ID A0A238LGF0_9RHOB Unreviewed; 614 AA.
AC A0A238LGF0;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Peptidyl-prolyl cis-trans isomerase D {ECO:0000313|EMBL:SMY07970.1};
DE EC=5.2.1.8 {ECO:0000313|EMBL:SMY07970.1};
GN Name=ppiD {ECO:0000313|EMBL:SMY07970.1};
GN ORFNames=LOM8899_02115 {ECO:0000313|EMBL:SMY07970.1};
OS Flavimaricola marinus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Flavimaricola.
OX NCBI_TaxID=1819565 {ECO:0000313|EMBL:SMY07970.1, ECO:0000313|Proteomes:UP000201613};
RN [1] {ECO:0000313|EMBL:SMY07970.1, ECO:0000313|Proteomes:UP000201613}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8899 {ECO:0000313|EMBL:SMY07970.1,
RC ECO:0000313|Proteomes:UP000201613};
RA Song R., Chenine A.L., Ruprecht R.M.;
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the PpiD chaperone family.
CC {ECO:0000256|ARBA:ARBA00038408}.
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; FXZK01000003; SMY07970.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A238LGF0; -.
DR OrthoDB; 9768393at2; -.
DR Proteomes; UP000201613; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:InterPro.
DR Gene3D; 1.10.4030.10; Porin chaperone SurA, peptide-binding domain; 1.
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; SSF54534; FKBP-like; 1.
DR SUPFAM; SSF109998; Triger factor/SurA peptide-binding domain-like; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Isomerase {ECO:0000313|EMBL:SMY07970.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000201613};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 9..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 243..361
FT /note="PpiC"
FT /evidence="ECO:0000259|Pfam:PF13145"
SQ SEQUENCE 614 AA; 65614 MW; 381AF71BCCD39294 CRC64;
MAKGKGSRIG VWIILGLLFV GLIGFGTTNL SGNIRSIGSA GDKDIGVQTY ANALTQQIDA
FSAQLGQPLS FPQAQAFGID RAVLSQVVST AVLDNEVAQL GVSVGDERVA ERVVQIPAFQ
GISGSFDREA YRFTLDRNGL TEREFESGLR DDMARTLLQS AVLGGIPEAE VYADTMLNFV
GERRSFDWAP LTADILTDPL PAPTEEDMLA QYEATPEAYT APEIRKITYA AILPEMIQDE
VEVDDTAVRE LYDARINDYV QPERRLVERL VFGNEAQAND AMASLTAGET DFDTLVSDRG
LDLADVDLGD VAADDLGAAS EAVFGAAPGD VVGPVMTSLG PALFRMNAIL GAEEISFEEA
APDLRAELGR DRARRVIAGE YDRIIDLIAG GAAIEDLAEQ TRLELGTIDW SEEVSDGIAA
YDLFRQQAMA TEVGAFPELS ELDDGGLFTL RVDEIVAPAL RPLDEVREQV IADRVDRATA
EAVGAVGAEL QAQVGNGAAM SDLGLSVTSE ANAIRRNFIP DTPQGLMAEV FDMALGEARV
ISDETGLTVL VHLTDIAPVD MDDPTMAAEA EAIAARTSQG IAQDIYSIFT ASVQARTDVS
INQAAITAVH ANYQ
//
