ID A0A1Y0ELU6_9BURK Unreviewed; 648 AA.
AC A0A1Y0ELU6;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-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=CCO03_07950 {ECO:0000313|EMBL:ARU04613.1};
OS Comamonas serinivorans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Comamonas.
OX NCBI_TaxID=1082851 {ECO:0000313|EMBL:ARU04613.1, ECO:0000313|Proteomes:UP000196138};
RN [1] {ECO:0000313|EMBL:ARU04613.1, ECO:0000313|Proteomes:UP000196138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26136 {ECO:0000313|EMBL:ARU04613.1,
RC ECO:0000313|Proteomes:UP000196138};
RA Song R., Chenine A.L., Ruprecht R.M.;
RL Submitted (MAY-2017) 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; CP021455; ARU04613.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y0ELU6; -.
DR KEGG; cser:CCO03_07950; -.
DR OrthoDB; 9812372at2; -.
DR Proteomes; UP000196138; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; PF00639; Rotamase; 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000196138};
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..374
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 648 AA; 70777 MW; EE3A5E4FF0BBAC35 CRC64;
MFDLFRNHTK ILMGLLVLLI VPSFVFFGIE GYTQFNDKQK AVAVVDGHKI NQLEWDEANR
QAAMRLRAQN PDVDPALLDS PEIKYATLEQ LVREQVLAAA ARNAHLIVGN AQVATYLSQD
PTIASLRGAD GKLNMEAYAQ MLARQNMTPE MFEAGVRQQL SAQQVMLGVV GSGFAVPAQA
DVTLNAFRQA RNIQYVLLKP EEYAAKVDVK PTDLEAYYKK NEAMFKRPES ADIEYVELTL
DALKASVTVS EADLKTYYES NKASLGEAEQ RRASHILIEA PKDMPADERA KARAKADAIH
AELLKNPASF GDVAKRESQD AASAEQGGDL GFFSAQNAAV VDDISKAAFA LKNKGDISAV
IDADFGFDIV QLTDIKPSEA PAFETVRAKL EDQYRTEQAQ KTFTSTADEM GKLAFEQRDS
LKPIADAFKL PIKTAAGLVH DRVQPPQVPQ ALGNAELISA IFADDVARNK GNTQPVAVAP
STVVVARVSK YVAAHTESLA DVQEPLKKLY VTEQSAKLAQ EAAKVQLEAA RKSPQSLAWL
PAVDVARDKA GEVPTPIVEA ALRASTRQLP AFSVVDLGPQ GSAILRVNKV TAPEVLPAEA
QKQAEQQYAM GWSRAEMDAY YNMLKDRFKV KIHEADPKKQ TALTNANK
//