ID A0A0G3BMX0_9BURK Unreviewed; 633 AA.
AC A0A0G3BMX0;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Periplasmic chaperone PpiD {ECO:0000256|ARBA:ARBA00040743};
DE AltName: Full=Periplasmic folding chaperone {ECO:0000256|ARBA:ARBA00042775};
GN Name=ppiD {ECO:0000313|EMBL:AKJ28746.1};
GN ORFNames=AAW51_2055 {ECO:0000313|EMBL:AKJ28746.1};
OS Caldimonas brevitalea.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Caldimonas.
OX NCBI_TaxID=413882 {ECO:0000313|EMBL:AKJ28746.1, ECO:0000313|Proteomes:UP000035352};
RN [1] {ECO:0000313|EMBL:AKJ28746.1, ECO:0000313|Proteomes:UP000035352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7029 {ECO:0000313|EMBL:AKJ28746.1,
RC ECO:0000313|Proteomes:UP000035352};
RA Tang B., Yu Y.;
RL Submitted (MAY-2015) 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; CP011371; AKJ28746.1; -; Genomic_DNA.
DR RefSeq; WP_047194544.1; NZ_CP011371.1.
DR AlphaFoldDB; A0A0G3BMX0; -.
DR STRING; 413882.AAW51_2055; -.
DR KEGG; pbh:AAW51_2055; -.
DR PATRIC; fig|413882.6.peg.2159; -.
DR OrthoDB; 9812372at2; -.
DR Proteomes; UP000035352; Chromosome.
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:AKJ28746.1}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000035352};
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 633 AA; 70188 MW; FAA09D8ED0CE84B7 CRC64;
MFDFVRNNTR ILFFVLLLLI IPSFVFFGVE GYSQFREGAK TVAEVAGQDI TEAELEAAHR
NQVERMRAQM PGIDSKMFDT PEMRRQTLEA LVRERVMLTA ADKQHLVTSD ERLQRIFATD
PQLAFLRKPD GTLNRDILAA QGMSPQGFEQ RLRQDLSLRQ VMLGVSDSTM ASKTVTETAL
DAFMQQRDVQ VARFEAKDYL AKVNPTDADL EAYYKDPKNV AQFQTQEQVK IEYVVLDLES
VKKGITVPED ELRNYYKENE ARYSTPEERR ASHILIKADK GAPAAQRDAA KAKAEKLLAE
LKQNPDRFAE LAKQNSEDPG SAANGGDLEF FGRGAMVKPF EEAAFTLKQG EISPVVETDF
GFHIIRVTGA RGGDKKSFEA VKAEIEDEVR TQQAQKRYAE VAEQFSNMVY EQTDALKPVA
DKLQLPLQTA DKVTRTPGPG AQGVLANPKL LAALFTTEAI SSKRNTEALE VAPSQLVAAR
VVEHQPARTL PLEEVKPRVR EALVARQAAE MARKEGEAKL AAWQKAPAEA NLPPAVKVSR
LQPGGQSREV VEAALKAKTD KLPSWVGVDL GPQGYAVVRI NSVAGRAEVP AADQLPRQYA
QAWGAAEAQA YYEALKKRYK TEITYDPKAA PAP
//
