SLYD_YERPE
ID SLYD_YERPE Reviewed; 195 AA.
AC Q7CFU4; Q74XZ9;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=YPO0193, y3975, YP_0191;
OS Yersinia pestis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis;
RX PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(2004).
RN [4]
RP FUNCTION AS A CHAPERONE AND A PPIASE, AND CATALYTIC ACTIVITY.
RX PubMed=16388577; DOI=10.1021/bi051922n;
RA Scholz C., Eckert B., Hagn F., Schaarschmidt P., Balbach J., Schmid F.X.;
RT "SlyD proteins from different species exhibit high prolyl isomerase and
RT chaperone activities.";
RL Biochemistry 45:20-33(2006).
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. {ECO:0000269|PubMed:16388577}.
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 Evidence={ECO:0000269|PubMed:16388577};
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAS60467.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL590842; CAL18877.1; -; Genomic_DNA.
DR EMBL; AE009952; AAM87519.1; -; Genomic_DNA.
DR EMBL; AE017042; AAS60467.1; ALT_INIT; Genomic_DNA.
DR PIR; AD0024; AD0024.
DR RefSeq; WP_002212316.1; NZ_WUCM01000004.1.
DR RefSeq; YP_002345275.1; NC_003143.1.
DR AlphaFoldDB; Q7CFU4; -.
DR SMR; Q7CFU4; -.
DR STRING; 214092.YPO0193; -.
DR PaxDb; Q7CFU4; -.
DR DNASU; 1148922; -.
DR EnsemblBacteria; AAM87519; AAM87519; y3975.
DR EnsemblBacteria; AAS60467; AAS60467; YP_0191.
DR GeneID; 57974410; -.
DR KEGG; ype:YPO0193; -.
DR KEGG; ypk:y3975; -.
DR KEGG; ypm:YP_0191; -.
DR PATRIC; fig|214092.21.peg.425; -.
DR eggNOG; COG1047; Bacteria.
DR HOGENOM; CLU_098197_1_0_6; -.
DR OMA; HSHEGGC; -.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; Chromosome.
DR Proteomes; UP000002490; 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; IDA:UniProtKB.
DR GO; GO:0042026; P:protein refolding; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Chaperone; Cytoplasm; Isomerase; Metal-binding; Nickel; Reference proteome;
KW Rotamase.
FT CHAIN 1..195
FT /note="FKBP-type peptidyl-prolyl cis-trans isomerase SlyD"
FT /id="PRO_0000392673"
FT DOMAIN 6..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 166
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000255"
FT BINDING 167
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000255"
FT BINDING 186
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000255"
FT BINDING 192
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000255"
FT BINDING 194
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000255"
FT VARIANT 180..181
FT /note="Missing (in strain: 91001 / Biovar Mediaevalis)"
SQ SEQUENCE 195 AA; 21052 MW; 30ACC25DE545B692 CRC64;
MKVTKDLVVS LAYQVRTEDG VLVDESPVSA PLDYLHGHGS LIAGLENALE GHEAGDSFDV
RVNADEGYGS YDENLVQRVP KDVFMGVDEL EVGMRFLADT DQGPVPVEIT AVEDEHVVVD
GNHMLAGQDL NFHVEVVAVR EATEEELQHG HVHGEHDHHH EHGDGCCGGH GHDDHEHEHE
HGKGGCGKSG GCGCH
