ID A0A0W1QJF0_9SPHN Unreviewed; 661 AA.
AC A0A0W1QJF0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Peptidylprolyl isomerase {ECO:0000313|EMBL:KTF68465.1};
GN ORFNames=ATB93_13840 {ECO:0000313|EMBL:KTF68465.1};
OS Sphingomonas sp. WG.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1592629 {ECO:0000313|EMBL:KTF68465.1, ECO:0000313|Proteomes:UP000052965};
RN [1] {ECO:0000313|EMBL:KTF68465.1, ECO:0000313|Proteomes:UP000052965}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WG {ECO:0000313|EMBL:KTF68465.1,
RC ECO:0000313|Proteomes:UP000052965};
RA Li H., Feng Z., Sun Y., Jiao X., Zhou W., Zhu H.;
RT "Draft Genome Sequence of Sphingomonas sp. WG, a welan gum producing
RT strain.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the PpiD chaperone family.
CC {ECO:0000256|ARBA:ARBA00038408}.
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:KTF68465.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LNOS01000058; KTF68465.1; -; Genomic_DNA.
DR RefSeq; WP_019371027.1; NZ_LNOS01000058.1.
DR AlphaFoldDB; A0A0W1QJF0; -.
DR Proteomes; UP000052965; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR InterPro; IPR000297; PPIase_PpiC.
DR InterPro; IPR027304; Trigger_fact/SurA_dom_sf.
DR PANTHER; PTHR47529; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE D; 1.
DR PANTHER; PTHR47529:SF1; PERIPLASMIC CHAPERONE PPID; 1.
DR Pfam; PF13145; Rotamase_2; 1.
DR Pfam; PF13624; SurA_N_3; 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 Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00278,
KW ECO:0000313|EMBL:KTF68465.1}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000052965};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 247..374
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
FT REGION 435..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 661 AA; 70429 MW; 3BB6465E98E6C8F4 CRC64;
MNPKAWQKSS NERLFMLNAF RKFTKSRYGL VVVFIFLGLL AFAFTAGDVT GLRSSVTGAS
STTLAKVGST QVTEADVRDR IDRLIRNAQA QGQTVTMAQL LAQGGFEAAV SDAITSAAIQ
EFAHESDMRV GKRLIDSIIA NNPQFAGIDG KFSQQTFESL LAQNQIMPGQ FRDALTSQRY
AAWLIGPVTM RAAAPDGVVL PYASMLLERR TGVVGFVQSL AMDPGADPDQ KTLADYYGRN
RTRYLVPERR VVRYALARPE ALQAQAAPTE AEIADAYKKN ANRYAAVEKR TIQLVAAIDQ
GAARKIADAA KGGDIAAAAQ AAGLESRTLD AVDKAAAAKQ VSAPFADAAF AAPANAVQGP
VRLGASWYVY RVSKTETTAA RSLDQVRGEL TEEVRKRKLA ALLAETRQSI EDGIGDGKTF
EEAVRDAKLT AASTPALTAA GTNPDTPDTP ADPNLTAITK AGFGFEQAGD EPQVVPVGED
GGFAVVSLER IVPAAPRPLA QITEKVKADY LLDQALAKAR AAATAMLPKL QKGVPMAQAL
AEAGVTKGAA PKPFDLKRSE LRDKENFVQM AFDMPAKTAR LVEAPNRAGY YVVYVDTIQP
GNATGDAAAI APLRNALNQL GAAEYERQFS AAVAKAVTIR RNENAIARLR ADLQRQGAGG
Q
//
