ID A0A0Q5PPQ4_9BURK Unreviewed; 644 AA.
AC A0A0Q5PPQ4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Periplasmic chaperone PpiD {ECO:0000256|ARBA:ARBA00040743};
DE AltName: Full=Periplasmic folding chaperone {ECO:0000256|ARBA:ARBA00042775};
GN ORFNames=ASG35_23660 {ECO:0000313|EMBL:KQR87127.1};
OS Burkholderia sp. Leaf177.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=1736287 {ECO:0000313|EMBL:KQR87127.1, ECO:0000313|Proteomes:UP000051826};
RN [1] {ECO:0000313|EMBL:KQR87127.1, ECO:0000313|Proteomes:UP000051826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf177 {ECO:0000313|EMBL:KQR87127.1,
RC ECO:0000313|Proteomes:UP000051826};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQR87127.1, ECO:0000313|Proteomes:UP000051826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf177 {ECO:0000313|EMBL:KQR87127.1,
RC ECO:0000313|Proteomes:UP000051826};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KQR87127.1}.
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DR EMBL; LMPF01000002; KQR87127.1; -; Genomic_DNA.
DR RefSeq; WP_056353202.1; NZ_LMPF01000002.1.
DR AlphaFoldDB; A0A0Q5PPQ4; -.
DR OrthoDB; 9812372at2; -.
DR Proteomes; UP000051826; 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: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; PF13616; Rotamase_3; 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 Isomerase {ECO:0000256|PROSITE-ProRule:PRU00278,
KW ECO:0000313|EMBL:KQR87127.1}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000051826};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 269..374
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 644 AA; 69366 MW; B408E9D70847064E CRC64;
MLDFFRNHQR LMMALLILIV VPGLGIVGVQ GFSSFFDENA NVASVNGHKI TRAEYDGAMR
QQVDRARQML GAQFDPKMFE SPQMRASLID SLVQQRVLAD ETQRLHLTAS DQAVRRALLA
DPTIASLRKP DGSIDLDQYK QLLAMQGITP EQYDERVRYG LATDQLPSSI QSTAFTSKTL
AQSLTEIAEQ RRDVQGLAFR TADYTAKIQP TDAQLKAYYD AHSAELKTPE SASIQYLVMS
PATLATAIKP TDADLKKYYD DNIARFKTQA EVRASHILIT APKDASAADK AKAKAQADAL
LAQVKAHPDQ FAQIAQKESQ DPGSASKGGD LGYFSHGMIA GGKAFDDAAF GLKKGEISGV
VQTDFGYHII QATDVKPSAT QSFDEVKDQI TRDVTAAQAA KNLADEAEGF TSLVYEKSKT
LQPAADKYKL QIQTATVGPK PDPKLPADSP LNNPKVLNAI FAADAVKERN NTQAIDIGNS
TLVAARVTDY KPSAVPALDT IKDAVRTKVI AEQAAEMARK DGAAKLAAVQ KSNSTDGFSS
VAKVSRNDAQ GVPPAALAAI FKADSSKLPT YVGVDLGADG YAIYRVNGIE KPEPVAADRL
TGAQQQVAQV YAQAEMESYL DALKARSKVK INAPTSNAPA EQPQ
//
