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Protein

Peptidyl-prolyl cis-trans isomerase B

Gene

cypB

Organism
Streptomyces anulatus (Streptomyces chrysomallus)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.

Catalytic activityi

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

Enzyme regulationi

Inhibited by cyclosporin A (CsA).

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Rotamase

Keywords - Ligandi

Cyclosporin

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomerase B (EC:5.2.1.8)
Short name:
PPIase B
Alternative name(s):
Cyclophilin ScCypB
Rotamase B
S-cyclophilin
Gene namesi
Name:cypB
OrganismiStreptomyces anulatus (Streptomyces chrysomallus)
Taxonomic identifieri1892 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 175175Peptidyl-prolyl cis-trans isomerase BPRO_0000064207Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliP77949.
SMRiP77949. Positions 7-172.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 172170PPIase cyclophilin-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Family and domain databases

Gene3Di2.40.100.10. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
PANTHERiPTHR11071. PTHR11071. 1 hit.
PfamiPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PIRSFiPIRSF001467. Peptidylpro_ismrse. 1 hit.
PRINTSiPR00153. CSAPPISMRASE.
SUPFAMiSSF50891. SSF50891. 1 hit.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P77949-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEQLYATLK TNRGDIEIRL LPNHAPKTVR NFVELATGQR EWVNPETGEK
60 70 80 90 100
STDRLYDGTV FHRVISGFMI QGGDPLGNGT GGPGYKFADE FHPELGFTQP
110 120 130 140 150
YLLAMANAGP GTNGSQFFLT VSPTAWLTGK HTIFGEVSGE AGRKVVDAIA
160 170
ATPTNPRTDR PLEDVVIESV VVETR
Length:175
Mass (Da):19,017
Last modified:February 1, 1997 - v1
Checksum:iE77616D34EFA5791
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U64692 Genomic DNA. Translation: AAB51775.1.
PIRiT51359.
RefSeqiWP_050359820.1. NZ_CM003601.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U64692 Genomic DNA. Translation: AAB51775.1.
PIRiT51359.
RefSeqiWP_050359820.1. NZ_CM003601.1.

3D structure databases

ProteinModelPortaliP77949.
SMRiP77949. Positions 7-172.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di2.40.100.10. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
PANTHERiPTHR11071. PTHR11071. 1 hit.
PfamiPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PIRSFiPIRSF001467. Peptidylpro_ismrse. 1 hit.
PRINTSiPR00153. CSAPPISMRASE.
SUPFAMiSSF50891. SSF50891. 1 hit.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "ScCypB is a novel second cytosolic cyclophilin from Streptomyces chrysomallus which is phylogenetically distant from ScCypA."
    Pahl A., Gewies A., Keller U.
    Microbiology 143:117-126(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.

Entry informationi

Entry nameiPPIB_STRAQ
AccessioniPrimary (citable) accession number: P77949
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: February 1, 1997
Last modified: March 16, 2016
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. 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.