ID A0A258X906_9BURK Unreviewed; 167 AA. AC A0A258X906; DT 20-DEC-2017, integrated into UniProtKB/TrEMBL. DT 20-DEC-2017, sequence version 1. DT 22-FEB-2023, entry version 17. DE RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU363019}; DE Short=PPIase {ECO:0000256|RuleBase:RU363019}; DE EC=5.2.1.8 {ECO:0000256|RuleBase:RU363019}; GN ORFNames=B7Y22_04180 {ECO:0000313|EMBL:OYZ36948.1}; OS Polynucleobacter sp. 16-46-70. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Polynucleobacter. OX NCBI_TaxID=1970421 {ECO:0000313|EMBL:OYZ36948.1, ECO:0000313|Proteomes:UP000217067}; RN [1] {ECO:0000313|EMBL:OYZ36948.1, ECO:0000313|Proteomes:UP000217067} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=16-46-70 {ECO:0000313|EMBL:OYZ36948.1}; RA Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S., RA Camacho D., Thomas B.C., Warren L.A., Banfield J.F.; RT "Lifting the veil on microbial sulfur biogeochemistry in mining RT wastewaters."; RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the CC cis-trans isomerization of proline imidic peptide bonds in CC oligopeptides. {ECO:0000256|ARBA:ARBA00002388, CC ECO:0000256|RuleBase:RU363019}. 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|RuleBase:RU363019}; CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. CC {ECO:0000256|ARBA:ARBA00007365, ECO:0000256|RuleBase:RU363019}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:OYZ36948.1}. 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; NCHC01000069; OYZ36948.1; -; Genomic_DNA. DR AlphaFoldDB; A0A258X906; -. DR Proteomes; UP000217067; Unassembled WGS sequence. DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006457; P:protein folding; IEA:InterPro. DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:InterPro. DR CDD; cd01920; cyclophilin_EcCYP_like; 1. DR Gene3D; 2.40.100.10; Cyclophilin-like; 1. DR InterPro; IPR029000; Cyclophilin-like_dom_sf. DR InterPro; IPR024936; Cyclophilin-type_PPIase. DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS. DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom. DR InterPro; IPR044665; E_coli_cyclophilin_A-like. DR PANTHER; PTHR43246:SF11; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE B; 1. DR PANTHER; PTHR43246; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE CYP38, CHLOROPLASTIC; 1. DR Pfam; PF00160; Pro_isomerase; 1. DR PIRSF; PIRSF001467; Peptidylpro_ismrse; 1. DR PRINTS; PR00153; CSAPPISMRASE. DR SUPFAM; SSF50891; Cyclophilin-like; 1. DR PROSITE; PS00170; CSA_PPIASE_1; 1. DR PROSITE; PS50072; CSA_PPIASE_2; 1. PE 3: Inferred from homology; KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU363019}; KW Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|RuleBase:RU363019}. FT DOMAIN 1..164 FT /note="PPIase cyclophilin-type" FT /evidence="ECO:0000259|PROSITE:PS50072" SQ SEQUENCE 167 AA; 17989 MW; 0972522C30F40C39 CRC64; MAKVLLKTSK GDITLTLDAV KAPKSVANFL QYVKSGQYDG TIFHRVIDNF MIQGGGMTAG MKQKPTGAEI ENEANNGLKN ERGTVAMART SDPHSATSQF FINVNDNDFL NHTAPNAQGW GYAVFGKVTD GLDVVDAIRK VKTGSAGFHQ DVPTEDVVIE KASVLEE //