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Database: UniProt
Entry: A0A1Q2M5S5_9GAMM
LinkDB: A0A1Q2M5S5_9GAMM
Original site: A0A1Q2M5S5_9GAMM 
ID   A0A1Q2M5S5_9GAMM        Unreviewed;       202 AA.
AC   A0A1Q2M5S5;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
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=Mag101_10955 {ECO:0000313|EMBL:AQQ68095.1};
OS   Microbulbifer agarilyticus.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Microbulbiferaceae; Microbulbifer.
OX   NCBI_TaxID=260552 {ECO:0000313|EMBL:AQQ68095.1, ECO:0000313|Proteomes:UP000188219};
RN   [1] {ECO:0000313|EMBL:AQQ68095.1, ECO:0000313|Proteomes:UP000188219}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GP101 {ECO:0000313|EMBL:AQQ68095.1,
RC   ECO:0000313|Proteomes:UP000188219};
RA   Jung J., Bae S.S., Baek K.;
RT   "Genome of Microbulbifer agarilyticus GP101.";
RL   Submitted (FEB-2017) 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; CP019650; AQQ68095.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q2M5S5; -.
DR   STRING; 260552.Mag101_10955; -.
DR   KEGG; maga:Mag101_10955; -.
DR   eggNOG; COG0652; Bacteria.
DR   OrthoDB; 9807797at2; -.
DR   Proteomes; UP000188219; 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; cd01920; cyclophilin_EcCYP_like; 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; IPR044665; E_coli_cyclophilin_A-like.
DR   PANTHER; PTHR43246; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE CYP38, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR43246:SF2; PEPTIDYLPROLYL ISOMERASE; 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:AQQ68095.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000188219};
KW   Rotamase {ECO:0000256|RuleBase:RU363019};
KW   Signal {ECO:0000256|RuleBase:RU363019}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|RuleBase:RU363019"
FT   CHAIN           29..202
FT                   /note="Peptidyl-prolyl cis-trans isomerase"
FT                   /evidence="ECO:0000256|RuleBase:RU363019"
FT                   /id="PRO_5011814949"
FT   DOMAIN          38..192
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50072"
SQ   SEQUENCE   202 AA;  21965 MW;  DCC52DA05EC848AC CRC64;
     MKRLTPFRAL LHTVLATLLL GLSSLALAVT NNPRVELQTD LGTIELVLYA DKAPVTVENF
     LKYVDSGFYD GTIFHRVIPG FMAQGGGFTF DFQEKPTDDP IKNESDNGLS NQRGTIAMAR
     TSVPDSATSQ FFINLVDNSR LDGSADKPGY TVFGKVLLGM GVVQQIAAEP RGQHRAHPDA
     PNMAVRILKA KRKDSDSGEN AQ
//
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