ID D5VH36_CAUST Unreviewed; 452 AA.
AC D5VH36;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Parvulin-like PPIase {ECO:0000256|ARBA:ARBA00018370};
DE AltName: Full=Peptidyl-prolyl cis-trans isomerase plp {ECO:0000256|ARBA:ARBA00030642};
DE AltName: Full=Rotamase plp {ECO:0000256|ARBA:ARBA00031484};
GN OrderedLocusNames=Cseg_2292 {ECO:0000313|EMBL:ADG10754.1};
OS Caulobacter segnis (strain ATCC 21756 / DSM 7131 / JCM 7823 / NBRC 15250 /
OS LMG 17158 / TK0059) (Mycoplana segnis).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=509190 {ECO:0000313|EMBL:ADG10754.1, ECO:0000313|Proteomes:UP000002629};
RN [1] {ECO:0000313|Proteomes:UP000002629}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 21756 / DSM 7131 / JCM 7823 / NBRC 15250 / LMG 17158 /
RC TK0059 {ECO:0000313|Proteomes:UP000002629};
RX PubMed=21705585; DOI=10.1128/JB.05453-11;
RG US DOE Joint Genome Institute;
RA Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.;
RT "Genome sequences of eight morphologically diverse alphaproteobacteria.";
RL J. Bacteriol. 193:4567-4568(2011).
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DR EMBL; CP002008; ADG10754.1; -; Genomic_DNA.
DR RefSeq; WP_013079408.1; NC_014100.1.
DR AlphaFoldDB; D5VH36; -.
DR STRING; 509190.Cseg_2292; -.
DR KEGG; cse:Cseg_2292; -.
DR eggNOG; COG0760; Bacteria.
DR HOGENOM; CLU_034646_11_4_5; -.
DR Proteomes; UP000002629; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-KW.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.10.50.40; -; 2.
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; IPR023058; PPIase_PpiC_CS.
DR InterPro; IPR015391; SurA_N.
DR InterPro; IPR027304; Trigger_fact/SurA_dom_sf.
DR PANTHER; PTHR47637; CHAPERONE SURA; 1.
DR PANTHER; PTHR47637:SF1; CHAPERONE SURA; 1.
DR Pfam; PF00639; Rotamase; 2.
DR Pfam; PF09312; SurA_N; 1.
DR SUPFAM; SSF54534; FKBP-like; 2.
DR SUPFAM; SSF109998; Triger factor/SurA peptide-binding domain-like; 1.
DR PROSITE; PS01096; PPIC_PPIASE_1; 1.
DR PROSITE; PS50198; PPIC_PPIASE_2; 2.
PE 4: Predicted;
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00278,
KW ECO:0000313|EMBL:ADG10754.1}; Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..452
FT /note="Parvulin-like PPIase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007913225"
FT DOMAIN 207..305
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
FT DOMAIN 301..409
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 452 AA; 48632 MW; 4E4AAADB161C4883 CRC64;
MRSARSVTTF AAGAASILAL TAASFAPHAL AQDQAGAPPQ VEAPAAAPQA AAPAPLSESV
AAVVNDDIIS SYDLMQRMRL LMATSGMQPT QENLPQIQQE ALRSLIDERL QMQELRRVEK
QQKITIISTD KEVDEQVADI AQSNKMTSDQ LKQSLVQQGI GLDTWRAQLR ADSSWQSWIQ
GRYGSRLRIG EDQIKAYQRR LAESAAKPQY QISEVFLDAS RVGGMEVAVN GAAQLIAQMQ
QGAPFAAVAR QFSGSATAAN GGDVGWVNQG EMPTEVDEAL EQLRPGQLSR PIQVKDGVYI
IYLRDKRAGS KTAIVDLKQV AAPLPADATE AQVAAATKLL TDLRPKINSC QTLETVAGKV
DGLVAGDLGE AEITDLAPAF QEAASKLDIG QISDPIRTDA GLHLIAVCGK RQGGANAPTH
DQIENRLRGQ QLALISKRYL RDLRNQATIE TR
//
