ID A0A0G1K6J9_9BACT Unreviewed; 237 AA.
AC A0A0G1K6J9;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 08-NOV-2023, entry version 31.
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=UW75_C0022G0005 {ECO:0000313|EMBL:KKT79210.1};
OS Parcubacteria group bacterium GW2011_GWF2_44_8.
OC Bacteria.
OX NCBI_TaxID=1618971 {ECO:0000313|EMBL:KKT79210.1, ECO:0000313|Proteomes:UP000034896};
RN [1] {ECO:0000313|EMBL:KKT79210.1, ECO:0000313|Proteomes:UP000034896}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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 -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC {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:KKT79210.1}.
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DR EMBL; LCJN01000022; KKT79210.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1K6J9; -.
DR PATRIC; fig|1618971.3.peg.252; -.
DR Proteomes; UP000034896; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR CDD; cd00317; cyclophilin; 1.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
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 PRINTS; PR00153; CSAPPISMRASE.
DR SUPFAM; SSF50891; Cyclophilin-like; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|RuleBase:RU363019, ECO:0000313|EMBL:KKT79210.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Rotamase {ECO:0000256|RuleBase:RU363019};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 69..235
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
SQ SEQUENCE 237 AA; 25618 MW; 9E8A4A9D08C0A2F6 CRC64;
MTKSNIISVS AVLIICGLLV VGLATLFGPS TPTNSALTDE TTEEAVEETF LPLTAEELAA
YQVSMTNESN PVAVFETNLG TFELELFEDT MPVTAGNFIK LAEEGFYDGI QFHRVIDGFM
IQGGDPITKT DEVFRYGTGG PGYAIPDEHV AGEFLTNVRG TISMANSGPN SGGSQFFINV
ADNTNLDFDK QPLSSKHPVF GRVVNGMDIV DAISKVEVTD RDLPMEPVVI EKLTIRR
//
