ID A0A1F4K736_9BURK Unreviewed; 642 AA.
AC A0A1F4K736;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Periplasmic chaperone PpiD {ECO:0000256|ARBA:ARBA00040743};
DE AltName: Full=Periplasmic folding chaperone {ECO:0000256|ARBA:ARBA00042775};
GN ORFNames=A3F78_08820 {ECO:0000313|EMBL:OGB30394.1};
OS Burkholderiales bacterium RIFCSPLOWO2_12_FULL_61_40.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales.
OX NCBI_TaxID=1797566 {ECO:0000313|EMBL:OGB30394.1, ECO:0000313|Proteomes:UP000178940};
RN [1] {ECO:0000313|EMBL:OGB30394.1, ECO:0000313|Proteomes:UP000178940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGB30394.1}.
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DR EMBL; MESI01000093; OGB30394.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F4K736; -.
DR STRING; 1797566.A3F78_08820; -.
DR Proteomes; UP000178940; 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:OGB30394.1}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 268..371
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 642 AA; 70499 MW; D44351E9740EF169 CRC64;
MFDFVRKHTK VMMFLMFLLI IPAFVLVGVD GFKSINAGGD AVAKVGSHNV TQGEWDAAHK
NEVDRLRASM PNLDAKLLES PEARYVTLER LVRERVLSEA AQTFRLNTSD ARLARELQQN
PTIASLRKSD GTLDIERYRQ LAASQGLTPE GFEARVRNDL SVRQVESGIV GTAFSPAALA
DISLNAFFEK REVQIARFTP ADFAAKVNPS DTELDAFYQA NQSMFQAQES ANIEYVVLDL
DAVKKTITLN EADLKSYYEQ NAARLSGKEE RRASHILVNA NKDMSAADRQ KAKEKAQSLL
ALVRKAPESF ADVARKNSQD VGSAPNGGDL DFFGRGAMVK PFEDATFAMK KGDISDLVES
DFGFHIIRVT DIKVPKQRSF EELRAGIEAD LKAQQAQRKY AEVADAFTNG VYEQSDSLKP
IAERLKLDVK TASNLQRNGT PSVSGVLANP KLLAAVFSPD SVEKKRNTEA VEIAANQLVA
ARITQYTPAR TLPLAEVRSI VHDRLVAKRA AEMAGKEGAA KLAAWKAGGA ADNLPAVVTV
SREPNQPIQG PLLDAALRAD TSSLPAWVGV DLGAQGYAVV RVNKVLARTP PPDANKERAQ
YAQWVASAEN QAYYQWLKER FKVQMKVQRP TRASFDTQTS AE
//
