ID A0A5K7X5B3_9BACT Unreviewed; 144 AA.
AC A0A5K7X5B3;
DT 22-APR-2020, integrated into UniProtKB/TrEMBL.
DT 22-APR-2020, sequence version 1.
DT 24-JAN-2024, entry version 14.
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=PLANPX_1506 {ECO:0000313|EMBL:BBO31894.1};
OS Lacipirellula parvula.
OC Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Lacipirellulaceae;
OC Lacipirellula.
OX NCBI_TaxID=2650471 {ECO:0000313|EMBL:BBO31894.1, ECO:0000313|Proteomes:UP000326837};
RN [1] {ECO:0000313|Proteomes:UP000326837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PX69 {ECO:0000313|Proteomes:UP000326837};
RA Dedysh S.N., Kulichevskaya I.S., Beletsky A.V., Rakitin A.L.,
RA Mardanov A.V., Ivanova A.A., Saltykova V.X., Rijpstra W.I.C.,
RA Sinninghe Damste J.S., Ravin N.V.;
RT "Lacipirellula parvula gen. nov., sp. nov., representing a lineage of
RT planctomycetes widespread in freshwater anoxic habitats, and description of
RT the family Lacipirellulaceae.";
RL Submitted (OCT-2019) 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}.
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DR EMBL; AP021861; BBO31894.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5K7X5B3; -.
DR KEGG; lpav:PLANPX_1506; -.
DR Proteomes; UP000326837; Chromosome.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR CDD; cd00317; cyclophilin; 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; IPR044666; Cyclophilin_A-like.
DR PANTHER; PTHR45625; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE-RELATED; 1.
DR PANTHER; PTHR45625:SF4; PEPTIDYLPROLYL ISOMERASE DOMAIN AND WD REPEAT-CONTAINING PROTEIN 1; 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|RuleBase:RU363019, ECO:0000313|EMBL:BBO31894.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000326837};
KW Rotamase {ECO:0000256|RuleBase:RU363019}.
FT DOMAIN 1..132
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
SQ SEQUENCE 144 AA; 15677 MW; 1C2678F2CE54E494 CRC64;
MKVATMTTNK GVIRLELFAD KTPKTVENFE KLAKKGFYDG LKFHRVIEDF MIQGGCPEGT
GTGGPGYKFG DEFVADLKHS GPGILSMANA GPNTNGSQFF ITHVATPWLD GKHTVFGKVL
DKGQDVVNKI KQGDKIETLV ISEE
//
