNI GANTTFTLYV TKPFLGSMTI
     PKTDIAVIKG AWVDGMGSPS TGDFHDLVKL SIQGNLTAPQ SCKINQGDVI KVNFGFINGQ
     KFTTRNAMPD GFTPVDFDIT YDCGDTSKIK NSLQMRIDGT TGVVDQYNLV ARRRSSDNVP
     DVGIRIENLG GGVANIPFQN GILPVDPSGH GTVNMRAWPV NLVGGELETG KFQGTATITV
     IVR