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Database: UniProt
Entry: A0A0W0VBP2_9GAMM
LinkDB: A0A0W0VBP2_9GAMM
Original site: A0A0W0VBP2_9GAMM 
ID   A0A0W0VBP2_9GAMM        Unreviewed;       163 AA.
AC   A0A0W0VBP2;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
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=ppiB {ECO:0000313|EMBL:KTD17556.1};
GN   ORFNames=Ljor_1862 {ECO:0000313|EMBL:KTD17556.1};
OS   Legionella jordanis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=456 {ECO:0000313|EMBL:KTD17556.1, ECO:0000313|Proteomes:UP000055035};
RN   [1] {ECO:0000313|EMBL:KTD17556.1, ECO:0000313|Proteomes:UP000055035}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BL-540 {ECO:0000313|EMBL:KTD17556.1,
RC   ECO:0000313|Proteomes:UP000055035};
RA   Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA   Pupko T., Shuman H.A., Segal G.;
RT   "Genomic analysis of 38 Legionella species identifies large and diverse
RT   effector repertoires.";
RL   Submitted (NOV-2015) 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:KTD17556.1}.
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DR   EMBL; LNYJ01000011; KTD17556.1; -; Genomic_DNA.
DR   RefSeq; WP_058471301.1; NZ_RDQQ01000012.1.
DR   AlphaFoldDB; A0A0W0VBP2; -.
DR   STRING; 456.Ljor_1862; -.
DR   PATRIC; fig|456.5.peg.1987; -.
DR   OrthoDB; 9807797at2; -.
DR   Proteomes; UP000055035; 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; cd01920; cyclophilin_EcCYP_like; 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; IPR044665; E_coli_cyclophilin_A-like.
DR   PANTHER; PTHR43246:SF11; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE B; 1.
DR   PANTHER; PTHR43246; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE CYP38, CHLOROPLASTIC; 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:KTD17556.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000055035};
KW   Rotamase {ECO:0000256|RuleBase:RU363019}.
FT   DOMAIN          1..162
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50072"
SQ   SEQUENCE   163 AA;  18121 MW;  713B93DF37C0B4AA CRC64;
     MIVIRTSKGD IHVQLDEENT PLTAENFLNY VREGFYDNTI FHRVIDGFMI QGGGLTADMR
     QKSTQSPVKN EAKSAKPNKR GTIAMARTMD PHSATSQFFI NVADNAFLNF TGEHAQGYGY
     CVFGEVVDGM DVVDAIVKVK TGQRMGHADV PVEDIVIHEI REE
//
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