ID A0A1H0W8W3_9BURK Unreviewed; 641 AA.
AC A0A1H0W8W3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Periplasmic chaperone PpiD {ECO:0000256|ARBA:ARBA00040743};
DE AltName: Full=Periplasmic folding chaperone {ECO:0000256|ARBA:ARBA00042775};
GN ORFNames=SAMN05216303_108143 {ECO:0000313|EMBL:SDP87078.1};
OS Rhodoferax sp. OV413.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Rhodoferax.
OX NCBI_TaxID=1855285 {ECO:0000313|EMBL:SDP87078.1, ECO:0000313|Proteomes:UP000199151};
RN [1] {ECO:0000313|Proteomes:UP000199151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OV413 {ECO:0000313|Proteomes:UP000199151};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FNJA01000008; SDP87078.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H0W8W3; -.
DR STRING; 1855285.SAMN05216303_108143; -.
DR OrthoDB; 9812372at2; -.
DR Proteomes; UP000199151; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00278,
KW ECO:0000313|EMBL:SDP87078.1}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000199151};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 269..372
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
FT COILED 378..405
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 641 AA; 70067 MW; 64AC86F88BC10E36 CRC64;
MFDFVRKHSK IMMGLMFLLI IPAFIVVGGS EGFRRFNEGG DTVATVAGKD IKQTDWDAAH
RTQVQRVMAS QPGIDPKVLD SAEARYATLE NLVQERVLAA AADKSRLVTS DSRLARNLQD
DPSIASLRKP DGSLDIERYR QLLAAQGMTP EMFEARVRSD LSQRQVVSGV AGTSFSSAAE
ADLALNALFE KREVQVSLFR SADFAAKVSP SDADLEAWYK DHAALFQAPE QATIEYVVLD
LDAVKKSIVP NEQDLRTYYK ENADRLAGKE ERRASHILIN AAKDASSDER KKARAKAEEL
LAQVKKTPAS FAEVAKKNSQ DTGSAANGGD LDYFGRGAMV KPFEDAAFAL KKGDISDVVE
SDFGFHIIQL TDIRAPKQRS FEEMRPELEA ELKNQQAQSK FAEVAEAFTN GVYEQADSLK
PIAERLKLQV QTAPLSRTPV PGAKGVLANA KFLNAIFSSD SIEKKRNTEA IEIAANQLAS
GRITQYTAAH TRPFAEVKEQ VRIQLVGARA TEMAKKEGLE KLTAWKANPG AATLPAAVLV
SRENTQQQPV KVVDAALRAD ASSLPAWTAA DLGEQGYAVV KINKLVPRDA PVEAALKQGR
DQYVQGWAGA ESRAYYQLLK ERFKVKINVA KPLTKIGGDA G
//
