ID   YRAI_ECOLI              Reviewed;         231 AA.
AC   P42914; Q2M967;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Probable fimbrial chaperone YraI;
DE   Flags: Precursor;
GN   Name=yraI; OrderedLocusNames=b3143, JW3112;
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: Periplasm {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 periplasmic pilus chaperone family.
CC       {ECO:0000305}.
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DR   EMBL; U18997; AAA57946.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76177.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77189.1; -; Genomic_DNA.
DR   PIR; C65104; C65104.
DR   RefSeq; NP_417612.1; NC_000913.3.
DR   RefSeq; WP_000044775.1; NZ_LN832404.1.
DR   AlphaFoldDB; P42914; -.
DR   SMR; P42914; -.
DR   BioGRID; 4261996; 20.
DR   IntAct; P42914; 5.
DR   STRING; 511145.b3143; -.
DR   PaxDb; P42914; -.
DR   PRIDE; P42914; -.
DR   EnsemblBacteria; AAC76177; AAC76177; b3143.
DR   EnsemblBacteria; BAE77189; BAE77189; BAE77189.
DR   GeneID; 947657; -.
DR   KEGG; ecj:JW3112; -.
DR   KEGG; eco:b3143; -.
DR   PATRIC; fig|1411691.4.peg.3587; -.
DR   EchoBASE; EB2627; -.
DR   eggNOG; COG3121; Bacteria.
DR   HOGENOM; CLU_070768_2_1_6; -.
DR   InParanoid; P42914; -.
DR   OMA; WEAINDY; -.
DR   PhylomeDB; P42914; -.
DR   BioCyc; EcoCyc:G7638-MON; -.
DR   PRO; PR:P42914; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:InterPro.
DR   GO; GO:0061077; P:chaperone-mediated protein folding; IEA:InterPro.
DR   Gene3D; 2.60.40.10; -; 2.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR008962; PapD-like_sf.
DR   InterPro; IPR036316; Pili_assmbl_chap_C_dom_sf.
DR   InterPro; IPR001829; Pili_assmbl_chaperone_bac.
DR   InterPro; IPR016148; Pili_assmbl_chaperone_C.
DR   InterPro; IPR018046; Pili_assmbl_chaperone_CS.
DR   InterPro; IPR016147; Pili_assmbl_chaperone_N.
DR   Pfam; PF02753; PapD_C; 1.
DR   Pfam; PF00345; PapD_N; 1.
DR   PRINTS; PR00969; CHAPERONPILI.
DR   SUPFAM; SSF49354; SSF49354; 1.
DR   SUPFAM; SSF49584; SSF49584; 1.
DR   PROSITE; PS00635; PILI_CHAPERONE; 1.
PE   2: Evidence at transcript level;
KW   Chaperone; Fimbrium biogenesis; Immunoglobulin domain; Periplasm;
KW   Reference proteome; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..231
FT                   /note="Probable fimbrial chaperone YraI"
FT                   /id="PRO_0000009297"
SQ   SEQUENCE   231 AA;  25677 MW;  2416AC160661DE1B CRC64;
     MSKRTFAVIL TLLCSFCIGQ ALAGGIVLQR TRVIYDASRK EAALPVANKG AETPYLLQSW
     VDNIDGKSRA PFIITPPLFR LEAGDDSSLR IIKTADNLPE NKESLFYINV RAIPAKKKSD
     DVNANELTLV FKTRIKMFYR PAHLKGRVND AWKSLEFKRS DHSLNIYNPT EYYVVFAGLA
     VDKTDLTSKI EYIAPGEHKQ LPLPASGGKN VKWAAINDYG GSSGTETRPL Q