ID A0A2A4W310_9PROT Unreviewed; 645 AA.
AC A0A2A4W310;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=COB37_01250 {ECO:0000313|EMBL:PCI64471.1};
OS Kordiimonadales bacterium.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Kordiimonadales.
OX NCBI_TaxID=2030814 {ECO:0000313|EMBL:PCI64471.1, ECO:0000313|Proteomes:UP000217879};
RN [1] {ECO:0000313|Proteomes:UP000217879}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Tully B.J., Wheat C.G., Glazer B.T., Huber J.A.;
RT "A dynamic microbial community with high functional redundancy inhabits the
RT cold, oxic subseafloor aquifer.";
RL Submitted (AUG-2017) 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:PCI64471.1}.
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DR EMBL; NVTU01000003; PCI64471.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A4W310; -.
DR Proteomes; UP000217879; Unassembled WGS sequence.
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; 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
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 248..372
FT /note="PpiC"
FT /evidence="ECO:0000259|Pfam:PF13145"
SQ SEQUENCE 645 AA; 70349 MW; 49AA7E1FFB8B6D82 CRC64;
MLLKLRGGLD SFFVTILLGL LIGAFAIFGI GPSMLNSGNQ SVATVGDTNV STQSYVRQVN
SRAQQLQNQF GGQFTSAQII NLMQLDQQIL NQMIAEAAIT EHLGSLSMRA GDQEIRSALQ
EIDGFVLPDG TLSKDLIEQA LQRTGLSRVE FMTDVRQGIS RQQLFESLAS ENAMPPKFAE
ALYIWQAERR RATLIDIKAA DMIDIPTPTD EDLQTYYDEN IDAYKTAALR TYNYILVTPA
QFVDGIEVEE KDVLEQFEAN NSLYNKPEQR VLQQVSFNDK AGADAFLTAV NAGADFVEAG
ASVTDFTIEE IELGTFAKEA VVTEYSESTA NLIFALEDGG STEAVRGYSG WSVFRVAGIT
PAETKTLEDV RPEIEQALKE YQADGLMQDA IDKIYKAGID DGSPTLAAVA EETGLTLATV
SNVTSQGRSA SSELKLTQQN EYVILNRAYG IDIGDELGVT DIDPRDRAKG LFLVEVTDIK
DPEQRPLEDV KGDLTSAWTA VKRLEKAGEV AELARTRLAA GEKPEDVIAA IGGTSFVAKN
VSRTAQAGSS LALNIRDLIF DLPTGSIDFE RSADGNGYIV VRVDDVTAGD PLKGVVAIET
LITRLNGELA NEIYAQYQAY LLAEYPVSIN RTLQQSLFSE QNQQQ
//