ID A0A1Q7WS97_9CHLR Unreviewed; 171 AA.
AC A0A1Q7WS97;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=AUG45_06715 {ECO:0000313|EMBL:OLE33639.1};
OS Ktedonobacter sp. 13_1_20CM_3_54_15.
OC Bacteria; Chloroflexota; Ktedonobacteria; Ktedonobacterales;
OC Ktedonobacteraceae; Ktedonobacter.
OX NCBI_TaxID=1805224 {ECO:0000313|EMBL:OLE33639.1, ECO:0000313|Proteomes:UP000186882};
RN [1] {ECO:0000313|EMBL:OLE33639.1, ECO:0000313|Proteomes:UP000186882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27843720;
RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA Banfield J.F.;
RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT heterotrophy are prevalent below the grass root zone.";
RL PeerJ 4:E2687-E2687(2016).
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:OLE33639.1}.
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DR EMBL; MNJJ01000121; OLE33639.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q7WS97; -.
DR Proteomes; UP000186882; 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 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:OLE33639.1};
KW Rotamase {ECO:0000256|RuleBase:RU363019}.
FT DOMAIN 21..170
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT REGION 150..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 171 AA; 18341 MW; F0CA8063D77C0BC1 CRC64;
MAQKSYSGPP PMVIDPAKKY VATFHTDVGD FQVELFAAQA PQTVNNFVFL AREGFYNNTT
FHRVIRDFMA QGGDPTGTGT GGPGYKFADE RGALSLKHDR AGILSMANAG ANTNGSQFFI
TFGPTPHLNG KHGVFGVVTS GMDVVQSIRE RDPGRAREPG TGISSIEITE Q
//
