ID   SLYD_TREPA              Reviewed;         176 AA.
AC   O83369;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 114.
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=TP_0349;
OS   Treponema pallidum (strain Nichols).
OC   Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX   NCBI_TaxID=243276;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nichols;
RX   PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA   Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA   Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA   Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA   McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA   Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA   Venter J.C.;
RT   "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL   Science 281:375-388(1998).
RN   [2]
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}.
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DR   EMBL; AE000520; AAC65334.1; -; Genomic_DNA.
DR   PIR; D71336; D71336.
DR   RefSeq; WP_010881797.1; NC_021490.2.
DR   AlphaFoldDB; O83369; -.
DR   SMR; O83369; -.
DR   STRING; 243276.TPANIC_0349; -.
DR   EnsemblBacteria; AAC65334; AAC65334; TP_0349.
DR   GeneID; 57878879; -.
DR   KEGG; tpa:TP_0349; -.
DR   eggNOG; COG1047; Bacteria.
DR   HOGENOM; CLU_098197_1_0_12; -.
DR   OMA; HSHEGGC; -.
DR   OrthoDB; 2044224at2; -.
DR   Proteomes; UP000000811; 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..176
FT                   /note="FKBP-type peptidyl-prolyl cis-trans isomerase SlyD"
FT                   /id="PRO_0000075362"
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         161
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         175
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   176 AA;  18428 MW;  77F8FE1901E73399 CRC64;
     MKIANECVVN IEYTLRDDTG EIIDSSDVMG ALEYVQGHGM IIPGLETALI NREEGEEFSV
     TIPPVGAYGE VQEDLRMTVG RDQFPPNVPI EVGMRFDAGS GGDSRPVTVT DVQGETIIVD
     GNHPLAGKTL HFEVAVRSVR EATDDDLAAL LFRESTSGGG CGSGAGGCGS CGAGCH