SLYD_HELPY
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 03-AUG-2022, entry version 117.
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; Proteobacteria; 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.C694_05800; -.
DR PaxDb; O25748; -.
DR EnsemblBacteria; AAD08168; AAD08168; HP_1123.
DR KEGG; hpy:HP_1123; -.
DR PATRIC; fig|85962.47.peg.1206; -.
DR eggNOG; COG1047; Bacteria.
DR OMA; FGQTEDH; -.
DR PhylomeDB; O25748; -.
DR BioCyc; MetaCyc:HP_RS05520-MON; -.
DR EvolutionaryTrace; O25748; -.
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 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 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
