UniProt Accession

 SLYD_ECOLI; P0A9K9; P30856; Q2M714 

Genbank Protein ID

 Z21496; L13261; L28082; U18997; U00096; AP009048 

Genbank Nucleotide ID

 CAA79705.1; AAA18574.1; AAC41458.1; AAA58146.1; AAC76374.1; BAE77942.1 

Protein Name

 FKBP-type peptidyl-prolyl cis-trans isomerase SlyD 

Protein Synonyms/Alias

 PPIase; Histidine-rich protein; Metallochaperone SlyD; Rotamase; Sensitivity to lysis protein D; WHP 

Gene Name

 slyD 

Gene Synonyms/Alias

 b3349; JW3311 

Created Date

 July 27, 2013 

Organism

 Escherichia coli (strain K12) 

NCBI Taxa ID

 83333 

Lysine Modification

Position	Peptide	Type	References
5	***MKVAKDLVVSLA	acetylation	[1]
81	NLVQRVPKDVFMGVD	acetylation	[1]

Reference

 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618] 

Functional Description

 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. SlyD could be involved in Tat-dependent translocation, by binding to the Tat-type signal of folded proteins. The PPIase substrate specificity, carried out with synthetic peptides of the 'suc-Ala-Xaa-Pro-Phe-4NA' type (where Xaa is the AA tested), was found to be Phe > Ala > Leu. 

Sequence Annotation

 DOMAIN 1 95 PPIase FKBP-type.
 REGION 1 69 PPIase first part.
 REGION 76 120 IF-chaperone.
 REGION 129 151 PPIase second part.
 REGION 152 196 Metal-binding.
 METAL 167 167 Nickel (Potential).
 METAL 168 168 Nickel (Potential).
 METAL 184 184 Nickel (Potential).
 METAL 185 185 Nickel (Potential).
 METAL 193 193 Nickel (Potential).
 METAL 195 195 Nickel (Potential).  

Keyword

 3D-structure; Chaperone; Cobalt; Complete proteome; Copper; Cytoplasm; Direct protein sequencing; Isomerase; Metal-binding; Nickel; Reference proteome; Rotamase; Zinc. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 196 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0016020; C:membrane; IBA:RefGenome.
 GO:0050897; F:cobalt ion binding; IDA:EcoCyc.
 GO:0005507; F:copper ion binding; IDA:EcoCyc.
 GO:0005528; F:FK506 binding; IBA:RefGenome.
 GO:0016151; F:nickel cation binding; IDA:EcoCyc.
 GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:EcoCyc.
 GO:0051082; F:unfolded protein binding; IDA:EcoCyc.
 GO:0008270; F:zinc ion binding; IDA:EcoCyc.
 GO:0022417; P:protein maturation by protein folding; IMP:EcoliWiki.
 GO:0042026; P:protein refolding; IDA:EcoCyc.
 GO:0050821; P:protein stabilization; IMP:EcoliWiki.
 GO:0009408; P:response to heat; IEP:EcoliWiki. 

Interpro

 IPR023566; PPIase_FKBP.
 IPR001179; PPIase_FKBP_dom. 

Pfam

 PF00254; FKBP_C 

SMART

  

PROSITE

 PS50059; FKBP_PPIASE 

PRINTS