ID A0A2T4U851_9BACI Unreviewed; 248 AA.
AC A0A2T4U851;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=C6Y45_05505 {ECO:0000313|EMBL:PTL39579.1};
OS Alkalicoccus saliphilus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Alkalicoccus.
OX NCBI_TaxID=200989 {ECO:0000313|EMBL:PTL39579.1, ECO:0000313|Proteomes:UP000240509};
RN [1] {ECO:0000313|EMBL:PTL39579.1, ECO:0000313|Proteomes:UP000240509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6AG {ECO:0000313|EMBL:PTL39579.1,
RC ECO:0000313|Proteomes:UP000240509};
RA Zhao B.;
RT "Alkalicoccus saliphilus sp. nov., isolated from a mineral pool.";
RL Submitted (MAR-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|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:PTL39579.1}.
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DR EMBL; PZJJ01000006; PTL39579.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T4U851; -.
DR OrthoDB; 9807797at2; -.
DR Proteomes; UP000240509; 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; 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:PTL39579.1};
KW Rotamase {ECO:0000256|RuleBase:RU363019}.
FT DOMAIN 64..244
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..52
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 248 AA; 27586 MW; FBEDB2C888BA23F1 CRC64;
MLLFSACGNN NEEAADEIDE NLQNDPAGEE EVDQENIDEP EEQDDELEDL EDLTYPQFEE
DESNYPQAVL HTSMGEIELI LFPEEAPLAV ENFITLAEEG YYDEVIFHRV IENFMVQGGD
PSGTGMGGDS AFGEPFEDEF DPSLGHFRGA LSMANSGPDT NSSQFFIVQA DESQVSEEMF
QDSGFPEQRV EYYVEEGGTP HLDFQHTVFG HVTEGMDVVD EIAAVETESA DKPSEDVVIE
SVEIVDEE
//
