ID   SLYD_HELPY              Reviewed;         185 AA.
AC   O25748;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   27-MAR-2024, entry version 124.
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=HP_1123;
OS   Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700392 / 26695;
RX   PubMed=9252185; DOI=10.1038/41483;
RA   Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA   Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA   Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA   Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA   McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA   Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA   Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA   Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT   "The complete genome sequence of the gastric pathogen Helicobacter
RT   pylori.";
RL   Nature 388:539-547(1997).
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; AE000511; AAD08168.1; -; Genomic_DNA.
DR   PIR; C64660; C64660.
DR   RefSeq; NP_207914.1; NC_000915.1.
DR   RefSeq; WP_001179304.1; NC_018939.1.
DR   PDB; 2KR7; NMR; -; A=1-151.
DR   PDBsum; 2KR7; -.
DR   AlphaFoldDB; O25748; -.
DR   BMRB; O25748; -.
DR   SMR; O25748; -.
DR   STRING; 85962.HP_1123; -.
DR   PaxDb; 85962-C694_05800; -.
DR   EnsemblBacteria; AAD08168; AAD08168; HP_1123.
DR   KEGG; hpy:HP_1123; -.
DR   PATRIC; fig|85962.47.peg.1206; -.
DR   eggNOG; COG1047; Bacteria.
DR   InParanoid; O25748; -.
DR   OrthoDB; 9808891at2; -.
DR   PhylomeDB; O25748; -.
DR   BioCyc; MetaCyc:HP_RS05520-MONOMER; -.
DR   EvolutionaryTrace; O25748; -.
DR   PHI-base; PHI:11080; -.
DR   Proteomes; UP000000429; 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   GO; GO:0042026; P:protein refolding; IEA:UniProt.
DR   Gene3D; 2.40.10.330; -; 1.
DR   Gene3D; 3.10.50.40; -; 1.
DR   InterPro; IPR046357; PPIase_dom_sf.
DR   InterPro; IPR001179; PPIase_FKBP_dom.
DR   InterPro; IPR048261; SlpA/SlyD-like_ins_sf.
DR   PANTHER; PTHR47861; FKBP-TYPE PEPTIDYL-PROLYL CIS-TRANS ISOMERASE SLYD; 1.
DR   PANTHER; PTHR47861:SF3; FKBP-TYPE PEPTIDYL-PROLYL CIS-TRANS ISOMERASE SLYD; 1.
DR   Pfam; PF00254; FKBP_C; 1.
DR   SUPFAM; SSF54534; FKBP-like; 1.
DR   PROSITE; PS50059; FKBP_PPIASE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Chaperone; Cytoplasm; Isomerase; Metal-binding; Nickel;
KW   Reference proteome; Rotamase.
FT   CHAIN           1..185
FT                   /note="FKBP-type peptidyl-prolyl cis-trans isomerase SlyD"
FT                   /id="PRO_0000075359"
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   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"
FT   STRAND          12..23
FT                   /evidence="ECO:0007829|PDB:2KR7"
FT   STRAND          27..31
FT                   /evidence="ECO:0007829|PDB:2KR7"
FT   TURN            32..34
FT                   /evidence="ECO:0007829|PDB:2KR7"
FT   STRAND          37..40
FT                   /evidence="ECO:0007829|PDB:2KR7"
FT   HELIX           48..54
FT                   /evidence="ECO:0007829|PDB:2KR7"
FT   STRAND          62..67
FT                   /evidence="ECO:0007829|PDB:2KR7"
FT   TURN            69..73
FT                   /evidence="ECO:0007829|PDB:2KR7"
FT   STRAND          80..85
FT                   /evidence="ECO:0007829|PDB:2KR7"
FT   HELIX           86..89
FT                   /evidence="ECO:0007829|PDB:2KR7"
FT   STRAND          99..104
FT                   /evidence="ECO:0007829|PDB:2KR7"
FT   TURN            105..107
FT                   /evidence="ECO:0007829|PDB:2KR7"
FT   STRAND          108..117
FT                   /evidence="ECO:0007829|PDB:2KR7"
FT   STRAND          119..126
FT                   /evidence="ECO:0007829|PDB:2KR7"
FT   STRAND          135..145
FT                   /evidence="ECO:0007829|PDB:2KR7"
SQ   SEQUENCE   185 AA;  19997 MW;  26D0D84D771997FF CRC64;
     MQNHDLESIK QAALIEYEVR EQGSSIVLDS NISKEPLEFI IGTNQIIAGL EKAVLKAQIG
     EWEEVVIAPE EAYGVYESSY LQEVPRDQFE GIELEKGMSV FGQTEDNQTI QAIIKDFSAT
     HVMVDYNHPL AGKTLAFRFK VLGFREVSEE EILASHHGGG TGCCGGHGGH GGKKGGGCGC
     SCSHG
//