ID A0A2X0VEQ1_9GAMM Unreviewed; 164 AA.
AC A0A2X0VEQ1;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
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:SPT69272.1};
GN ORFNames=NCTC13093_00638 {ECO:0000313|EMBL:SPT69272.1};
OS Anaerobiospirillum thomasii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Succinivibrionaceae; Anaerobiospirillum.
OX NCBI_TaxID=179995 {ECO:0000313|EMBL:SPT69272.1, ECO:0000313|Proteomes:UP000250086};
RN [1] {ECO:0000313|EMBL:SPT69272.1, ECO:0000313|Proteomes:UP000250086}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC13093 {ECO:0000313|EMBL:SPT69272.1,
RC ECO:0000313|Proteomes:UP000250086};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) 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|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; UAPV01000001; SPT69272.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2X0VEQ1; -.
DR OrthoDB; 9807797at2; -.
DR Proteomes; UP000250086; 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; 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:UP000250086};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|RuleBase:RU363019}.
FT DOMAIN 1..162
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
SQ SEQUENCE 164 AA; 18242 MW; 5762D9C66EC48918 CRC64;
MVTLHTNLGD IVIELNTDKA PITCENFVKY IKSGHYNGTI FHRVIKGFMI QGGGMTQTLE
QKETLDPIDN EADNGLKNKT GAIAMARTQD PHSATSQFFI NTVDNDFLNF KSKDLQGWGY
CVFGKVVDGM DVVKKIEAVK TGSRGFYQDV PEEAVIIESV DYQI
//
