ID F1W0C6_9BURK Unreviewed; 642 AA.
AC F1W0C6;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Periplasmic chaperone PpiD {ECO:0000256|ARBA:ARBA00040743};
DE AltName: Full=Periplasmic folding chaperone {ECO:0000256|ARBA:ARBA00042775};
GN ORFNames=IMCC9480_3518 {ECO:0000313|EMBL:EGF31691.1};
OS Oxalobacteraceae bacterium IMCC9480.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae.
OX NCBI_TaxID=937450 {ECO:0000313|EMBL:EGF31691.1, ECO:0000313|Proteomes:UP000004494};
RN [1] {ECO:0000313|EMBL:EGF31691.1, ECO:0000313|Proteomes:UP000004494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC9480 {ECO:0000313|EMBL:EGF31691.1,
RC ECO:0000313|Proteomes:UP000004494};
RX PubMed=21572000; DOI=10.1128/JB.05088-11;
RA Oh H.M., Lee K., Jang Y., Kang I., Kim H.J., Kang T.W., Kim S.Y., Cho J.C.;
RT "Genome sequence of strain IMCC9480, a xanthorhodopsin-bearing
RT betaproteobacterium isolated from the Arctic Ocean.";
RL J. Bacteriol. 193:3421-3421(2011).
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:EGF31691.1}.
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DR EMBL; AEPR01000376; EGF31691.1; -; Genomic_DNA.
DR AlphaFoldDB; F1W0C6; -.
DR OrthoDB; 9812372at2; -.
DR Proteomes; UP000004494; 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:EGF31691.1}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000004494};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 266..369
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 642 AA; 69986 MW; F07FE10662F7F497 CRC64;
MFEFVRTHKR LMQFLLLLII VPSFALVGLG SYKSFGDAEN VIAKVGGQPI TQVEYDAAQR
EQMARFKQMF GAQFDPKMFD TPEARQGILD NLIAQRALSV EAARQHLSVA DAALQQSITG
IAGLVGPDGK FDGERYRSLL AMQGMTPAMY EQRLRQDMAV QQLNSAIQST AFAPKTVATR
LSDINDQERT VQELLFKPAD YAAKVNVTAD MLKAYYDKNA RQFEVPEQAT IQYVVLSSDA
LASQIAVTDQ EVADFYEQNK KSFGVDEQRR ASHILINLKK GASATEKAAA KAKAEQVLAQ
VRKAPGDFAK IAKASSEDQG SAPEGGDLDF FGKGAMTPPF EEAVFKLKLN EISGLVESDF
GFHIIEVTAI KPASFRTLDQ VKPQIVADIK RQKAAKQYSE AAESFGNTVY EQADSLKPVA
DKLKLKIETV SGLTRTPNPL AAPTALFNNA KFLNAVFADD TLKNKHNTEA IEVAPSTLMA
GRIVDYKPVG KRPFAEVEAV VREKVIAEES AVLAKKAGEA KLAALKTADD ASGFGVAKVV
SRSKNDGMNG PGFDSVMKAD ISKLPAIAGA DLSRQGYAVY RISKVAQAEK IDAPRRLEEQ
QQIANALAQQ EMIAYLNVLK EKAKVKIIKP VARSPVVSDD RL
//
