DSBD_PHOLL
ID DSBD_PHOLL Reviewed; 575 AA.
AC Q7MZX2;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Thiol:disulfide interchange protein DsbD {ECO:0000255|HAMAP-Rule:MF_00399};
DE EC=1.8.1.8 {ECO:0000255|HAMAP-Rule:MF_00399};
DE AltName: Full=Protein-disulfide reductase {ECO:0000255|HAMAP-Rule:MF_00399};
DE Short=Disulfide reductase {ECO:0000255|HAMAP-Rule:MF_00399};
DE Flags: Precursor;
GN Name=dsbD {ECO:0000255|HAMAP-Rule:MF_00399}; OrderedLocusNames=plu4139;
OS Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS TT01).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Photorhabdus.
OX NCBI_TaxID=243265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15139 / CIP 105565 / TT01;
RX PubMed=14528314; DOI=10.1038/nbt886;
RA Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA Glaser P., Boemare N., Danchin A., Kunst F.;
RT "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT luminescens.";
RL Nat. Biotechnol. 21:1307-1313(2003).
CC -!- FUNCTION: Required to facilitate the formation of correct disulfide
CC bonds in some periplasmic proteins and for the assembly of the
CC periplasmic c-type cytochromes. Acts by transferring electrons from
CC cytoplasmic thioredoxin to the periplasm. This transfer involves a
CC cascade of disulfide bond formation and reduction steps.
CC {ECO:0000255|HAMAP-Rule:MF_00399}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-dithiol + NAD(+) = [protein]-disulfide + H(+) +
CC NADH; Xref=Rhea:RHEA:18749, Rhea:RHEA-COMP:10593, Rhea:RHEA-
CC COMP:10594, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.8.1.8;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00399};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-dithiol + NADP(+) = [protein]-disulfide + H(+) +
CC NADPH; Xref=Rhea:RHEA:18753, Rhea:RHEA-COMP:10593, Rhea:RHEA-
CC COMP:10594, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.8;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00399};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00399}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00399}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. DsbD subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00399}.
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DR EMBL; BX571872; CAE16511.1; -; Genomic_DNA.
DR RefSeq; WP_011148255.1; NC_005126.1.
DR AlphaFoldDB; Q7MZX2; -.
DR SMR; Q7MZX2; -.
DR STRING; 243265.plu4139; -.
DR EnsemblBacteria; CAE16511; CAE16511; plu4139.
DR GeneID; 24170648; -.
DR KEGG; plu:plu4139; -.
DR eggNOG; COG4232; Bacteria.
DR HOGENOM; CLU_014657_3_0_6; -.
DR OMA; YYADWCV; -.
DR OrthoDB; 1055204at2; -.
DR BioCyc; PLUM243265:PLU_RS20480-MON; -.
DR Proteomes; UP000002514; Chromosome.
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 (NAD(P)) activity; IEA:UniProtKB-UniRule.
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; Cell membrane; Cytochrome c-type biogenesis;
KW Disulfide bond; Electron transport; Membrane; NAD; Oxidoreductase;
KW Redox-active center; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..24
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT CHAIN 25..575
FT /note="Thiol:disulfide interchange protein DsbD"
FT /id="PRO_0000304391"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT TRANSMEM 297..317
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT TRANSMEM 336..356
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT TRANSMEM 367..387
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT TRANSMEM 394..414
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT TRANSMEM 425..445
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT DOMAIN 444..575
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT DISULFID 126..132
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT DISULFID 192..314
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT DISULFID 490..493
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
SQ SEQUENCE 575 AA; 64073 MW; CBEC7F62BF5E7852 CRC64;
MIKRTLMLFL LLCSPLLTPA AANALFEQPG QNPYLPVDQA FMFDFQQKGD KLTLDWQIKP
GYYLYHKQLH IEPQQATLGK ITLPQGTAHR DEFFGETEVY FQQLIVNVPV TKANNNSNIV
VTYQGCAAAG YCYPPETRLV PLSAVIPSKT TDAISAEPVH KTPESASNDQ QHLPFSPLWA
ILIGIGIAFT PCVLPMYPLI SSIILGSQRP KSLKQIFWLA LSYVQGMAVT YTLLGLIVAA
AGLQFQAALQ HPYVLIGLSV LFILLALSMF GLYSLQLPSA VQTRLVNWSN QQKNGSLFGV
FAMGALAGLI CSPCTTAPLS AILLYIAQSG NTVAGGLTLY LYALGMGLPL IAVTLFGHKL
LPRSGPWMQY VKEAFGFIIL ALPVFLLERV IGDAWGIRLW SLLAVSFLGW GFVLTIRSQN
GWVRVIQLIL LILMLIATRP LQDWFWGTTV TQQSQHSLNF RQINNWQELE QIMTQNSHKT
VMLDFYADWC TACKEFEKYT FSDPQVQSQL GDTLLLQANV TNNSPQQKQL LEKLSVRGLP
TILFFDSQGK EIPDSRVNGF MDATRFNEHL QHLPK
