DSBD_HAEI8
ID DSBD_HAEI8 Reviewed; 579 AA.
AC Q4QM23;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 109.
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=NTHI1048;
OS Haemophilus influenzae (strain 86-028NP).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=281310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=86-028NP;
RX PubMed=15968074; DOI=10.1128/jb.187.13.4627-4636.2005;
RA Harrison A., Dyer D.W., Gillaspy A., Ray W.C., Mungur R., Carson M.B.,
RA Zhong H., Gipson J., Gipson M., Johnson L.S., Lewis L., Bakaletz L.O.,
RA Munson R.S. Jr.;
RT "Genomic sequence of an otitis media isolate of nontypeable Haemophilus
RT influenzae: comparative study with H. influenzae serotype d, strain KW20.";
RL J. Bacteriol. 187:4627-4636(2005).
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; CP000057; AAX87924.1; -; Genomic_DNA.
DR RefSeq; WP_011272260.1; NC_007146.2.
DR AlphaFoldDB; Q4QM23; -.
DR SMR; Q4QM23; -.
DR EnsemblBacteria; AAX87924; AAX87924; NTHI1048.
DR KEGG; hit:NTHI1048; -.
DR HOGENOM; CLU_014657_3_0_6; -.
DR OMA; YYADWCV; -.
DR OrthoDB; 1055204at2; -.
DR Proteomes; UP000002525; 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 Pfam; PF00085; Thioredoxin; 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..16
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT CHAIN 17..579
FT /note="Thiol:disulfide interchange protein DsbD"
FT /id="PRO_0000304389"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT TRANSMEM 254..274
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT TRANSMEM 296..316
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT TRANSMEM 337..357
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT TRANSMEM 376..396
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT TRANSMEM 397..417
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT TRANSMEM 420..440
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT DOMAIN 449..579
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT DISULFID 124..129
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT DISULFID 193..315
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT DISULFID 495..498
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
SQ SEQUENCE 579 AA; 64418 MW; 798E5E8CA5F029BA CRC64;
MKKLFLFFTL IFTAFAANSG LFDKKQTFLK VDDAFAFSAT LSTDKSQLQA HWDIADGYYL
YQDKISAELV GKSNPLSLHT QQAAELHQDP YFGEVKVFTH SIDGIFRGTF NNADDKVEIT
YQGCTEGFCY PPETKVLRIG DLAVSQEQIV EKTVEKNTAL LSEQDRLADG LFHSKWTIFG
FFLLGLGLAF TPCVLPMLPL LSAIVIGQQQ RPNMMRAFSL AFLYVQGMAL TYTLLGLAVA
AIGLPFQIAL QHPYVMIGLS ILFVALALSM FGLFTIQLPN SLQNKLNTWS QKQTSGAFGG
AFAMGMIAGL VASPCTSAPL SGALLYVAQS GDLFTGAATL YLLALGMGVP LMLITLFGNK
ILPKSGEWMN TVKQTFGFVM LALPVFLLSR ILPEVWEPRL WAGLATVFFI WFALQMSKNG
FGYAIKIISF ALAMVTVQPL QNWIWQTQTT TQSAVENMPV SQVKFKQIKN TEELDRTLAE
NPHSIAMLDL YADWCVACKE FEKLTFSDPQ VQQQFQNILL LQVNMTKNSP ENKALMERFN
VMGLPTILFF DQQNNEIQGS RVTGFMDADA FSNWLKALH
