ID A0A0P0NZ69_9CAUL Unreviewed; 651 AA.
AC A0A0P0NZ69;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=AQ619_08955 {ECO:0000313|EMBL:ALL13467.1};
OS Caulobacter henricii.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=69395 {ECO:0000313|EMBL:ALL13467.1, ECO:0000313|Proteomes:UP000056905};
RN [1] {ECO:0000313|EMBL:ALL13467.1, ECO:0000313|Proteomes:UP000056905}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB4 {ECO:0000313|EMBL:ALL13467.1,
RC ECO:0000313|Proteomes:UP000056905};
RA Scott D., Ely B.;
RT "Conservation of the essential genome among Caulobacter and Brevundimonas
RT species.";
RL Submitted (OCT-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 ---------------------------------------------------------------------------
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; CP013002; ALL13467.1; -; Genomic_DNA.
DR RefSeq; WP_062146493.1; NZ_CP013002.1.
DR AlphaFoldDB; A0A0P0NZ69; -.
DR STRING; 69395.AQ619_08955; -.
DR KEGG; chq:AQ619_08955; -.
DR OrthoDB; 9768393at2; -.
DR Proteomes; UP000056905; Chromosome.
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 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; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000056905};
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..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 256..372
FT /note="PpiC"
FT /evidence="ECO:0000259|Pfam:PF13145"
FT DOMAIN 399..485
FT /note="PpiC"
FT /evidence="ECO:0000259|Pfam:PF13145"
SQ SEQUENCE 651 AA; 69177 MW; 2106C744BBB85295 CRC64;
MLAGFRTFAK SPFAVILFGL LIVSFAVFGI SDVFKGPRLS GVVAAGSRSV SAADFKTRYE
NYRKGTERQS GETLTADQAV ERGIDRQILQ EIALQESMSE VIRKFGIQPS DKLVGNVVRE
QMSNLHPNQR PFDPITGKFD PKMYEALLRE NGMTPDSYQA SISDEIAQTH VFTGVANGLH
APRIYAALQA AYGLESRDLA AFAINPATVE RPGNPTDAQL TAFMKQNAER LTRPESRVLS
IMRVSAQALE PSVTINPADV QKTFDFRKET LATPETRSLV QIVAPDAKAA GVIAQRLAKG
DQPAVVASAF GQKPVILNDK PKSALPDRKV ADAAFSLAAG QVSAPITGSL GISVVKVTKV
TPGAVPSLES VRSQIEAELR VQGAQAKAYE QTQTYQDAHD AGSDLIAAAS KAGAMVMTSA
PITAQGTDQT GQPIPGLTPD ILKTAFDLSS GGESELVEIG KGEYYAVKVE KVIPAALPAL
ADIRPQLAQV WLQNEMTNRL QAKAESLAAR VKKGESLEAV AAAAGSRVQR VPGISRENAQ
QHQGLGRDLL LATFAAKPGE VFSSRAGQMA FVVAKLEAVR SGKIADMARI SQTIRPQVDS
GLMRDLGEAA RLGAQASLKT KTNLTLARQA IGVDTDALAK AEAAKSGKAQ K
//
