ID   ELFD_ECOLI              Reviewed;         233 AA.
AC   P75856;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 151.
DE   RecName: Full=Probable fimbrial chaperone protein ElfD;
DE   Flags: Precursor;
GN   Name=elfD; Synonyms=ycbR; OrderedLocusNames=b0939, JW0922;
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 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA   Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA   Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA   Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA   Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA   Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA   Horiuchi T.;
RT   "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 12.7-28.0 min region on the linkage map.";
RL   DNA Res. 3:137-155(1996).
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, AND INDUCTION.
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 elfADCG-ycbUVF fimbrial operon, which promotes
CC       adhesion of bacteria to different abiotic surfaces. Could be required
CC       for the biogenesis of the ElfA fimbriae. {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   -!- 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; U00096; AAC74025.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA35694.1; -; Genomic_DNA.
DR   PIR; B64834; B64834.
DR   RefSeq; NP_415459.1; NC_000913.3.
DR   RefSeq; WP_001295349.1; NZ_SSZK01000002.1.
DR   AlphaFoldDB; P75856; -.
DR   SMR; P75856; -.
DR   BioGRID; 4262112; 120.
DR   BioGRID; 851114; 1.
DR   IntAct; P75856; 3.
DR   STRING; 511145.b0939; -.
DR   PaxDb; P75856; -.
DR   PRIDE; P75856; -.
DR   EnsemblBacteria; AAC74025; AAC74025; b0939.
DR   EnsemblBacteria; BAA35694; BAA35694; BAA35694.
DR   GeneID; 946773; -.
DR   KEGG; ecj:JW0922; -.
DR   KEGG; eco:b0939; -.
DR   PATRIC; fig|1411691.4.peg.1335; -.
DR   EchoBASE; EB3474; -.
DR   eggNOG; COG3121; Bacteria.
DR   HOGENOM; CLU_070768_2_1_6; -.
DR   OMA; FTWAAGK; -.
DR   PhylomeDB; P75856; -.
DR   BioCyc; EcoCyc:G6481-MON; -.
DR   PRO; PR:P75856; -.
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..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..233
FT                   /note="Probable fimbrial chaperone protein ElfD"
FT                   /id="PRO_0000009292"
SQ   SEQUENCE   233 AA;  25389 MW;  1B18AB3806077C76 CRC64;
     MKTCITKGIV TVSLTAILLS CSSAWAAGKG GIGLAATRLV YSEGEEQISL GVRNTSPDVP
     YLIQSWVMTP DNKKSADFII TPPLFVLNPA NENLLRIMYI GAPLAKDRET LFFTSVRAVP
     STTKRKEGNT LKIATQSVIK LFWRPKGLAY PLGEAPAKLR CTSSADMVTV SNPTPYFITL
     TDLKIGGKVV KNQMISPFDK YQFSLPKGAK NSSVTYRTIN DYGAETPQLN CKS