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Database: UniProt
Entry: E1TCX8_BURSG
LinkDB: E1TCX8_BURSG
Original site: E1TCX8_BURSG 
ID   E1TCX8_BURSG            Unreviewed;       304 AA.
AC   E1TCX8;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   SubName: Full=PpiC-type peptidyl-prolyl cis-trans isomerase {ECO:0000313|EMBL:ADN58193.1};
GN   OrderedLocusNames=BC1003_2240 {ECO:0000313|EMBL:ADN58193.1};
OS   Burkholderia sp. (strain CCGE1003).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=640512 {ECO:0000313|EMBL:ADN58193.1};
RN   [1] {ECO:0000313|EMBL:ADN58193.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CCGE1003 {ECO:0000313|EMBL:ADN58193.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Daligault H., Davenport K., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G.,
RA   Martinez-Romero E., Rogel M.A., Auchtung J., Tiedje J.M., Woyke T.;
RT   "Complete sequence of chromosome1 of Burkholderia sp. CCGE1003.";
RL   Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the PpiC/parvulin rotamase family.
CC       {ECO:0000256|ARBA:ARBA00007656}.
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DR   EMBL; CP002217; ADN58193.1; -; Genomic_DNA.
DR   AlphaFoldDB; E1TCX8; -.
DR   STRING; 640512.BC1003_2240; -.
DR   KEGG; bgf:BC1003_2240; -.
DR   eggNOG; COG0760; Bacteria.
DR   HOGENOM; CLU_034646_1_1_4; -.
DR   OrthoDB; 8929268at2; -.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.50.40; -; 1.
DR   Gene3D; 1.10.4030.10; Porin chaperone SurA, peptide-binding domain; 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; PF13145; Rotamase_2; 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:ADN58193.1};
KW   Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           34..304
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007913410"
FT   DOMAIN          160..259
FT                   /note="PpiC"
FT                   /evidence="ECO:0000259|PROSITE:PS50198"
SQ   SEQUENCE   304 AA;  32642 MW;  CD2C0FF1ED4FED01 CRC64;
     MKHRPIAVTI RNATLFVMLA AAGLAVGTPV AQAANKPSTK PSAEKSVEAA PGPLPANAVA
     RVNNVVITQA QLDDAVRASN APDTPTLRAS IKNQMIAREL FRQAAEKQHY ESRPQVVAAV
     EQAKSAAMTA AYLRDQVKPA PVTDADVKAK YDAIVATLGE FEYKPSAIAV KDADTAQTVL
     TQLKKGTDFA QLAKQYSQGP GAAQGGALNW ISFRTPIQPG NTQNWPQPLA EALVKLPQGG
     VSSAPVQVGD AFWILRVDEK RPTQVPQYDQ IKDTLRKQLE QVALQKATAQ VVVDLMKNAR
     IQQQ
//
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