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Database: UniProt
Entry: A0A0D1EIC6_9RHOB
LinkDB: A0A0D1EIC6_9RHOB
Original site: A0A0D1EIC6_9RHOB 
ID   A0A0D1EIC6_9RHOB        Unreviewed;       622 AA.
AC   A0A0D1EIC6;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
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   Name=ppiD {ECO:0000313|EMBL:KIT17349.1};
GN   ORFNames=jaqu_10810 {ECO:0000313|EMBL:KIT17349.1};
OS   Jannaschia aquimarina.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Jannaschia.
OX   NCBI_TaxID=935700 {ECO:0000313|EMBL:KIT17349.1, ECO:0000313|Proteomes:UP000032232};
RN   [1] {ECO:0000313|EMBL:KIT17349.1, ECO:0000313|Proteomes:UP000032232}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GSW-M26 {ECO:0000313|EMBL:KIT17349.1,
RC   ECO:0000313|Proteomes:UP000032232};
RA   Voget S., Daniel R.;
RT   "Genome Sequence of Jannaschia aquimarina DSM28248, a member of the
RT   Roseobacter clade.";
RL   Submitted (FEB-2015) 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:KIT17349.1}.
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DR   EMBL; JYFE01000020; KIT17349.1; -; Genomic_DNA.
DR   RefSeq; WP_043917908.1; NZ_JYFE01000020.1.
DR   AlphaFoldDB; A0A0D1EIC6; -.
DR   STRING; 935700.jaqu_10810; -.
DR   PATRIC; fig|935700.4.peg.1127; -.
DR   OrthoDB; 9768393at2; -.
DR   Proteomes; UP000032232; 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: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; 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.
DR   PROSITE; PS50198; PPIC_PPIASE_2; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Isomerase {ECO:0000256|PROSITE-ProRule:PRU00278,
KW   ECO:0000313|EMBL:KIT17349.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032232};
KW   Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
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..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          266..353
FT                   /note="PpiC"
FT                   /evidence="ECO:0000259|PROSITE:PS50198"
FT   COILED          368..395
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   622 AA;  66474 MW;  13F77100A2CC635F CRC64;
     MAEEGARRKK KGNVVIWAVL GLLILALGGF GIGGFGSSQQ SVASVGDRDI SASDYGNALQ
     QEQARIGRQF GQSLTVDQMR ALGLDQLVME RLLAGAALDN DADQLGVSVG DAEVAQRLRA
     IPAFQSAAGF DREVYQDVLR RQGTNPRNFE AALRDEAARE ILQAAIVGVT EPPEGYATTI
     ANWLEETRDI TVAEVTAAQL QAGPAAPTDE DLETYLQDNS RRFETPERRR VTYAWASPDI
     VAEGIDVDEA DARALYEQRI DRYRIPARVL AERLVFADEA AAQAAADAVA AGETDFDTLV
     MERGLTLDDV DQGEIAEADV DAPVRDALFA LEEPGIAGPV ETSLGPALFR VNAILDPQET
     PFEDVQDKLA AEAALDEARR EIDAAREAID DLMAGGATLE EVAADTIMEV GTLELDPSIS
     EGIAGYEAFR TAVSAAEVDD FPELFDLSDG GLAAIRLDGI DEPMLPALAD IRAQVEAAWQ
     SDSLQRRLAE RAEALAERLR EGESFEDLGL SADSVTGIER DGGVANASRD LVDTVFAAED
     GAILAEPGDE TRAYVIRIDG VTRPDLESPD SAELVEAIEA TARRDIGADL LTGYTAAARD
     AAGFEVNANA IRAIQSQVMG VR
//
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