YADV_ECOLI
ID YADV_ECOLI Reviewed; 246 AA.
AC P33128;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Probable fimbrial chaperone YadV;
DE Flags: Precursor;
GN Name=yadV; Synonyms=ecpD; OrderedLocusNames=b0140, JW0136;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION BY HEAT SHOCK.
RC STRAIN=K12;
RX PubMed=8102362; DOI=10.1128/jb.175.16.5009-5021.1993;
RA Raina S., Missiakas D., Baird L., Kumar S., Georgopoulos C.;
RT "Identification and transcriptional analysis of the Escherichia coli htrE
RT operon which is homologous to pap and related pilin operons.";
RL J. Bacteriol. 175:5009-5021(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8202364; DOI=10.1093/nar/22.9.1637;
RA Fujita N., Mori H., Yura T., Ishihama A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-
RT 4.1 min (110,917-193,643 bp) region.";
RL Nucleic Acids Res. 22:1637-1639(1994).
RN [3]
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 [4]
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 [5]
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 yadCKLM-htrE-yadVN fimbrial operon. Could
CC contribute to adhesion to various surfaces in specific environmental
CC niches. {ECO:0000269|PubMed:20345943}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC -!- INDUCTION: Repressed by H-NS. Induced by heat shock.
CC {ECO:0000269|PubMed:20345943, ECO:0000269|PubMed:8102362}.
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}.
CC -!- CAUTION: Was originally called ecpD, but ecp is now used for the
CC ecpABCDE operon involved in E.coli common pilus (ECP) synthesis.
CC {ECO:0000305|PubMed:8102362}.
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DR EMBL; L00680; AAA23720.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73251.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96716.1; -; Genomic_DNA.
DR PIR; S45209; S45209.
DR RefSeq; NP_414682.1; NC_000913.3.
DR RefSeq; WP_000465928.1; NZ_STEB01000010.1.
DR PDB; 5GHU; X-ray; 1.63 A; A=26-246.
DR PDBsum; 5GHU; -.
DR AlphaFoldDB; P33128; -.
DR SMR; P33128; -.
DR BioGRID; 4263031; 16.
DR DIP; DIP-9492N; -.
DR IntAct; P33128; 1.
DR STRING; 511145.b0140; -.
DR PaxDb; P33128; -.
DR PRIDE; P33128; -.
DR EnsemblBacteria; AAC73251; AAC73251; b0140.
DR EnsemblBacteria; BAB96716; BAB96716; BAB96716.
DR GeneID; 944859; -.
DR KEGG; ecj:JW0136; -.
DR KEGG; eco:b0140; -.
DR PATRIC; fig|1411691.4.peg.2141; -.
DR EchoBASE; EB1916; -.
DR eggNOG; COG3121; Bacteria.
DR HOGENOM; CLU_070768_0_2_6; -.
DR InParanoid; P33128; -.
DR OMA; AWIDNGN; -.
DR PhylomeDB; P33128; -.
DR BioCyc; EcoCyc:EG11973-MON; -.
DR PRO; PR:P33128; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IMP:EcoCyc.
DR GO; GO:0071555; P:cell wall organization; IEA:InterPro.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IEA:InterPro.
DR DisProt; DP02923; -.
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 1: Evidence at protein level;
KW 3D-structure; Chaperone; Fimbrium biogenesis; Immunoglobulin domain;
KW Periplasm; Reference proteome; Signal; Stress response.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..246
FT /note="Probable fimbrial chaperone YadV"
FT /id="PRO_0000009269"
FT CONFLICT 79
FT /note="A -> R (in Ref. 1; AAA23720)"
FT /evidence="ECO:0000305"
FT CONFLICT 110..111
FT /note="SV -> RA (in Ref. 1; AAA23720)"
FT /evidence="ECO:0000305"
FT STRAND 27..37
FT /evidence="ECO:0007829|PDB:5GHU"
FT STRAND 43..49
FT /evidence="ECO:0007829|PDB:5GHU"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:5GHU"
FT STRAND 55..63
FT /evidence="ECO:0007829|PDB:5GHU"
FT STRAND 76..86
FT /evidence="ECO:0007829|PDB:5GHU"
FT STRAND 91..98
FT /evidence="ECO:0007829|PDB:5GHU"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:5GHU"
FT STRAND 110..119
FT /evidence="ECO:0007829|PDB:5GHU"
FT STRAND 138..147
FT /evidence="ECO:0007829|PDB:5GHU"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:5GHU"
FT HELIX 158..161
FT /evidence="ECO:0007829|PDB:5GHU"
FT STRAND 163..167
FT /evidence="ECO:0007829|PDB:5GHU"
FT STRAND 174..179
FT /evidence="ECO:0007829|PDB:5GHU"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:5GHU"
FT STRAND 187..194
FT /evidence="ECO:0007829|PDB:5GHU"
FT STRAND 197..201
FT /evidence="ECO:0007829|PDB:5GHU"
FT STRAND 210..216
FT /evidence="ECO:0007829|PDB:5GHU"
FT STRAND 227..233
FT /evidence="ECO:0007829|PDB:5GHU"
FT STRAND 239..245
FT /evidence="ECO:0007829|PDB:5GHU"
SQ SEQUENCE 246 AA; 27054 MW; 33C77D484DD77E08 CRC64;
MFFNTKHTTA LCFVTCMAFS SSSIADIVIS GTRVIYKSDQ KSVNVRLENK GNNPLLVQSW
LDTGDDNAEP GSITVPFTAT PPVSRIDAKR GQTIKLMYTA STSLPKDRES VFWFNVLEVP
PKPDAEKVAN QSLLQLAFRT RIKLFYRPDG LKGNPSEAPL ALKWFWSGSE GKASLRVTNP
TPYYVSFSSG DLEASGKRYP IDVKMIAPFS DEVMKVNGLN GKANSAKVHF YAINDFGGAI
EGNARL
