ID A7GX96_CAMC5 Unreviewed; 163 AA.
AC A7GX96;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 95.
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 Name=ppiB {ECO:0000313|EMBL:EAT99444.1};
GN ORFNames=CCV52592_1036 {ECO:0000313|EMBL:EAT99444.1};
OS Campylobacter curvus (strain 525.92).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=360105 {ECO:0000313|EMBL:EAT99444.1, ECO:0000313|Proteomes:UP000006380};
RN [1] {ECO:0000313|Proteomes:UP000006380}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=525.92 {ECO:0000313|Proteomes:UP000006380};
RA Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA Mandrell R.E., Lastovica A.J., Nelson K.E.;
RT "Genome sequence of Campylobacter curvus 525.92 isolated from human
RT feces.";
RL Submitted (JUL-2007) 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 -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC {ECO:0000256|RuleBase:RU363019}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000767; EAT99444.1; -; Genomic_DNA.
DR RefSeq; WP_011992017.1; NC_009715.2.
DR AlphaFoldDB; A7GX96; -.
DR STRING; 360105.CCV52592_1036; -.
DR KEGG; ccv:CCV52592_1036; -.
DR HOGENOM; CLU_012062_16_4_7; -.
DR OrthoDB; 9807797at2; -.
DR Proteomes; UP000006380; 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; 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 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:EAT99444.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006380};
KW Rotamase {ECO:0000256|RuleBase:RU363019}.
FT DOMAIN 28..150
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
SQ SEQUENCE 163 AA; 17943 MW; 2A1C6914B2E00286 CRC64;
MLEELKIYDV DLDELRKSRF AVLSTEKGDI TLELFADEAP QAVANFVELI KSGFYNGLNF
HRVIPNFVIQ GGCPNGNGMG GPGWRIKCEC DGQKVKHERG SLSMAHAGRD TGGSQFFICH
SPQPHLNGVH TVFGKCANEE SLKVLDSIRQ GDKIILAQIK ESL
//
