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O25748 (SLYD_HELPY) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
FKBP-type peptidyl-prolyl cis-trans isomerase SlyD
Short name=PPIase
EC=5.2.1.8
Alternative name(s):
Metallochaperone SlyD
Gene names
Name:slyD
Ordered Locus Names:HP_1123
OrganismHelicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori) [Reference proteome] [HAMAP]
Taxonomic identifier85962 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Helicobacter ›

Protein attributes

Sequence length185 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

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.

Catalytic activity

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

Subcellular location

Cytoplasm By similarity.

Domain

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 similarities

Belongs to the FKBP-type PPIase family.

Contains 1 PPIase FKBP-type domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMetal-binding
Nickel
   Molecular functionChaperone
Isomerase
Rotamase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processprotein folding

Inferred from electronic annotation. Source: UniProtKB-KW

protein peptidyl-prolyl isomerization

Inferred from electronic annotation. Source: GOC

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

peptidyl-prolyl cis-trans isomerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 185185FKBP-type peptidyl-prolyl cis-trans isomerase SlyD
PRO_0000075359

Regions

Domain1 – 9999PPIase FKBP-type
Region1 – 7474PPIase first part By similarity
Region81 – 12545IF-chaperone By similarity
Region134 – 15623PPIase second part By similarity
Region157 – 18529Metal-binding By similarity
Compositional bias158 – 18528Gly-rich

Secondary structure

1 ......................... 185
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O25748 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 26D0D84D771997FF

FASTA18519,997
        10         20         30         40         50         60 
MQNHDLESIK QAALIEYEVR EQGSSIVLDS NISKEPLEFI IGTNQIIAGL EKAVLKAQIG 

        70         80         90        100        110        120 
EWEEVVIAPE EAYGVYESSY LQEVPRDQFE GIELEKGMSV FGQTEDNQTI QAIIKDFSAT 

       130        140        150        160        170        180 
HVMVDYNHPL AGKTLAFRFK VLGFREVSEE EILASHHGGG TGCCGGHGGH GGKKGGGCGC 


SCSHG

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE000511 Genomic DNA. Translation: AAD08168.1.
PIRC64660.
RefSeqNP_207914.1. NC_000915.1.
YP_006935040.1. NC_018939.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2KR7NMR-A1-151[»]
ProteinModelPortalO25748.
ModBaseSearch...

Protein-protein interaction databases

STRING85962.HP1123.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAD08168; AAD08168; HP_1123.
GeneID13870318.
899660.
KEGGheo:C694_05800.
hpy:HP1123.
PATRIC20593591. VBIHelPyl33062_1175.

Phylogenomic databases

eggNOGCOG1047.
KOK03775.
OMAHMLAGQT.
ProtClustDBCLSK872504.

Family and domain databases

InterProIPR023566. PPIase_FKBP.
IPR001179. PPIase_FKBP_dom.
[Graphical view]
PANTHERPTHR10516. PTHR10516. 1 hit.
PfamPF00254. FKBP_C. 1 hit.
[Graphical view]
PROSITEPS50059. FKBP_PPIASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO25748.

Entry information

Entry nameSLYD_HELPY
AccessionPrimary (citable) accession number: O25748
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 1, 1998
Last modified: May 1, 2013
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Helicobacter pylori

Helicobacter pylori (strain 26695): entries and gene names

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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