ID   SLYD_HELPJ              Reviewed;         185 AA.
AC   Q9ZK89;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 116.
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=jhp_1052;
OS   Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J99 / ATCC 700824;
RX   PubMed=9923682; DOI=10.1038/16495;
RA   Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA   Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA   Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA   Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT   "Genomic sequence comparison of two unrelated isolates of the human gastric
RT   pathogen Helicobacter pylori.";
RL   Nature 397:176-180(1999).
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 (By 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   -!- 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; AE001439; AAD06631.1; -; Genomic_DNA.
DR   PIR; D71854; D71854.
DR   RefSeq; WP_001179280.1; NZ_CP011330.1.
DR   AlphaFoldDB; Q9ZK89; -.
DR   SMR; Q9ZK89; -.
DR   STRING; 85963.jhp_1052; -.
DR   EnsemblBacteria; AAD06631; AAD06631; jhp_1052.
DR   KEGG; hpj:jhp_1052; -.
DR   PATRIC; fig|85963.30.peg.1536; -.
DR   eggNOG; COG1047; Bacteria.
DR   OMA; FGQTEDH; -.
DR   Proteomes; UP000000804; 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..185
FT                   /note="FKBP-type peptidyl-prolyl cis-trans isomerase SlyD"
FT                   /id="PRO_0000075360"
FT   DOMAIN          1..99
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT   REGION          1..74
FT                   /note="PPIase first part"
FT                   /evidence="ECO:0000250"
FT   REGION          81..125
FT                   /note="IF-chaperone"
FT                   /evidence="ECO:0000250"
FT   REGION          134..156
FT                   /note="PPIase second part"
FT                   /evidence="ECO:0000250"
FT   REGION          164..185
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         163
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000255"
FT   BINDING         164
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000255"
FT   BINDING         178
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   185 AA;  20100 MW;  2D48E82AC450B0CB CRC64;
     MQNHDLESIK QAALIEYEVR EQGSSDVLDS NISKEPLEFI IGANQIIVGL EKAVLKAQIG
     EWEEIVIAPE EAYGVYESGY LQEVPRDQFE GIELEKGMSV FGQTEDNQTI QATIKDFSNT
     HVMVDYNHPL AGKTLAFRFK VLGFREVSEE EILASHHDSG TGCCGGHGGH GGKKGGGCGC
     SCSHG