ID   YEHC_ECOLI              Reviewed;         239 AA.
AC   P33342; Q2MAW8;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=Probable fimbrial chaperone YehC;
DE   Flags: Precursor;
GN   Name=yehC; OrderedLocusNames=b2110, JW2097;
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 / BHB2600;
RA   Richterich P., Lakey N., Gryan G., Jaehn L., Mintz L., Robison K.,
RA   Church G.M.;
RT   "Automated multiplex sequencing of the E.coli genome.";
RL   Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases.
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., Mau B.,
RA   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 MG1655
RT   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 chaperone-
RT   usher fimbriae with distinct surface specificities.";
RL   Environ. Microbiol. 12:1957-1977(2010).
CC   -!- FUNCTION: Part of the yehABCD fimbrial operon. Could contribute to
CC       adhesion to various surfaces in specific environmental niches.
CC       {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; U00007; AAA60474.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC75171.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76588.1; -; Genomic_DNA.
DR   PIR; E64978; E64978.
DR   RefSeq; NP_416613.1; NC_000913.3.
DR   AlphaFoldDB; P33342; -.
DR   SMR; P33342; -.
DR   BioGRID; 4260436; 28.
DR   IntAct; P33342; 4.
DR   STRING; 511145.b2110; -.
DR   PaxDb; P33342; -.
DR   PRIDE; P33342; -.
DR   EnsemblBacteria; AAC75171; AAC75171; b2110.
DR   EnsemblBacteria; BAE76588; BAE76588; BAE76588.
DR   GeneID; 946621; -.
DR   KEGG; ecj:JW2097; -.
DR   KEGG; eco:b2110; -.
DR   PATRIC; fig|511145.12.peg.2187; -.
DR   EchoBASE; EB1932; -.
DR   eggNOG; COG3121; Bacteria.
DR   HOGENOM; CLU_070768_0_1_6; -.
DR   OMA; TIMIAPQ; -.
DR   PhylomeDB; P33342; -.
DR   BioCyc; EcoCyc:EG11989-MON; -.
DR   PRO; PR:P33342; -.
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..31
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..239
FT                   /note="Probable fimbrial chaperone YehC"
FT                   /id="PRO_0000009293"
SQ   SEQUENCE   239 AA;  26589 MW;  78B84A20BFAB39A8 CRC64;
     MAAIPWRPFN LRGIKMKGLL SLLIFSMVLP AHAGIVIYGT RIIYPAENKE VMVQLMNQGN
     RSSLLQAWID DGDTSLPPEK IQVPFMLTPP VAKIGANSGQ QVKIKIMPNK LPTNKESIFY
     LNVLDIPPNS PEQEGKNALK FAMQNRIKLF YRPAGIAPVN KATFKKLLVN RSGNGLVIKN
     DSANWVTISD VKANNVKVNY ETIMIAPLES QSVNVKSNNA NNWHLTIIDD HGNYISDKI