ID A0A420XFK1_9PAST Unreviewed; 239 AA.
AC A0A420XFK1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU003915};
DE EC=5.2.1.8 {ECO:0000256|RuleBase:RU003915};
GN ORFNames=DES31_1614 {ECO:0000313|EMBL:RKR71278.1};
OS Otariodibacter oris.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Otariodibacter.
OX NCBI_TaxID=1032623 {ECO:0000313|EMBL:RKR71278.1, ECO:0000313|Proteomes:UP000280099};
RN [1] {ECO:0000313|EMBL:RKR71278.1, ECO:0000313|Proteomes:UP000280099}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23800 {ECO:0000313|EMBL:RKR71278.1,
RC ECO:0000313|Proteomes:UP000280099};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (OCT-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 -!- 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|ARBA:ARBA00000971, ECO:0000256|PROSITE-
CC ProRule:PRU00277, ECO:0000256|RuleBase:RU003915};
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family.
CC {ECO:0000256|ARBA:ARBA00006577, ECO:0000256|RuleBase:RU003915}.
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:RKR71278.1}.
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DR EMBL; RBJC01000008; RKR71278.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A420XFK1; -.
DR OrthoDB; 9814548at2; -.
DR Proteomes; UP000280099; 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 Gene3D; 3.10.50.40; -; 1.
DR Gene3D; 1.10.287.460; Peptidyl-prolyl cis-trans isomerase, FKBP-type, N-terminal domain; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR InterPro; IPR000774; PPIase_FKBP_N.
DR InterPro; IPR036944; PPIase_FKBP_N_sf.
DR PANTHER; PTHR43811; FKBP-TYPE PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FKPA; 1.
DR PANTHER; PTHR43811:SF54; FKBP-TYPE PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FKPA; 1.
DR Pfam; PF00254; FKBP_C; 1.
DR Pfam; PF01346; FKBP_N; 1.
DR SUPFAM; SSF54534; FKBP-like; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00277,
KW ECO:0000256|RuleBase:RU003915};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|PROSITE-
KW ProRule:PRU00277}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..239
FT /note="Peptidyl-prolyl cis-trans isomerase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019427667"
FT DOMAIN 150..235
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
FT COILED 81..108
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 239 AA; 26587 MW; FB1CD046943A6BA0 CRC64;
MLKTKLSILA FATSSMFLSQ ITLAEDADTK FIDESSYAVG VLMGKNIEGV IESQKDIFSY
DQDQILAGVQ DTIKKTGKLT DEDLQKQLQA LDNYLQEKEA TIKAEKDKVT IEEGNKFRAD
YEKQDGVKKT TSGLLYKIEK AGEGDSPKAE DTVKVHYKGT LTDGTVFDSS YDRGEPIEFQ
LNQLIPAWIE AIPMLKKGGK MEIVVPPELG YGDREAGQIP ANSTLKFEIE LLDFKPTDK
//
