ID A0A0D0Q2Z0_9RHOB Unreviewed; 615 AA.
AC A0A0D0Q2Z0;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=Periplasmic chaperone PpiD {ECO:0000256|ARBA:ARBA00040743};
DE AltName: Full=Periplasmic folding chaperone {ECO:0000256|ARBA:ARBA00042775};
DE AltName: Full=Rotamase plp {ECO:0000256|ARBA:ARBA00031484};
GN ORFNames=Wenmar_02651 {ECO:0000313|EMBL:KIQ68919.1};
OS Wenxinia marina DSM 24838.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Wenxinia.
OX NCBI_TaxID=1123501 {ECO:0000313|EMBL:KIQ68919.1, ECO:0000313|Proteomes:UP000035100};
RN [1] {ECO:0000313|EMBL:KIQ68919.1, ECO:0000313|Proteomes:UP000035100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24838 {ECO:0000313|EMBL:KIQ68919.1,
RC ECO:0000313|Proteomes:UP000035100};
RA Fiebig A., Goeker M., Klenk H.-P.P.;
RL Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004382}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004382}; Periplasmic side
CC {ECO:0000256|ARBA:ARBA00004382}.
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:KIQ68919.1}.
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DR EMBL; AONG01000012; KIQ68919.1; -; Genomic_DNA.
DR RefSeq; WP_018301552.1; NZ_KN848373.1.
DR AlphaFoldDB; A0A0D0Q2Z0; -.
DR STRING; 1123501.Wenmar_02651; -.
DR PATRIC; fig|1123501.6.peg.2762; -.
DR eggNOG; COG0760; Bacteria.
DR OrthoDB; 9768393at2; -.
DR Proteomes; UP000035100; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:InterPro.
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; 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 inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Isomerase {ECO:0000313|EMBL:KIQ68919.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000035100};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 245..363
FT /note="PpiC"
FT /evidence="ECO:0000259|Pfam:PF13145"
SQ SEQUENCE 615 AA; 66425 MW; 725B05A6DD2AC132 CRC64;
MAVGKSASRL GFYLIIGLLL VGLAGFGATN ISSGGRTTLA AVGEEEITMQ QYANALNDRL
RAFEQTIGQP VTMELARQLG LDQAVLQGLV IEAALDDEAD EMGLSVGDAE VRERVLARPE
FQGLDGQFDR DIYGQRLDSI GLTEGEFETQ IRDDSARAIL QAAVIGGVPR PEAYAATVAE
WIGQRRSPTF VRITEGDLAE PPAPPTDEEI AAYWEENPDL FTTPEVRHIS YAWLTPEMLA
ETIEIPEEDL RARYEERLAE FVQPERRLVE RLVLSTQEVA EEARAALDAG ETDFETLVSN
RGLALSDVDL GDVAEDDLGA AGPDVFAAQP GEVVGPLETP VGPALFRVNA ILSAQEIPFE
EAAEDLRAEV ANERAIRLID SETDGLADLI AGGADLDDLV ANSSLEAGQI DWTDGTSEGI
AAYDEFRQAA AAAEQGAYPE IATLEDGGVF ALRLDEVTEP QVRPLDEVRD EVAAALDEAR
TREAVLARAE EIATDIRESG AFRVPGRNPR TQLGIGRRDF LEGLPRDFVS AVFEMDRGEV
RTVPTEDGVI VVRLDGISAA DEGSETVAAE RQQIAERTGQ SIAQDIYGAF ATAVQQDTDI
RIDDAAVNAV LTQFQ
//
