ID A0A5E7XTG0_9SPHN Unreviewed; 261 AA.
AC A0A5E7XTG0;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 08-NOV-2023, entry version 11.
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=SPHINGO361_100205 {ECO:0000313|EMBL:VVS97441.1};
OS Sphingomonas sp. EC-HK361.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=2038397 {ECO:0000313|EMBL:VVS97441.1, ECO:0000313|Proteomes:UP000326488};
RN [1] {ECO:0000313|EMBL:VVS97441.1, ECO:0000313|Proteomes:UP000326488}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SPHINGO361 {ECO:0000313|EMBL:VVS97441.1};
RA Dittami M. S.;
RL Submitted (SEP-2019) 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|ARBA:ARBA00007365, ECO:0000256|RuleBase:RU363019}.
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DR EMBL; CABVLH010000002; VVS97441.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5E7XTG0; -.
DR Proteomes; UP000326488; 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:VVS97441.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000326488};
KW Rotamase {ECO:0000256|RuleBase:RU363019};
KW Signal {ECO:0000256|RuleBase:RU363019}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|RuleBase:RU363019"
FT CHAIN 21..261
FT /note="Peptidyl-prolyl cis-trans isomerase"
FT /evidence="ECO:0000256|RuleBase:RU363019"
FT /id="PRO_5023128611"
FT DOMAIN 75..215
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
SQ SEQUENCE 261 AA; 28034 MW; 6D6B6C5F96A5AF5A CRC64;
MRVFAVLAFF GCLAATPALA QSQGDAVKKA EQAKMASKLA DEQREATAAT AAVRITPPPM
TDKNNQWLLD LSDGGRVTIW LRPDVAPRMV TRIKNLTRQH FYDGLLFHRV IDGFMAQGGD
PKGDGTGGST LPDVKAEFNY LPHVRGAVSA ARADSEDSAN SQFFIVFQPR LSLDKKYTVF
GRVIDGMQYV DAIERGEPPQ NPTRILHAYI AGDNPPAYQP APPPAPVASD TVTALPGTKT
IAKKTVPGKN VAAPKLAPAT K
//
