ID Q63J95_BURPS Unreviewed; 113 AA. AC Q63J95; DT 25-OCT-2004, integrated into UniProtKB/TrEMBL. DT 25-OCT-2004, sequence version 1. DT 27-MAR-2024, entry version 123. DE RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU003915}; DE EC=5.2.1.8 {ECO:0000256|RuleBase:RU003915}; GN Name=fbp {ECO:0000313|EMBL:CAH39299.1}; GN OrderedLocusNames=BPSS1823 {ECO:0000313|EMBL:CAH39299.1}; OS Burkholderia pseudomallei (strain K96243). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=272560 {ECO:0000313|EMBL:CAH39299.1, ECO:0000313|Proteomes:UP000000605}; RN [1] {ECO:0000313|EMBL:CAH39299.1, ECO:0000313|Proteomes:UP000000605} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K96243 {ECO:0000313|EMBL:CAH39299.1, RC ECO:0000313|Proteomes:UP000000605}; RX PubMed=15377794; DOI=10.1073/pnas.0403302101; RA Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.M., Atkins T., RA Crossman L.C., Pitt T., Churcher C., Mungall K., Bentley S.D., Sebaihia M., RA Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A., Brown N.F., RA Challis G.L., Cherevach I., Chillingworth T., Cronin A., Crosset B., RA Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z., Hauser H., RA Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S., Price C., RA Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M., Simmonds M., RA Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M., Whitehead S., RA Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.; RT "Genomic plasticity of the causative agent of melioidosis, Burkholderia RT pseudomallei."; RL Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004). RN [2] {ECO:0007829|PDB:2KE0, ECO:0007829|PDB:2KO7} RP STRUCTURE BY NMR. RX PubMed=21574961; DOI=10.1042/BJ20110345; RA Norville I.H., O'Shea K., Sarkar-Tyson M., Zheng S., Titball R.W., RA Varani G., Harmer N.J.; RT "The structure of a Burkholderia pseudomallei immunophilin-inhibitor RT complex reveals new approaches to antimicrobial development."; RL Biochem. J. 437:413-422(2011). RN [3] {ECO:0007829|PDB:3UQA} RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 2-113. RX PubMed=24366729; DOI=10.1128/AAC.01875-13; RA Begley D.W., Fox D., Jenner D., Juli C., Pierce P.G., Abendroth J., RA Muruthi M., Safford K., Anderson V., Atkins K., Barnes S.R., Moen S.O., RA Raymond A.C., Stacy R., Myler P.J., Staker B.L., Harmer N.J., RA Norville I.H., Holzgrabe U., Sarkar-Tyson M., Edwards T.E., Lorimer D.D.; RT "A structural biology approach enables the development of antimicrobials RT targeting bacterial immunophilins."; RL Antimicrob. Agents Chemother. 58:1458-1467(2014). RN [4] {ECO:0007829|PDB:5V8T} RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 2-113 IN COMPLEX WITH MG(2+). RA Lorimer D.D., Dranow D.M., Seufert F., Abendroth J., Holzgrabe U.; RT "Crystal structure of SMT fusion Peptidyl-prolyl cis-trans isomerase from RT Burkholderia pseudomallei complexed with SF354."; RL Submitted (MAR-2017) to the PDB data bank. CC -!- CATALYTIC ACTIVITY: CC Reaction=[protein]-peptidylproline (omega=180) = [protein]- CC peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA- CC COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833, CC ChEBI:CHEBI:83834; EC=5.2.1.8; CC Evidence={ECO:0000256|ARBA:ARBA00000971, ECO:0000256|PROSITE- CC ProRule:PRU00277, ECO:0000256|RuleBase:RU003915}; CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. CC {ECO:0000256|ARBA:ARBA00006577, ECO:0000256|RuleBase:RU003915}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BX571966; CAH39299.1; -; Genomic_DNA. DR RefSeq; WP_004525093.1; NZ_CP009537.1. DR RefSeq; YP_111827.1; NC_006351.1. DR PDB; 2KE0; NMR; -; A=1-113. DR PDB; 2KO7; NMR; -; A=1-113. DR PDB; 2Y78; X-ray; 0.91 A; A=1-113. DR PDB; 3UQA; X-ray; 1.55 A; A=3-113. DR PDB; 5V8T; X-ray; 2.10 A; A/B=2-113. DR PDBsum; 2KE0; -. DR PDBsum; 2KO7; -. DR PDBsum; 2Y78; -. DR PDBsum; 3UQA; -. DR PDBsum; 5V8T; -. DR AlphaFoldDB; Q63J95; -. DR SMR; Q63J95; -. DR STRING; 272560.BPSS1823; -. DR KEGG; bps:BPSS1823; -. DR PATRIC; fig|272560.51.peg.5270; -. DR eggNOG; COG0545; Bacteria. DR EvolutionaryTrace; Q63J95; -. DR Proteomes; UP000000605; Chromosome 2. DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006457; P:protein folding; IEA:UniProt. DR Gene3D; 3.10.50.40; -; 1. DR InterPro; IPR046357; PPIase_dom_sf. DR InterPro; IPR001179; PPIase_FKBP_dom. DR PANTHER; PTHR43811:SF19; 39 KDA FK506-BINDING NUCLEAR PROTEIN; 1. DR PANTHER; PTHR43811; FKBP-TYPE PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FKPA; 1. DR Pfam; PF00254; FKBP_C; 1. DR SUPFAM; SSF54534; FKBP-like; 1. DR PROSITE; PS50059; FKBP_PPIASE; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:2KE0, ECO:0007829|PDB:2KO7}; KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00277, KW ECO:0000256|RuleBase:RU003915}; Metal-binding {ECO:0007829|PDB:5V8T}; KW Reference proteome {ECO:0000313|Proteomes:UP000000605}; KW Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|PROSITE- KW ProRule:PRU00277}. FT DOMAIN 26..113 FT /note="PPIase FKBP-type" FT /evidence="ECO:0000259|PROSITE:PS50059" FT BINDING 51 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0007829|PDB:5V8T" FT BINDING 52 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0007829|PDB:5V8T" SQ SEQUENCE 113 AA; 11930 MW; 10AB26FB56F3F284 CRC64; MTVVTTESGL KYEDLTEGSG AEARAGQTVS VHYTGWLTDG QKFDSSKDRN DPFAFVLGGG MVIKGWDEGV QGMKVGGVRR LTIPPQLGYG ARGAGGVIPP NATLVFEVEL LDV //