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SLYD_ECOL6
ID   SLYD_ECOL6              Reviewed;         196 AA.
AC   P0A9L0; P30856;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=FKBP-type peptidyl-prolyl cis-trans isomerase SlyD;
DE            Short=PPIase;
DE            EC=5.2.1.8;
DE   AltName: Full=Metallochaperone SlyD;
GN   Name=slyD; OrderedLocusNames=c4123;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Folding helper with both chaperone and peptidyl-prolyl cis-
CC       trans isomerase (PPIase) activities. Chaperone activity prevents
CC       aggregation of unfolded or partially folded proteins and promotes their
CC       correct folding. PPIases catalyze the cis-trans isomerization of Xaa-
CC       Pro bonds of peptides, which accelerates slow steps of protein folding
CC       and thus shortens the lifetime of intermediates. Both strategies lower
CC       the concentration of intermediates and increase the productivity and
CC       yield of the folding reaction. SlyD could be involved in Tat-dependent
CC       translocation, by binding to the Tat-type signal of folded proteins (By
CC       similarity). {ECO:0000250}.
CC   -!- FUNCTION: Also involved in hydrogenase metallocenter assembly, probably
CC       by participating in the nickel insertion step. This function in
CC       hydrogenase biosynthesis requires chaperone activity and the presence
CC       of the metal-binding domain, but not PPIase activity (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC         peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC         COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC         ChEBI:CHEBI:83834; EC=5.2.1.8;
CC   -!- SUBUNIT: Monomer. Binds to a broad range of unrelated Tat signal
CC       sequences. Interacts with the hydrogenase nickel incorporation protein
CC       HypB (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- DOMAIN: The N-terminal region consists of two globular folded domains
CC       that contain prolyl isomerase and chaperone activities. {ECO:0000250}.
CC   -!- DOMAIN: The C-terminal region binds nickel ions. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}.
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DR   EMBL; AE014075; AAN82561.1; -; Genomic_DNA.
DR   RefSeq; WP_000861334.1; NC_004431.1.
DR   AlphaFoldDB; P0A9L0; -.
DR   BMRB; P0A9L0; -.
DR   SMR; P0A9L0; -.
DR   STRING; 199310.c4123; -.
DR   EnsemblBacteria; AAN82561; AAN82561; c4123.
DR   GeneID; 66672771; -.
DR   KEGG; ecc:c4123; -.
DR   eggNOG; COG1047; Bacteria.
DR   HOGENOM; CLU_098197_1_0_6; -.
DR   OMA; HSHEGGC; -.
DR   BioCyc; ECOL199310:C4123-MON; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.50.40; -; 1.
DR   InterPro; IPR046357; PPIase_dom_sf.
DR   InterPro; IPR001179; PPIase_FKBP_dom.
DR   Pfam; PF00254; FKBP_C; 1.
DR   PROSITE; PS50059; FKBP_PPIASE; 1.
PE   3: Inferred from homology;
KW   Chaperone; Cytoplasm; Isomerase; Metal-binding; Nickel; Rotamase.
FT   CHAIN           1..196
FT                   /note="FKBP-type peptidyl-prolyl cis-trans isomerase SlyD"
FT                   /id="PRO_0000075357"
FT   DOMAIN          1..95
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT   REGION          1..69
FT                   /note="PPIase first part"
FT                   /evidence="ECO:0000250"
FT   REGION          76..120
FT                   /note="IF-chaperone"
FT                   /evidence="ECO:0000250"
FT   REGION          129..151
FT                   /note="PPIase second part"
FT                   /evidence="ECO:0000250"
FT   BINDING         167
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000255"
FT   BINDING         168
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000255"
FT   BINDING         184
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000255"
FT   BINDING         185
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000255"
FT   BINDING         193
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000255"
FT   BINDING         195
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   196 AA;  20853 MW;  46DCC7C7ECD61DBA CRC64;
     MKVAKDLVVS LAYQVRTEDG VLVDESPVSA PLDYLHGHGS LISGLETALE GHEVGDKFDV
     AVGANDAYGQ YDENLVQRVP KDVFMGVDEL QVGMRFLAET DQGPVPVEIT AVEDDHVVVD
     GNHMLAGQNL KFNVEVVAIR EATEEELAHG HVHGAHDHHH DHDHDGCCGG HGHDHGHEHG
     GEGCCGGKGN GGCGCH
 
 
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