ID A0A0B1YI98_9RALS Unreviewed; 645 AA.
AC A0A0B1YI98;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Periplasmic chaperone PpiD {ECO:0000256|ARBA:ARBA00040743};
DE AltName: Full=Periplasmic folding chaperone {ECO:0000256|ARBA:ARBA00042775};
GN ORFNames=PI87_09115 {ECO:0000313|EMBL:KHK56561.1};
OS Ralstonia sp. A12.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=1217052 {ECO:0000313|EMBL:KHK56561.1, ECO:0000313|Proteomes:UP000030970};
RN [1] {ECO:0000313|EMBL:KHK56561.1, ECO:0000313|Proteomes:UP000030970}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A12 {ECO:0000313|EMBL:KHK56561.1,
RC ECO:0000313|Proteomes:UP000030970};
RA Chen J.W., Yin W.F., Chan K.G.;
RT "Draft Genome of Ralstonia A12.";
RL Submitted (NOV-2014) 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:KHK56561.1}.
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DR EMBL; JSZO01000006; KHK56561.1; -; Genomic_DNA.
DR RefSeq; WP_039597408.1; NZ_JSZO01000006.1.
DR AlphaFoldDB; A0A0B1YI98; -.
DR STRING; 1217052.PI87_09115; -.
DR OrthoDB; 9812372at2; -.
DR Proteomes; UP000030970; 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; IPR023058; PPIase_PpiC_CS.
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; PS01096; PPIC_PPIASE_1; 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:KHK56561.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
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 269..373
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 645 AA; 70530 MW; C611F06749485FD6 CRC64;
MLEFVRTHRR LMFLVLLILV FPSFVFFGVQ SYSSFMDSSH DAAKVDGKVI TTAEVDNRVR
EQTDRLRQML GAQYDPRQFE GPQMRRDVLD GIIQQRVLSN EVAHANLNVS NEKIRDTILQ
IPAVAALRKP DGSFDEQAYV QLLAAQNMTP EQLEGNLRFE LAQQQLPQSI VSTAFVPKSL
VDHLIQVRDQ QREVQALLFK PADYAAKVNV DDKAIQAYYD AHQQEFSVPE QVKAEYVVFS
GEDMMKQIPV TPEQIKEYYD QNAARFKTQE ERRAAHILIK LPDNAKAADK DAAKKKAEEV
LAEVRKNPAS FAELAKKYSG DPGSAAQGGE LGFLGKGATV PPFENALFAL KQPGDISDVV
QSDFGFHIIK LEEVKGGGVQ PLEAVKPELE REVRTQLANK KYTELADAFS NAVEDQSDSL
KPVADKLKLQ VQTADNVTRT PTPALASSPI GNEKVLKALF ADDVIKNHRN TAAIQVGPTT
LVAARAAEYR PATVKKLADV REQVKAKVIA EQAAALAKKA GEEKLAAVKQ SNSADGFSAA
QTVSRQQAQG TPPTALTAIL RADATTLPTT IGVDLGAQGY ALYRINKVLP PANVDEARRA
ADAQQLAQAA GQADFNAYYE ALKARAKVKI NSGVVDAAKP SSSDE
//
