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Database: UniProt
Entry: A0A1V3S818_9BURK
LinkDB: A0A1V3S818_9BURK
Original site: A0A1V3S818_9BURK 
ID   A0A1V3S818_9BURK        Unreviewed;       259 AA.
AC   A0A1V3S818;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Peptidylprolyl isomerase {ECO:0000313|EMBL:OOG85238.1};
GN   ORFNames=B0E41_09105 {ECO:0000313|EMBL:OOG85238.1};
OS   Hydrogenophaga sp. A37.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Hydrogenophaga.
OX   NCBI_TaxID=1945864 {ECO:0000313|EMBL:OOG85238.1, ECO:0000313|Proteomes:UP000189189};
RN   [1] {ECO:0000313|EMBL:OOG85238.1, ECO:0000313|Proteomes:UP000189189}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A37 {ECO:0000313|EMBL:OOG85238.1,
RC   ECO:0000313|Proteomes:UP000189189};
RA   Lycus P., Bothun K.L., Bergaust L., Shapleigh J.P., Bakken L.R.,
RA   Frostegard A.;
RT   "Phenotypic and genotypic richness of denitrifiers revealed by a novel
RT   isolation strategy.";
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the PpiC/parvulin rotamase family.
CC       {ECO:0000256|ARBA:ARBA00007656}.
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:OOG85238.1}.
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DR   EMBL; MUNZ01000086; OOG85238.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V3S818; -.
DR   STRING; 1945864.B0E41_09105; -.
DR   OrthoDB; 14196at2; -.
DR   Proteomes; UP000189189; Unassembled WGS sequence.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.50.40; -; 1.
DR   InterPro; IPR046357; PPIase_dom_sf.
DR   InterPro; IPR000297; PPIase_PpiC.
DR   InterPro; IPR027304; Trigger_fact/SurA_dom_sf.
DR   PANTHER; PTHR47245:SF1; FOLDASE PROTEIN PRSA; 1.
DR   PANTHER; PTHR47245; PEPTIDYLPROLYL ISOMERASE; 1.
DR   Pfam; PF13616; Rotamase_3; 1.
DR   SUPFAM; SSF54534; FKBP-like; 1.
DR   SUPFAM; SSF109998; Triger factor/SurA peptide-binding domain-like; 1.
DR   PROSITE; PS50198; PPIC_PPIASE_2; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|PROSITE-ProRule:PRU00278,
KW   ECO:0000313|EMBL:OOG85238.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189189};
KW   Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..259
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012369800"
FT   DOMAIN          129..220
FT                   /note="PpiC"
FT                   /evidence="ECO:0000259|PROSITE:PS50198"
SQ   SEQUENCE   259 AA;  28496 MW;  52EEC30441DBA7A1 CRC64;
     MKFSLSALTA AALIATAPWA VAQNVAIVNG KAVPTARVAA LEQQIVASGR QVDDATRAQI
     KEEVVLREVF MQEAQKRGIA ATADFKTQME LARQTIMIRA LFADYQKKNP VTDAEIKAEY
     DKFTAANGGK EYRARHILVE KEEDAKAIIA AIKGGAKFED QAKAKSKDPG SGANGGDLDW
     ANAASYVTEF SEAMIKLEKG QMTPEPVKSQ FGFHIIRVDD VRQAKLPAFE ELKPQIAQQM
     QQQKLAEYQK TLREKAKVQ
//
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