SLYD_SHIFL
ID SLYD_SHIFL Reviewed; 196 AA.
AC P0A9L2; P30856;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, 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=SF3367, S4395;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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. SlyD could be involved in Tat-dependent
CC translocation, by binding to the Tat-type signal of folded proteins (By
CC 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 -!- SUBUNIT: Monomer. Binds to a broad range of unrelated Tat signal
CC sequences. Interacts with the hydrogenase nickel incorporation protein
CC HypB (By similarity). {ECO:0000250}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE005674; AAN44830.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP19347.1; -; Genomic_DNA.
DR RefSeq; NP_709123.1; NC_004337.2.
DR RefSeq; WP_000861334.1; NZ_WPGW01000003.1.
DR AlphaFoldDB; P0A9L2; -.
DR BMRB; P0A9L2; -.
DR SMR; P0A9L2; -.
DR STRING; 198214.SF3367; -.
DR EnsemblBacteria; AAN44830; AAN44830; SF3367.
DR EnsemblBacteria; AAP19347; AAP19347; S4395.
DR GeneID; 1025309; -.
DR GeneID; 66672771; -.
DR KEGG; sfl:SF3367; -.
DR KEGG; sfx:S4395; -.
DR PATRIC; fig|198214.7.peg.3977; -.
DR HOGENOM; CLU_098197_1_0_6; -.
DR OMA; HSHEGGC; -.
DR OrthoDB; 2044224at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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 3: Inferred from homology;
KW Chaperone; Cytoplasm; Isomerase; Metal-binding; Nickel; Reference proteome;
KW Rotamase.
FT CHAIN 1..196
FT /note="FKBP-type peptidyl-prolyl cis-trans isomerase SlyD"
FT /id="PRO_0000075361"
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 167
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 184
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000255"
FT BINDING 185
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000255"
FT BINDING 193
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000255"
FT BINDING 195
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /evidence="ECO:0000255"
SQ SEQUENCE 196 AA; 20853 MW; 46DCC7C7ECD61DBA CRC64;
MKVAKDLVVS LAYQVRTEDG VLVDESPVSA PLDYLHGHGS LISGLETALE GHEVGDKFDV
AVGANDAYGQ YDENLVQRVP KDVFMGVDEL QVGMRFLAET DQGPVPVEIT AVEDDHVVVD
GNHMLAGQNL KFNVEVVAIR EATEEELAHG HVHGAHDHHH DHDHDGCCGG HGHDHGHEHG
GEGCCGGKGN GGCGCH
