ID   YRAJ_ECOLI              Reviewed;         838 AA.
AC   P42915; Q2M966;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=Outer membrane usher protein YraJ;
DE   Flags: Precursor;
GN   Name=yraJ; OrderedLocusNames=b3144, JW3113;
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. Probably involved in the export and assembly of
CC       fimbrial subunits across the outer membrane.
CC       {ECO:0000269|PubMed:20345943}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250}; Multi-pass
CC       membrane protein {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 export usher family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA57947.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; U18997; AAA57947.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U00096; AAC76178.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77190.1; -; Genomic_DNA.
DR   PIR; D65104; D65104.
DR   RefSeq; NP_417613.1; NC_000913.3.
DR   RefSeq; WP_001355538.1; NZ_LN832404.1.
DR   AlphaFoldDB; P42915; -.
DR   SMR; P42915; -.
DR   BioGRID; 4261988; 145.
DR   STRING; 511145.b3144; -.
DR   TCDB; 1.B.11.3.6; the outer membrane fimbrial usher porin (fup) family.
DR   PaxDb; P42915; -.
DR   PRIDE; P42915; -.
DR   EnsemblBacteria; AAC76178; AAC76178; b3144.
DR   EnsemblBacteria; BAE77190; BAE77190; BAE77190.
DR   GeneID; 947656; -.
DR   KEGG; ecj:JW3113; -.
DR   KEGG; eco:b3144; -.
DR   PATRIC; fig|1411691.4.peg.3586; -.
DR   EchoBASE; EB2628; -.
DR   eggNOG; COG3188; Bacteria.
DR   HOGENOM; CLU_009120_3_1_6; -.
DR   InParanoid; P42915; -.
DR   OMA; PHARTEF; -.
DR   PhylomeDB; P42915; -.
DR   BioCyc; EcoCyc:G7639-MON; -.
DR   PRO; PR:P42915; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0009279; C:cell outer membrane; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015473; F:fimbrial usher porin activity; IBA:GO_Central.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR   GO; GO:0009297; P:pilus assembly; IBA:GO_Central.
DR   Gene3D; 2.60.40.2070; -; 1.
DR   Gene3D; 2.60.40.2610; -; 1.
DR   Gene3D; 3.10.20.410; -; 1.
DR   InterPro; IPR000015; Fimb_usher.
DR   InterPro; IPR018030; Fimbrial_membr_usher_CS.
DR   InterPro; IPR042186; FimD_plug_dom.
DR   InterPro; IPR025949; PapC-like_C.
DR   InterPro; IPR043142; PapC-like_C_sf.
DR   InterPro; IPR025885; PapC_N.
DR   InterPro; IPR037224; PapC_N_sf.
DR   PANTHER; PTHR30451; PTHR30451; 1.
DR   Pfam; PF13953; PapC_C; 1.
DR   Pfam; PF13954; PapC_N; 1.
DR   Pfam; PF00577; Usher; 1.
DR   SUPFAM; SSF141729; SSF141729; 1.
DR   PROSITE; PS01151; FIMBRIAL_USHER; 1.
PE   2: Evidence at transcript level;
KW   Cell outer membrane; Disulfide bond; Fimbrium biogenesis; Membrane;
KW   Reference proteome; Signal; Transmembrane; Transmembrane beta strand;
KW   Transport.
FT   SIGNAL          1..40
FT                   /evidence="ECO:0000255"
FT   CHAIN           41..838
FT                   /note="Outer membrane usher protein YraJ"
FT                   /id="PRO_0000009335"
FT   DISULFID        815..837
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   838 AA;  93616 MW;  FD265CC903A269BA CRC64;
     MPQRHHQGHK RTPKQLALII KRCLPMVLTG SGMLCTTANA EEYYFDPIML ETTKSGMQTT
     DLSRFSKKYA QLPGTYQVDI WLNKKKVSQK KITFTANAEQ LLQPQFTVEQ LRELGIKVDE
     IPALAEKDDD SVINSLEQII PGTAAEFDFN HQQLNLSIPQ IALYRDARGY VSPSRWDDGI
     PTLFTNYSFT GSDNRYRQGN RSQRQYLNMQ NGANFGPWRL RNYSTWTRND QTSSWNTISS
     YLQRDIKALK SQLLLGESAT SGSIFSSYTF TGVQLASDDN MLPNSQRGFA PTVRGIANSS
     AIVTIRQNGY VIYQSNVSAG AFEINDLYPS SNSGDLEVTI EESDGTQRRF IQPYSSLPMM
     QRPGHLKYSA TAGRYRADAN SDSKEPEFAE ATAIYGLNNT FTLYGGLLGS EDYYALGIGI
     GGTLGALGAL SMDINRADTQ FDNQHSFHGY QWRTQYIKDI PETNTNIAVS YYRYTNDGYF
     SFNEANTRNW DYNSRQKSEI QFNISQTIFD GVSLYASGSQ QDYWGNNDKN RNISVGVSGQ
     QWGVGYSLNY QYSRYTDQNN DRALSLNLSI PLERWLPRSR VSYQMTSQKD RPTQHEMRLD
     GSLLDDGRLS YSLEQSLDDD NNHNSSLNAS YRSPYGTFSA GYSYGNDSSQ YNYGVTGGVV
     IHPHGVTLSQ YLGNAFALID ANGASGVRIQ NYPGIATDPF GYAVVPYLTT YQENRLSVDT
     TQLPDNVDLE QTTQFVVPNR GAMVAARFNA NIGYRVLVTV SDRNGKPLPF GALASNDDTG
     QQSIVDEGGI LYLSGISSKS QSWTVRWGNQ ADQQCQFAFS TPDSEPTTSV LQGTAQCH