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Protein

FKBP-type peptidyl-prolyl cis-trans isomerase SlyD

Gene

slyD

Organism
Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Folding helper with both chaperone and peptidyl-prolyl cis-trans isomerase (PPIase) activities. Chaperone activity prevents aggregation of unfolded or partially folded proteins and promotes their correct folding. PPIases catalyze the cis-trans isomerization of Xaa-Pro bonds of peptides, which accelerates slow steps of protein folding and thus shortens the lifetime of intermediates. Both strategies lower the concentration of intermediates and increase the productivity and yield of the folding reaction (By similarity).By similarity
Also involved in hydrogenase metallocenter assembly, probably by participating in the nickel insertion step. This function in hydrogenase biosynthesis requires chaperone activity and the presence of the metal-binding domain, but not PPIase activity (By similarity).By similarity

Catalytic activityi

Peptidylproline (omega=180) = peptidylproline (omega=0).

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Isomerase, Rotamase

Keywords - Ligandi

Metal-binding, Nickel

Enzyme and pathway databases

BioCyciHPY:HP1123-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
FKBP-type peptidyl-prolyl cis-trans isomerase SlyD (EC:5.2.1.8)
Short name:
PPIase
Alternative name(s):
Metallochaperone SlyD
Gene namesi
Name:slyD
Ordered Locus Names:HP_1123
OrganismiHelicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Taxonomic identifieri85962 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter
Proteomesi
  • UP000000429 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000753591 – 185FKBP-type peptidyl-prolyl cis-trans isomerase SlyDAdd BLAST185

Proteomic databases

PaxDbiO25748.

Interactioni

Protein-protein interaction databases

STRINGi85962.HP1123.

Structurei

Secondary structure

1185
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi12 – 23Combined sources12
Beta strandi27 – 31Combined sources5
Turni32 – 34Combined sources3
Beta strandi37 – 40Combined sources4
Helixi48 – 54Combined sources7
Beta strandi62 – 67Combined sources6
Turni69 – 73Combined sources5
Beta strandi80 – 85Combined sources6
Helixi86 – 89Combined sources4
Beta strandi99 – 104Combined sources6
Turni105 – 107Combined sources3
Beta strandi108 – 117Combined sources10
Beta strandi119 – 126Combined sources8
Beta strandi135 – 145Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2KR7NMR-A1-151[»]
ProteinModelPortaliO25748.
SMRiO25748.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO25748.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 99PPIase FKBP-typePROSITE-ProRule annotationAdd BLAST99

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 74PPIase first partBy similarityAdd BLAST74
Regioni81 – 125IF-chaperoneBy similarityAdd BLAST45
Regioni134 – 156PPIase second partBy similarityAdd BLAST23
Regioni157 – 185Metal-bindingBy similarityAdd BLAST29

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi158 – 185Gly-richAdd BLAST28

Domaini

The N-terminal region consists of two globular folded domains that contain prolyl isomerase and chaperone activities.By similarity
The C-terminal region binds nickel ions.By similarity

Sequence similaritiesi

Belongs to the FKBP-type PPIase family.Curated
Contains 1 PPIase FKBP-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4108YZY. Bacteria.
COG1047. LUCA.
KOiK03775.
OMAiTEDHQTI.

Family and domain databases

InterProiIPR023566. PPIase_FKBP.
IPR001179. PPIase_FKBP_dom.
[Graphical view]
PANTHERiPTHR10516. PTHR10516. 2 hits.
PfamiPF00254. FKBP_C. 1 hit.
[Graphical view]
PROSITEiPS50059. FKBP_PPIASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O25748-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQNHDLESIK QAALIEYEVR EQGSSIVLDS NISKEPLEFI IGTNQIIAGL
60 70 80 90 100
EKAVLKAQIG EWEEVVIAPE EAYGVYESSY LQEVPRDQFE GIELEKGMSV
110 120 130 140 150
FGQTEDNQTI QAIIKDFSAT HVMVDYNHPL AGKTLAFRFK VLGFREVSEE
160 170 180
EILASHHGGG TGCCGGHGGH GGKKGGGCGC SCSHG
Length:185
Mass (Da):19,997
Last modified:January 1, 1998 - v1
Checksum:i26D0D84D771997FF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000511 Genomic DNA. Translation: AAD08168.1.
PIRiC64660.
RefSeqiNP_207914.1. NC_000915.1.
WP_001179304.1. NC_018939.1.

Genome annotation databases

EnsemblBacteriaiAAD08168; AAD08168; HP_1123.
GeneIDi899660.
KEGGiheo:C694_05800.
hpy:HP1123.
PATRICi20593591. VBIHelPyl33062_1175.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000511 Genomic DNA. Translation: AAD08168.1.
PIRiC64660.
RefSeqiNP_207914.1. NC_000915.1.
WP_001179304.1. NC_018939.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2KR7NMR-A1-151[»]
ProteinModelPortaliO25748.
SMRiO25748.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi85962.HP1123.

Proteomic databases

PaxDbiO25748.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAD08168; AAD08168; HP_1123.
GeneIDi899660.
KEGGiheo:C694_05800.
hpy:HP1123.
PATRICi20593591. VBIHelPyl33062_1175.

Phylogenomic databases

eggNOGiENOG4108YZY. Bacteria.
COG1047. LUCA.
KOiK03775.
OMAiTEDHQTI.

Enzyme and pathway databases

BioCyciHPY:HP1123-MONOMER.

Miscellaneous databases

EvolutionaryTraceiO25748.

Family and domain databases

InterProiIPR023566. PPIase_FKBP.
IPR001179. PPIase_FKBP_dom.
[Graphical view]
PANTHERiPTHR10516. PTHR10516. 2 hits.
PfamiPF00254. FKBP_C. 1 hit.
[Graphical view]
PROSITEiPS50059. FKBP_PPIASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSLYD_HELPY
AccessioniPrimary (citable) accession number: O25748
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 1, 1998
Last modified: November 2, 2016
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Helicobacter pylori
    Helicobacter pylori (strain 26695): entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.