UniProt: A0A1R0WNX5

Database: UniProt
Entry: A0A1R0WNX5_9BACL

LinkDB:  A0A1R0WNX5_9BACL 
Original site:  A0A1R0WNX5_9BACL

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Ontology (2)   
   GO (2)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (4)   
   EMBL (4)   
Protein domain (8)   
   InterPro (5)   
   Pfam (1)   
   PROSITE (2)   
All databases (18)   

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ID   A0A1R0WNX5_9BACL        Unreviewed;       143 AA.
AC   A0A1R0WNX5;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
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=BJP51_05230 {ECO:0000313|EMBL:OMD23580.1}, BSK60_12805
GN   {ECO:0000313|EMBL:OME14298.1}, BSO21_29275
GN   {ECO:0000313|EMBL:OMD09788.1}, CA596_08360
GN   {ECO:0000313|EMBL:OZQ77191.1};
OS   Paenibacillus odorifer.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=189426 {ECO:0000313|EMBL:OMD09788.1, ECO:0000313|Proteomes:UP000187158};
RN   [1] {ECO:0000313|EMBL:OMD09788.1, ECO:0000313|Proteomes:UP000187158}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSL F4-0242 {ECO:0000313|EMBL:OME14298.1,
RC   ECO:0000313|Proteomes:UP000187446}, FSL H7-0433
RC   {ECO:0000313|EMBL:OMD09788.1, ECO:0000313|Proteomes:UP000187158}, and
RC   FSL H7-0604 {ECO:0000313|EMBL:OMD23580.1,
RC   ECO:0000313|Proteomes:UP000187465};
RA   Beno S.M.;
RT   "Paenibacillus species isolates.";
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:OZQ77191.1, ECO:0000313|Proteomes:UP000216042}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VTT E-133288 {ECO:0000313|EMBL:OZQ77191.1,
RC   ECO:0000313|Proteomes:UP000216042};
RA   Marjamaa K., Vikman M., Arvas M., Salavirta H., Storgards E., Itavaara M.;
RT   "Xylanolytic bacteria in gas generation experiment (Olkiluoto, Finland).";
RL   Submitted (MAY-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|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}.
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:OMD09788.1}.
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DR   EMBL; MPVP01000361; OMD09788.1; -; Genomic_DNA.
DR   EMBL; MKQP01000056; OMD23580.1; -; Genomic_DNA.
DR   EMBL; MPTN01000008; OME14298.1; -; Genomic_DNA.
DR   EMBL; NFUZ01000008; OZQ77191.1; -; Genomic_DNA.
DR   RefSeq; WP_036676135.1; NZ_NFUZ01000008.1.
DR   AlphaFoldDB; A0A1R0WNX5; -.
DR   STRING; 189426.PODO_20950; -.
DR   GeneID; 31572632; -.
DR   KEGG; pod:PODO_20950; -.
DR   eggNOG; COG0652; Bacteria.
DR   OrthoDB; 9807797at2; -.
DR   Proteomes; UP000187158; Unassembled WGS sequence.
DR   Proteomes; UP000187446; Unassembled WGS sequence.
DR   Proteomes; UP000187465; Unassembled WGS sequence.
DR   Proteomes; UP000216042; 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   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:OMD09788.1};
KW   Rotamase {ECO:0000256|RuleBase:RU363019}.
FT   DOMAIN          10..130
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50072"
SQ   SEQUENCE   143 AA;  15242 MW;  00FC8BFC7650AAB9 CRC64;
     MAKQAKITLE NGGVVLLDLF DQDAPNTVAN FEKLAKEGFY NGLTFHRVIP GFVAQGGCPN
     GTGSGGPGYT INCEINPNKH ERGTLAMAHA GKNTGGSQFY ICYAPQPHLD GVHTVFGKVV
     EGMDLVDAFK GRDKMTSVEI IEA
//

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