ID   SLYD_AERHY              Reviewed;         212 AA.
AC   O07046;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 76.
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; Synonyms=ilpA;
OS   Aeromonas hydrophila.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=644;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=A6;
RX   PubMed=9171380; DOI=10.1128/jb.179.11.3397-3403.1997;
RA   Wong C.Y.F., Heuzenroeder M.W., Quinn D.M., Flower R.L.P.;
RT   "Cloning and characterization of two immunophilin-like genes, ilpA and
RT   fkpA, on a single 3.9-kilobase fragment of Aeromonas hydrophila genomic
RT   DNA.";
RL   J. Bacteriol. 179:3397-3403(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; U56832; AAC45359.1; -; Genomic_DNA.
DR   AlphaFoldDB; O07046; -.
DR   SMR; O07046; -.
DR   STRING; 1448139.AI20_14265; -.
DR   eggNOG; COG1047; Bacteria.
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..212
FT                   /note="FKBP-type peptidyl-prolyl cis-trans isomerase SlyD"
FT                   /id="PRO_0000075363"
FT   DOMAIN          1..94
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..119
FT                   /note="IF-chaperone"
FT                   /evidence="ECO:0000250"
FT   REGION          128..150
FT                   /note="PPIase second part"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   212 AA;  22430 MW;  0982895472433E1D CRC64;
     MKVAPLSVVT LEYTVTDEHG EVIDTTVGKE PLVYLHGTRY LVSGLEAELE GRSVGEAFDV
     TLTPEQAYGQ YDENLVQEVP GELFDGMEVS EGDTFVAETD DGHRPVTVIE VSEEFVKVDG
     NHPLAGVTLG FKVEIKDVRA ATAEELAHGH VHGAGGCGHD HGHDHDHDHG HEHGGYCGGG
     HHGHDHGHDH GDDHGHGGCC GGGGCGAKGH QH