ID A0A0A7PH24_9SPHN Unreviewed; 446 AA.
AC A0A0A7PH24;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
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 ORFNames=SKP52_12650 {ECO:0000313|EMBL:AJA09421.1};
OS Sphingopyxis fribergensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=1515612 {ECO:0000313|EMBL:AJA09421.1, ECO:0000313|Proteomes:UP000030907};
RN [1] {ECO:0000313|EMBL:AJA09421.1, ECO:0000313|Proteomes:UP000030907}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Kp5.2 {ECO:0000313|EMBL:AJA09421.1,
RC ECO:0000313|Proteomes:UP000030907};
RX PubMed=26040579; DOI=10.1099/ijs.0.000371;
RA Oelschlagel M., Ruckert C., Kalinowski J., Schmidt G., Schlomann M.,
RA Tischler D.;
RT "Description of Sphingopyxis fribergensis sp. nov. - a soil bacterium with
RT the ability to degrade styrene and phenylacetic acid.";
RL Int. J. Syst. Evol. Microbiol. 65:3008-3015(2015).
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DR EMBL; CP009122; AJA09421.1; -; Genomic_DNA.
DR RefSeq; WP_052208216.1; NZ_CP009122.1.
DR AlphaFoldDB; A0A0A7PH24; -.
DR STRING; 1515612.SKP52_12650; -.
DR KEGG; sphk:SKP52_12650; -.
DR HOGENOM; CLU_034646_11_4_5; -.
DR OrthoDB; 9791746at2; -.
DR Proteomes; UP000030907; 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; -; 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; 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; 1.
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; PS50198; PPIC_PPIASE_2; 1.
PE 4: Predicted;
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00278,
KW ECO:0000313|EMBL:AJA09421.1}; 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..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..446
FT /note="Parvulin-like PPIase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007760837"
FT DOMAIN 197..294
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 446 AA; 47745 MW; E11F4D9A434B8E96 CRC64;
MTKFSTMTGL IALAAVGVTP VLAQTVADSD VPTTSLNIPG NVQLFGDAKP NVYRPSATVN
GEIITATDIE QRMALIRIAN NNVELPPEEI QRLRSQVFSN LIDEKLQIQE AKAADITIDE
NVVNDQFARL ATRFKQTPEQ FSTYLVSKGS SAAAVKQQIR GEFAWDRLLS RNIQSTTNVS
TEEVDLIVKQ MEATKGQDEF HLGEIYLSTT PETAPAVAEN AKKIIQALQA GGSFAAYARQ
FSEASTAVVG GDLGWVKAGQ LPGSMGEAAT QMQPGQLVGP VEVPGGVSIM LMIDRRQVLT
ADPRDAILSL KQISLDFPAG TTPAKASELA GQFAEKTRGI AGCGAADAVA QSLGASVVSR
DNIEMRALPA PLQATLANLQ VGQTTQPFGA ANEGVSVLVL CGRDLPQTAT APNLEQIEQK
LLEDKVNKRA QRYLRDLRRD AVIEYS
//
