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Database: UniProt
Entry: A0A0J1D433_9BURK
LinkDB: A0A0J1D433_9BURK
Original site: A0A0J1D433_9BURK 
ID   A0A0J1D433_9BURK        Unreviewed;       599 AA.
AC   A0A0J1D433;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   20-DEC-2017, entry version 20.
DE   RecName: Full=Thiol:disulfide interchange protein DsbD {ECO:0000256|HAMAP-Rule:MF_00399};
DE            EC=1.8.1.8 {ECO:0000256|HAMAP-Rule:MF_00399};
DE   AltName: Full=Protein-disulfide reductase {ECO:0000256|HAMAP-Rule:MF_00399};
DE            Short=Disulfide reductase {ECO:0000256|HAMAP-Rule:MF_00399};
DE   Flags: Precursor;
GN   Name=dsbD {ECO:0000256|HAMAP-Rule:MF_00399};
GN   ORFNames=EOS_04225 {ECO:0000313|EMBL:KLU27426.1};
OS   Caballeronia mineralivorans PML1(12).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Caballeronia.
OX   NCBI_TaxID=908627 {ECO:0000313|EMBL:KLU27426.1, ECO:0000313|Proteomes:UP000035963};
RN   [1] {ECO:0000313|EMBL:KLU27426.1, ECO:0000313|Proteomes:UP000035963}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PML1(12) {ECO:0000313|Proteomes:UP000035963};
RX   PubMed=26205858;
RA   Uroz S., Oger P.;
RT   "Draft Genome Sequence of Burkholderia sp. Strain PML1(12), an
RT   Ectomycorrhizosphere-Inhabiting Bacterium with Effective Mineral-
RT   Weathering Ability.";
RL   Genome Announc. 3:e00798-15(2015).
CC   -!- FUNCTION: Required to facilitate the formation of correct
CC       disulfide bonds in some periplasmic proteins and for the assembly
CC       of the periplasmic c-type cytochromes. Acts by transferring
CC       electrons from cytoplasmic thioredoxin to the periplasm. This
CC       transfer involves a cascade of disulfide bond formation and
CC       reduction steps. {ECO:0000256|HAMAP-Rule:MF_00399}.
CC   -!- CATALYTIC ACTIVITY: Protein dithiol + NAD(P)(+) = protein
CC       disulfide + NAD(P)H. {ECO:0000256|HAMAP-Rule:MF_00399}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_00399}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_00399}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. DsbD subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00399}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KLU27426.1}.
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DR   EMBL; AEJF01000028; KLU27426.1; -; Genomic_DNA.
DR   EnsemblBacteria; KLU27426; KLU27426; EOS_04225.
DR   PATRIC; fig|908627.4.peg.934; -.
DR   Proteomes; UP000035963; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0047134; F:protein-disulfide reductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   GO; GO:0017004; P:cytochrome complex assembly; IEA:UniProtKB-UniRule.
DR   CDD; cd02953; DsbDgamma; 1.
DR   Gene3D; 2.60.40.1250; -; 1.
DR   HAMAP; MF_00399; DbsD; 1.
DR   InterPro; IPR003834; Cyt_c_assmbl_TM_dom.
DR   InterPro; IPR035671; DsbD_gamma.
DR   InterPro; IPR028250; DsbDN.
DR   InterPro; IPR036929; DsbDN_sf.
DR   InterPro; IPR022910; Thiol_diS_interchange_DbsD.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR32234:SF0; PTHR32234:SF0; 1.
DR   Pfam; PF11412; DsbC; 1.
DR   Pfam; PF02683; DsbD; 1.
DR   Pfam; PF13098; Thioredoxin_2; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   SUPFAM; SSF74863; SSF74863; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00399};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00399};
KW   Complete proteome {ECO:0000313|Proteomes:UP000035963};
KW   Cytochrome c-type biogenesis {ECO:0000256|HAMAP-Rule:MF_00399};
KW   Disulfide bond {ECO:0000256|HAMAP-Rule:MF_00399};
KW   Electron transport {ECO:0000256|HAMAP-Rule:MF_00399};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00399,
KW   ECO:0000256|SAAS:SAAS00093715};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_00399};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00399};
KW   Redox-active center {ECO:0000256|HAMAP-Rule:MF_00399};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035963};
KW   Signal {ECO:0000256|HAMAP-Rule:MF_00399};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_00399,
KW   ECO:0000256|SAAS:SAAS00464121};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00399,
KW   ECO:0000256|SAAS:SAAS00093729};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_00399}.
FT   SIGNAL        1     18       {ECO:0000256|HAMAP-Rule:MF_00399}.
FT   CHAIN        19    599       Thiol:disulfide interchange protein DsbD.
FT                                {ECO:0000256|HAMAP-Rule:MF_00399}.
FT                                /FTId=PRO_5008989439.
FT   TRANSMEM    175    208       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00399}.
FT   TRANSMEM    220    244       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00399}.
FT   TRANSMEM    256    280       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00399}.
FT   TRANSMEM    300    330       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00399}.
FT   TRANSMEM    336    364       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00399}.
FT   TRANSMEM    376    394       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00399}.
FT   TRANSMEM    400    427       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00399}.
FT   TRANSMEM    434    452       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00399}.
FT   DOMAIN      465    596       Thioredoxin. {ECO:0000259|PROSITE:
FT                                PS51352}.
FT   DISULFID    117    123       Redox-active. {ECO:0000256|HAMAP-Rule:
FT                                MF_00399}.
FT   DISULFID    195    317       Redox-active. {ECO:0000256|HAMAP-Rule:
FT                                MF_00399}.
FT   DISULFID    513    516       Redox-active. {ECO:0000256|HAMAP-Rule:
FT                                MF_00399}.
SQ   SEQUENCE   599 AA;  62942 MW;  B7DA5BD9BD226882 CRC64;
     MLVSCLVLLL GSFSPSRAAD DFLDPAVAFK FNATEKPGEI DVRYKVADGY YMYRERFAFA
     VKNGTATLGE PQLPAGKVHF DQTFNKDVET YRGELVIRIP VKQASGPFDI AVTSQGCADQ
     GICYPPMERT YRVSGAALQA ASANGQTQSA NTIDVPWYDR ATNADYAQSL LESGGFFAIV
     GLYFVAGVVL SLLPCSYPMI PILSAIIIGE GARVTRSRGF GLSAAYVFGM ALVYTALGVL
     AAMIGQSLGA WLQNPWVLGA FGVLLALFAL TLIAGFDIAL PARWQNSVNQ ASQKRSGGKV
     AAVVVMGALS ALVVGACMTA PLFAVLAFIA HTGNALLGGA ALFSMGVGLG VPLLIIGLGA
     GTLLPRAGNW MDGVKVFFGV VLLAAALWIV WPALSAVAQM ALAALWLLIA AAALGLFTSG
     APVVSIWRRL GRGFGAALAI WGAALLVGLA AGSTDPLRPL AVFAARTGSG AEASAQQSAP
     GEVFAPVRSS AELDLALKAA GRPAMLDFYA DWCVSCKEME HLTFSDPRVR ARLAQLNLLR
     ADVTANNTDD QVLLKRFKLF GPPGIILFDA QGNEVVRVVG YESADTFLKS LDKLSAPTT
//
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