SLYD_VIBCH
ID SLYD_VIBCH Reviewed; 201 AA.
AC Q9KNX6;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 101.
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=VC_2604;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
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; AE003852; AAF95745.1; -; Genomic_DNA.
DR PIR; H82055; H82055.
DR RefSeq; NP_232232.1; NC_002505.1.
DR RefSeq; WP_000687664.1; NZ_LT906614.1.
DR AlphaFoldDB; Q9KNX6; -.
DR SMR; Q9KNX6; -.
DR STRING; 243277.VC_2604; -.
DR DNASU; 2615621; -.
DR EnsemblBacteria; AAF95745; AAF95745; VC_2604.
DR GeneID; 57741206; -.
DR KEGG; vch:VC_2604; -.
DR PATRIC; fig|243277.26.peg.2483; -.
DR eggNOG; COG1047; Bacteria.
DR HOGENOM; CLU_098197_1_0_6; -.
DR OMA; HSHEGGC; -.
DR BioCyc; VCHO:VC2604-MON; -.
DR Proteomes; UP000000584; Chromosome 1.
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..201
FT /note="FKBP-type peptidyl-prolyl cis-trans isomerase SlyD"
FT /id="PRO_0000392672"
FT DOMAIN 6..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 172
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000255"
FT BINDING 173
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000255"
FT BINDING 192
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000255"
FT BINDING 198
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000255"
SQ SEQUENCE 201 AA; 21248 MW; F86CC733E679F730 CRC64;
MKIEKNTVAS LAYQLTIEDG VVVDQSTVDA PLDYLHGHNN LITGLERELE GKVAGDKFTV
TIAPEDAYGE HNEDLVQRVP ADVFQGVDEL EVGMRFLADT DQGPIPVEIT EVDGDEVVVD
GNHMLAGQSL TFTVEVVAVR AATEDEIAHG HIHQAGGCGH DHDHDHDHEG GCCGGEGHGH
DHHGHGKKEG GCCGGGGCGS H
