ID A0A076H623_9SYNE Unreviewed; 146 AA.
AC A0A076H623;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 42.
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=KR49_01995 {ECO:0000313|EMBL:AII45235.1};
OS Synechococcus sp. KORDI-49.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=585423 {ECO:0000313|EMBL:AII45235.1, ECO:0000313|Proteomes:UP000028589};
RN [1] {ECO:0000313|EMBL:AII45235.1, ECO:0000313|Proteomes:UP000028589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KORDI-49 {ECO:0000313|EMBL:AII45235.1,
RC ECO:0000313|Proteomes:UP000028589};
RA Choi D.H., Kwon K.-K., Lee J.-H., Noh J.H.;
RT "Genome sequences of Synechococcus sp. KORDI-49.";
RL Submitted (JUN-2013) 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; CP006270; AII45235.1; -; Genomic_DNA.
DR RefSeq; WP_043691074.1; NZ_CP006270.1.
DR AlphaFoldDB; A0A076H623; -.
DR STRING; 585423.KR49_01995; -.
DR KEGG; synr:KR49_01995; -.
DR PATRIC; fig|585423.3.peg.374; -.
DR eggNOG; COG0652; Bacteria.
DR HOGENOM; CLU_012062_16_4_3; -.
DR OrthoDB; 9807797at2; -.
DR Proteomes; UP000028589; 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; IPR024936; Cyclophilin-type_PPIase.
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 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|RuleBase:RU363019};
KW Rotamase {ECO:0000256|RuleBase:RU363019}.
FT DOMAIN 1..122
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
SQ SEQUENCE 146 AA; 15452 MW; CEEEB3FA32CCE710 CRC64;
MTKALMETEA GPIELELFEA DAPNTVANFV KLAKDGFYDG LAFHRVIPGF MAQGGCPNSR
EGSKGMPGTG GPGYQIDCEI NSKKHQAGTL AMAHAGKNTG GSQFYICHEA QPHLDGVHTV
FGLTGNMDTV LKLGNGSRIT KVTIQD
//