ID A0A5B8RVJ3_9BURK Unreviewed; 190 AA.
AC A0A5B8RVJ3;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
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=FOZ74_11055 {ECO:0000313|EMBL:QEA13531.1};
OS Comamonas flocculans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Comamonas.
OX NCBI_TaxID=2597701 {ECO:0000313|EMBL:QEA13531.1, ECO:0000313|Proteomes:UP000321199};
RN [1] {ECO:0000313|EMBL:QEA13531.1, ECO:0000313|Proteomes:UP000321199}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NLF 7-7 {ECO:0000313|EMBL:QEA13531.1,
RC ECO:0000313|Proteomes:UP000321199};
RA Kim D.H., Kim J.G.;
RT "Complete genome sequence of Comamonas sp. NLF 7-7 isolated from
RT livestock.";
RL Submitted (JUL-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|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 -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC {ECO:0000256|ARBA:ARBA00007365, ECO:0000256|RuleBase:RU363019}.
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DR EMBL; CP042344; QEA13531.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5B8RVJ3; -.
DR KEGG; cof:FOZ74_11055; -.
DR OrthoDB; 9807797at2; -.
DR Proteomes; UP000321199; 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; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR044665; E_coli_cyclophilin_A-like.
DR PANTHER; PTHR43246:SF12; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE A; 1.
DR PANTHER; PTHR43246; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE CYP38, CHLOROPLASTIC; 1.
DR Pfam; PF00160; Pro_isomerase; 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:QEA13531.1};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW Reference proteome {ECO:0000313|Proteomes:UP000321199};
KW Rotamase {ECO:0000256|RuleBase:RU363019};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU363019}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|RuleBase:RU363019"
FT CHAIN 23..190
FT /note="Peptidyl-prolyl cis-trans isomerase"
FT /evidence="ECO:0000256|RuleBase:RU363019"
FT /id="PRO_5023159439"
FT DOMAIN 34..188
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
SQ SEQUENCE 190 AA; 20267 MW; B5626462464C7F43 CRC64;
MTSRRSACLA LLVTAAALPA HAADDSQPKV KLATSLGDIV VQLDCAKAPK TVDNFLQYVR
EQHYDGTIFH RVINGFMIQG GGFTTDMVQK PTRAPVPLEA DNGLKNDAYT IAMARTANPN
SATAQFFINV KDNDGLNAPK PDGHGYAVFG KVIEGKEVVD KIKTVATGNR GPHQNVPTTP
VVIESATIVP
//
