DSBD_CROS8
ID DSBD_CROS8 Reviewed; 574 AA.
AC A7MMC7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=ESA_00148;
OS Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Cronobacter.
OX NCBI_TaxID=290339;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-894;
RX PubMed=20221447; DOI=10.1371/journal.pone.0009556;
RA Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L.,
RA Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A.,
RA Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K.,
RA McClelland M., Forsythe S.J.;
RT "Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic
RT hybridization analysis with other Cronobacter species.";
RL PLoS ONE 5:E9556-E9556(2010).
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; CP000783; ABU75452.1; -; Genomic_DNA.
DR RefSeq; WP_012123666.1; NC_009778.1.
DR AlphaFoldDB; A7MMC7; -.
DR SMR; A7MMC7; -.
DR EnsemblBacteria; ABU75452; ABU75452; ESA_00148.
DR KEGG; esa:ESA_00148; -.
DR PATRIC; fig|290339.8.peg.129; -.
DR HOGENOM; CLU_014657_3_0_6; -.
DR OMA; YYADWCV; -.
DR OrthoDB; 1055204at2; -.
DR Proteomes; UP000000260; 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; 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 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; Signal; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..19
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT CHAIN 20..574
FT /note="Thiol:disulfide interchange protein DsbD"
FT /id="PRO_1000049608"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT TRANSMEM 218..238
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 306..326
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT TRANSMEM 333..353
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 399..419
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT DOMAIN 430..574
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT REGION 147..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 122..128
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 489..492
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
SQ SEQUENCE 574 AA; 61676 MW; 9063912E6842813A CRC64;
MAHRILTLIL LFCSAHASAS LFGQQNASQF VPADQAFAFD FQQQQHQLTL NWQIKPGYYL
YRQQIRVTPA NASVAPPALP TGEPHEDEFF GKSEIYRDAL SVPVTVEQAA PGATLSVTYQ
GCAEAGFCYP PETRTVPLSA VEPTESVKAN AATPSAATGE QTRVNSDSPS ATLPFSAFWA
LLIGIGVAFT PCVLPMYPLI SGIVLGGDKR LSTRRALLLA FIYVQGMALT YTALGLVVAA
AGLQFQAALQ SPWVLVTLSA VFVLLALSMF GLFTLQLPAS LQTRLTLMSN RQRGGSPGGV
FAMGAIAGLI CSPCTTAPLS AILLYIAQSG NLWLGGGTLY LYALGMGLPL ILVTVFGNRL
LPKSGPWMEQ VKTAFGFVIL ALPVFLLERV LGEPWGVRLW SVLGVAFFGW AFVTSLNATR
SWMRAVQIVL LGAAMICARP LQDWVFGAPV AESQAHLAFT RIATVDDLDR ALAQAKGKPV
MLDLYADWCV ACKEFEKYTF SAPEVQRALD GAVLLQADVT ANSAADVALL KRLNVLGLPT
IIFFDAQGNE IPNGRVTGFM DAPAFATHLH NRLR
