ID A0A0S2DKL8_LYSEN Unreviewed; 168 AA.
AC A0A0S2DKL8;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=BV903_007555 {ECO:0000313|EMBL:UZW62133.1}, D9T17_09615
GN {ECO:0000313|EMBL:ROU07217.1}, FE772_18465
GN {ECO:0000313|EMBL:QCW27327.1}, GLE_3751 {ECO:0000313|EMBL:ALN59095.1};
OS Lysobacter enzymogenes.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=69 {ECO:0000313|EMBL:ALN59095.1, ECO:0000313|Proteomes:UP000061569};
RN [1] {ECO:0000313|EMBL:ALN59095.1, ECO:0000313|Proteomes:UP000061569}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C3 {ECO:0000313|EMBL:ALN59095.1,
RC ECO:0000313|Proteomes:UP000061569};
RA Kobayashi D.Y.;
RT "Genome sequences of Lysobacter enzymogenes strain C3 and Lysobacter
RT antibioticus ATCC 29479.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:UZW62133.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=B25 {ECO:0000313|EMBL:UZW62133.1};
RX PubMed=28473380; DOI=10.1128/genomea.00271-17;
RA Hernandez I., Fernandez C.;
RT "Draft Genome Sequence and Assembly of a Lysobacter enzymogenes Strain with
RT Biological Control Activity against Root Knot Nematodes.";
RL Genome Announc. 5:e00271-e00217(2017).
RN [3] {ECO:0000313|EMBL:ROU07217.1, ECO:0000313|Proteomes:UP000275910}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OH11 {ECO:0000313|EMBL:ROU07217.1,
RC ECO:0000313|Proteomes:UP000275910};
RA Liu F., Zhao Y., Qian G., Chen Y., Xu H.;
RT "The genome of Lysobacter enzymogenes OH11.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:QCW27327.1, ECO:0000313|Proteomes:UP000308311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YC36 {ECO:0000313|EMBL:QCW27327.1,
RC ECO:0000313|Proteomes:UP000308311};
RA Feng T.;
RT "Intraspecies Signal LeDSF and Interspecies Signal Indole Synergistically
RT Regulate the Twitching Motility of Lysobacter enzymogenes.";
RL Submitted (MAY-2019) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:UZW62133.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=B25 {ECO:0000313|EMBL:UZW62133.1};
RA Fernandez G., Fernandez C., Hernandez I.;
RT "Improved assembly of Lysobacter enzymogenes B25.";
RL Submitted (OCT-2022) 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; CP013140; ALN59095.1; -; Genomic_DNA.
DR EMBL; CP040656; QCW27327.1; -; Genomic_DNA.
DR EMBL; RCTY01000023; ROU07217.1; -; Genomic_DNA.
DR EMBL; CP110813; UZW62133.1; -; Genomic_DNA.
DR RefSeq; WP_057948523.1; NZ_RCTY01000023.1.
DR STRING; 69.GLE_3751; -.
DR KEGG; lez:GLE_3751; -.
DR PATRIC; fig|69.6.peg.3695; -.
DR OrthoDB; 9807797at2; -.
DR Proteomes; UP000061569; Chromosome.
DR Proteomes; UP000190203; Chromosome.
DR Proteomes; UP000275910; Unassembled WGS sequence.
DR Proteomes; UP000308311; 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, ECO:0000313|EMBL:ALN59095.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000061569};
KW Rotamase {ECO:0000256|RuleBase:RU363019}.
FT DOMAIN 1..131
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
SQ SEQUENCE 168 AA; 18113 MW; 38CCE54FB1ED9707 CRC64;
MSLIATFDTS RGPIRVELNA EKAPLTVANF VNLAQRGFYD GLNFHRVIPN FMIQGGCPQG
TGTGGPGYRF EDETRNGLGH QRGVLSMANA GPGTNGSQFF ITHIVCDWLD GKHTVFGKVL
EGQEIVDTVQ QGDKLNSVKI EGDTAAVLAA KAERVAEWNK VLDANARP
//