ID A0A1A6DWN3_9BURK Unreviewed; 633 AA.
AC A0A1A6DWN3;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Periplasmic chaperone PpiD {ECO:0000256|ARBA:ARBA00040743};
DE AltName: Full=Periplasmic folding chaperone {ECO:0000256|ARBA:ARBA00042775};
GN ORFNames=A9O67_01545 {ECO:0000313|EMBL:OBS31347.1};
OS Tepidimonas fonticaldi.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Tepidimonas.
OX NCBI_TaxID=1101373 {ECO:0000313|EMBL:OBS31347.1, ECO:0000313|Proteomes:UP000091969};
RN [1] {ECO:0000313|EMBL:OBS31347.1, ECO:0000313|Proteomes:UP000091969}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PL17 {ECO:0000313|EMBL:OBS31347.1,
RC ECO:0000313|Proteomes:UP000091969};
RA Pinnaka A.K.;
RT "Genome sequence of Tepidimonas fonticaldi PL17.";
RL Submitted (JUN-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}.
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:OBS31347.1}.
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DR EMBL; LZDH01000034; OBS31347.1; -; Genomic_DNA.
DR RefSeq; WP_068607439.1; NZ_LZDH01000034.1.
DR AlphaFoldDB; A0A1A6DWN3; -.
DR STRING; 1101373.A9O67_01545; -.
DR OrthoDB; 9812372at2; -.
DR Proteomes; UP000091969; 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; 6.10.140.970; -; 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 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 633 AA; 70117 MW; 714F3B39D6E7877F CRC64;
MFDVFRNNMK VLMALLMLLI IPSFVFFGIE GYTRFRDQSE PVARVGGERI TRTEWDAAHR
REVERLAASM PGVDRALLEG EDSRRATLER LVTERVLARA AQDMRLVATD RRLAAELLRD
PTIAGLRKPD GTLDVQRYQD LLRAQGMTAE QFEAGVRADL ARRAVTQAVA DSAVMPKASA
EWAAQAFFER REVAPAFFRP ADHASAIQVS DADLKAFYDE HADEFRTPEQ ADIEYVVLDP
QAVAARITPS EAELRDYYRQ NVADTSRAEQ RRASHILLLL PPGASADEKA RVRAEAEQIL
AEVRRDPKRF AELARTRSQD PGSAAKGGDL DWFGRGAMVK PFEDAVFALQ KGQISDIVES
EFGLHIIQLT DVRQPEAEPF EKARPRIEAE VRRQLAQRRF AEDAERFSNL VYEQSDTLAP
AAQALGLTVH RATVERTGPV GAAADALLRE PALLRAVFNE EALGQKRNSA AIELGGNRLL
SVRVLAHRPS ERRPFEAVAS EVRQRLVQQR ARAAALEAAR AAQAQWSAQT PAASALRTPV
LVSRQDAQGL PPAAVRAAMS ARLEGDAPAW VVVDLGADGA AVLRVRRGPP REAPDAVRLL
NERQELARLW GEGEAQAYLG ALRQRYKAEI LVK
//
