ID K6ZQN3_9ALTE Unreviewed; 259 AA.
AC K6ZQN3;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 70.
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=ppiA {ECO:0000313|EMBL:GAC32592.1};
GN ORFNames=GPLA_1678 {ECO:0000313|EMBL:GAC32592.1};
OS Paraglaciecola polaris LMG 21857.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Paraglaciecola.
OX NCBI_TaxID=1129793 {ECO:0000313|EMBL:GAC32592.1, ECO:0000313|Proteomes:UP000006322};
RN [1] {ECO:0000313|EMBL:GAC32592.1, ECO:0000313|Proteomes:UP000006322}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 21857 {ECO:0000313|EMBL:GAC32592.1,
RC ECO:0000313|Proteomes:UP000006322};
RX PubMed=25009843;
RA Qin Q.-L., Xie B.-B., Yu Y., Shu Y.-L., Rong J.-C., Zhang Y.-J.,
RA Zhao D.-L., Chen X.-L., Zhang X.-Y., Chen B., Zhou B.-C., Zhang Y.-Z.;
RT "Comparative genomics of the marine bacterial genus Glaciecola reveals the
RT high degree of genomic diversity and genomic characteristic for cold
RT adaptation.";
RL Environ. Microbiol. 16:1642-1653(2014).
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}.
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:GAC32592.1}.
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DR EMBL; BAER01000042; GAC32592.1; -; Genomic_DNA.
DR RefSeq; WP_007104380.1; NZ_BAER01000042.1.
DR AlphaFoldDB; K6ZQN3; -.
DR STRING; 1129793.GPLA_1678; -.
DR OrthoDB; 9807797at2; -.
DR Proteomes; UP000006322; Unassembled WGS sequence.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR044665; E_coli_cyclophilin_A-like.
DR InterPro; IPR020008; GlyGly_CTERM.
DR NCBIfam; TIGR03501; GlyGly_CTERM; 1.
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 PRINTS; PR00153; CSAPPISMRASE.
DR SUPFAM; SSF50891; Cyclophilin-like; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU363019};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|RuleBase:RU363019};
KW Signal {ECO:0000256|RuleBase:RU363019}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|RuleBase:RU363019"
FT CHAIN 25..259
FT /note="Peptidyl-prolyl cis-trans isomerase"
FT /evidence="ECO:0000256|RuleBase:RU363019"
FT /id="PRO_5006527438"
FT DOMAIN 33..188
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
SQ SEQUENCE 259 AA; 26761 MW; D44CA074FA542032 CRC64;
MRLKFSTLAV VAALTSVSVG QANATEVQIK TVLGNVNVNL FDTATPQTVA NFLSYVNSGA
YANNVVHRSE PNFVVQAGGF QYNNSLPLDN VPTGTAVQNE PELSNVRGTI AMAKLGGSVN
SATSQWFINV SNNSANLDVQ NGGFTVFGQV LGDGMDIIDA IAALERFNLG GAASAAPLRN
YTQADATAGV DITDEHLVLI SDVVVTDAAT VTHAELTPTA NTLIEQDNGG SSSGGSGGSA
GFWGLLGLAV LGIRRRIFS
//
