ID A0A1L9NXZ5_9RHOB Unreviewed; 615 AA.
AC A0A1L9NXZ5;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Peptidyl-prolyl cis-trans isomerase D {ECO:0000313|EMBL:OJI94168.1};
DE EC=5.2.1.8 {ECO:0000313|EMBL:OJI94168.1};
GN Name=ppiD {ECO:0000313|EMBL:OJI94168.1};
GN ORFNames=PFRI_16080 {ECO:0000313|EMBL:OJI94168.1};
OS Planktotalea frisia.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Planktotalea.
OX NCBI_TaxID=696762 {ECO:0000313|EMBL:OJI94168.1, ECO:0000313|Proteomes:UP000184514};
RN [1] {ECO:0000313|EMBL:OJI94168.1, ECO:0000313|Proteomes:UP000184514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH6-1 {ECO:0000313|EMBL:OJI94168.1,
RC ECO:0000313|Proteomes:UP000184514};
RA Poehlein A., Bakenhus I., Voget S., Brinkhoff T., Simon M.;
RT "Genome sequence of Planktotalea frisia SH6-1.";
RL Submitted (OCT-2016) 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:OJI94168.1}.
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DR EMBL; MLCB01000117; OJI94168.1; -; Genomic_DNA.
DR RefSeq; WP_072630192.1; NZ_QKZM01000029.1.
DR AlphaFoldDB; A0A1L9NXZ5; -.
DR STRING; 696762.PFRI_16080; -.
DR OrthoDB; 9768393at2; -.
DR Proteomes; UP000184514; 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:OJI94168.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000184514};
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..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 245..364
FT /note="PpiC"
FT /evidence="ECO:0000259|Pfam:PF13145"
SQ SEQUENCE 615 AA; 66259 MW; 7B51990B8B5A58C0 CRC64;
MAVRGNTISK TFIWILLALL IVGLAGFGAT SLGGNIRTIG SVGDKPISVE LYSRTLQEDL
RAISAQAGQN VPFSTAQALG VDRQSLARVV TSRALDHETA QLGLSVGDAQ LQEQILGMSA
FQGINGQFDR EAYRFTLENA GLNEAAFEES LREEAARTLV QGAILSGTTV PSSYADTIVA
YIGERRNATV ARLKAADLAE PVADPSGEQL KAYYDENIEN YALPQTKKIT YAWLSPDMIT
DTVEVDESML QAAYDERDAE FNKTERRLVE RLVFGTQDDA NSAKAQLEAG GTTFEALVED
RGLSLVDVDL GDMTLSALEG AGDAVFAGET GDVVGPLPSD LGPALFRING ILAAQNTSFE
DAKPQLRDEL AADRARRVVE AQMSDIDDLL AGGATLEDLA KETDMELGQI DWTPEAEDGL
AAYEAFRDVA RSVSDEDFPE VEILEDGGIF ALRLDETLEP RPQPLDEITE RVTLGWRTAA
TLDALRAEAE ALLPQITSDS DFADVDLEAE TLTELTRTGF VEAMPPAAIL ALFEAERGAT
VVVDDVTDVL IVRLEDVLAA DEDSDDVKRL RAQLTSQASS AVAQDLFDAF ATDIQQRAGI
TLDQNALNAV HANFN
//