ID A0A0Q4G111_9BURK Unreviewed; 639 AA.
AC A0A0Q4G111;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Periplasmic chaperone PpiD {ECO:0000256|ARBA:ARBA00040743};
DE AltName: Full=Periplasmic folding chaperone {ECO:0000256|ARBA:ARBA00042775};
GN ORFNames=ASE76_12155 {ECO:0000313|EMBL:KQM69000.1};
OS Xylophilus sp. Leaf220.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Xylophilus.
OX NCBI_TaxID=1735686 {ECO:0000313|EMBL:KQM69000.1, ECO:0000313|Proteomes:UP000051325};
RN [1] {ECO:0000313|EMBL:KQM69000.1, ECO:0000313|Proteomes:UP000051325}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf220 {ECO:0000313|EMBL:KQM69000.1,
RC ECO:0000313|Proteomes:UP000051325};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQM69000.1, ECO:0000313|Proteomes:UP000051325}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf220 {ECO:0000313|EMBL:KQM69000.1,
RC ECO:0000313|Proteomes:UP000051325};
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:KQM69000.1}.
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DR EMBL; LMKO01000025; KQM69000.1; -; Genomic_DNA.
DR RefSeq; WP_055842115.1; NZ_LMKO01000025.1.
DR AlphaFoldDB; A0A0Q4G111; -.
DR STRING; 1735686.ASE76_12155; -.
DR OrthoDB; 9812372at2; -.
DR Proteomes; UP000051325; 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:KQM69000.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000051325};
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..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 268..371
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 639 AA; 70246 MW; 04C93F638ED88091 CRC64;
MFESIRKHSK IVMIVLFLLI IPSFVLFGVD GYRQSMSASA TVATVDGHDI TQGDWDAAHR
QNIERMRAQS PNVDPRLLDS PEARYSSLER LVRERVLRIA AEQKRILPSD ARLARTLHDD
PGVAALRGPD GKLDMAQYRE ALQRQGMTPE MYESSVRSEL ALRQIIDSVQ ATAFASTGQA
NAALDPFFEK RTIQVAQFKP QDFTAKVSLT DADLQAYYQQ HQQQFRVQEQ ADVEYLVLDL
ESIKKTIVPT EADLRTYYEQ NQAKLAGQEE RRASHILLTV AKDAPAAERD KAKAKADELL
AAARKNPAQF AELARKNSQD PGSAANGGDL DFFARGAMVK PFEDAAFAMK KGEISDVVAS
DFGYHIIMLT DIKAPKVRTF AEMRPELEAE YRQQQAQAKF SEAAETFTNT VYEQAESLQP
AAERLKLTVR TAANVARTPA PGAVGALANP RLLEALFSAD AIEKKRNTEA IEIGPNQLAA
ARIVRHTPAQ TPAFEAVEAR VRELATAQRA AELARKDGEA KLAAWKADPA KASLPAAVTV
SRSDPQQQPR AVVDAAMRVA AAPLPGFEGV DLGAEGYAVV RVNKVEARQP ATGDNQARDR
AQVVQWWSSA EGAAYYELLK EKMKVRIKAD RPAASTVEG
//
