ID M1LP49_9PROT Unreviewed; 167 AA.
AC M1LP49;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 59.
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=CDEE_0395 {ECO:0000313|EMBL:AGF47457.1};
OS Candidatus Kinetoplastibacterium crithidii TCC036E.
OC Bacteria; Pseudomonadota; Betaproteobacteria;
OC Candidatus Kinetoplastibacterium.
OX NCBI_TaxID=1208918 {ECO:0000313|EMBL:AGF47457.1, ECO:0000313|Proteomes:UP000011686};
RN [1] {ECO:0000313|EMBL:AGF47457.1, ECO:0000313|Proteomes:UP000011686}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TCC036E {ECO:0000313|EMBL:AGF47457.1,
RC ECO:0000313|Proteomes:UP000011686};
RX PubMed=23345457;
RA Alves J.M., Serrano M.G., Maia da Silva F., Voegtly L.J., Matveyev A.V.,
RA Teixeira M.M., Camargo E.P., Buck G.A.;
RT "Genome evolution and phylogenomic analysis of candidatus
RT kinetoplastibacterium, the betaproteobacterial endosymbionts of strigomonas
RT and angomonas.";
RL Genome Biol. Evol. 5:338-350(2013).
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; CP003804; AGF47457.1; -; Genomic_DNA.
DR RefSeq; WP_015389061.1; NC_020283.1.
DR AlphaFoldDB; M1LP49; -.
DR STRING; 1208918.CDEE_0395; -.
DR KEGG; kct:CDEE_0395; -.
DR PATRIC; fig|1208918.3.peg.153; -.
DR eggNOG; COG0652; Bacteria.
DR HOGENOM; CLU_012062_16_9_4; -.
DR Proteomes; UP000011686; 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; 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; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE CYP38, CHLOROPLASTIC; 1.
DR PANTHER; PTHR43246:SF11; PEPTIDYLPROLYL ISOMERASE; 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 Reference proteome {ECO:0000313|Proteomes:UP000011686};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|RuleBase:RU363019}.
FT DOMAIN 7..165
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
SQ SEQUENCE 167 AA; 18759 MW; E5114F231A00F9D2 CRC64;
MIKAKIQTNL GEITVSLDKD KAPITVENFL HYVNTKFYDD TLFHRVIDGF MIQGGGLTKN
LENKTSEKKP IENEANNGLK NDKYTIAMAR TNDPHSATSQ FFINVADNDF LNYSAPTQNG
WGYAVFGKVV DGEETINKIK NSRTGNKGFH QNVPMEDIVI KTVEIIE
//