A8FTH5 (A8FTH5_SHESH) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Peptidyl-prolyl cis-trans isomerase RuleBase RU000493
EC=5.2.1.8 RuleBase RU000493

Gene names

Ordered Locus Names:

Ssed_1537 EMBL ABV36148.1

Organism

Shewanella sediminis (strain HAW-EB3) [Complete proteome] [HAMAP] EMBL ABV36148.1

Taxonomic identifier

425104 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Shewanellaceae › Shewanella › Shewanella sediminis

Protein attributes

Sequence length	187 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	PPIases accelerate the folding of proteins By similarity. RuleBase RU000493 PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides By similarity. RuleBase RU004223
Catalytic activity	Peptidylproline (omega=180) = peptidylproline (omega=0). RuleBase RU000493
Sequence similarities	Belongs to the cyclophilin-type PPIase family. RuleBase RU004223 Contains 1 PPIase cyclophilin-type domain. RuleBase RU003420

Ontologies

Keywords
Molecular function	Isomerase Rotamase RuleBase RU003420
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	protein folding Inferred from electronic annotation. Source: UniProtKB-KW protein peptidyl-prolyl isomerization Inferred from electronic annotation. Source: GOC
Molecular_function	peptidyl-prolyl cis-trans isomerase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	A8FTH5 [UniParc]. Last modified November 13, 2007. Version 1. Checksum: D09ADC94000CC38D	FASTA	187	20,601
	10 20 30 40 50 60 MQYGNCVRIQ PQFIIAKLTE NQNMITLHTN HGDITLELDA EKAPITAENF INYVKDGFYD 70 80 90 100 110 120 GTVFHRVIDG FMVQGGGFTE DMAQKRCNET IKNEANNGLS NVTGTVAMAR TSDPHSATAQ 130 140 150 160 170 180 FFININDNTF LDFKSESAQG WGYCVFAKVS AGMDVVNKIK AVSTGNRGMH QDVPLEAVII EKVTIAE

References

[1]

"Complete sequence of Shewanella sediminis HAW-EB3." US DOE Joint Genome Institute Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. , Kim E., Zhao J.-S., Richardson P. Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: HAW-EB3 EMBL ABV36148.1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000821 Genomic DNA. Translation: ABV36148.1.
RefSeq	YP_001473276.1. NC_009831.1.
3D structure databases
ProteinModelPortal	A8FTH5.
SMR	A8FTH5. Positions 24-186.
ModBase	Search...
Protein-protein interaction databases
STRING	425104.Ssed_1537.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABV36148; ABV36148; Ssed_1537.
GeneID	5612122.
KEGG	sse:Ssed_1537.
PATRIC	23560482. VBISheSed62411_1636.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0652.
HOGENOM	HOG000065978.
KO	K03768.
OMA	YANEESL.
ProtClustDB	CLSK2794520.
Family and domain databases
InterPro	IPR002130. Cyclophilin-like_PPIase_dom. IPR020892. Cyclophilin-type_PPIase_CS. [Graphical view]
Pfam	PF00160. Pro_isomerase. 1 hit. [Graphical view]
PRINTS	PR00153. CSAPPISMRASE.
SUPFAM	SSF50891. CSA_PPIase. 1 hit.
PROSITE	PS00170. CSA_PPIASE_1. 1 hit. PS50072. CSA_PPIASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

A8FTH5_SHESH

Accession

Primary (citable) accession number: A8FTH5

Entry history

Integrated into UniProtKB/TrEMBL:	November 13, 2007
Last sequence update:	November 13, 2007
Last modified:	May 1, 2013
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)