DSBD_PASMU
ID DSBD_PASMU Reviewed; 576 AA.
AC Q9CP40;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=Thiol:disulfide interchange protein DsbD;
DE EC=1.8.1.8;
DE AltName: Full=Protein-disulfide reductase;
DE Short=Disulfide reductase;
DE Flags: Precursor;
GN Name=dsbD; OrderedLocusNames=PM0221;
OS Pasteurella multocida (strain Pm70).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Pasteurella.
OX NCBI_TaxID=272843;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pm70;
RX PubMed=11248100; DOI=10.1073/pnas.051634598;
RA May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT "Complete genomic sequence of Pasteurella multocida Pm70.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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 (By
CC similarity). {ECO:0000250}.
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 -!- 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 -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. DsbD subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK02305.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE004439; AAK02305.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q9CP40; -.
DR SMR; Q9CP40; -.
DR STRING; 747.DR93_1842; -.
DR PRIDE; Q9CP40; -.
DR EnsemblBacteria; AAK02305; AAK02305; PM0221.
DR KEGG; pmu:PM0221; -.
DR PATRIC; fig|272843.6.peg.229; -.
DR HOGENOM; CLU_014657_3_0_6; -.
DR OMA; YRHRFQF; -.
DR Proteomes; UP000000809; 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; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..576
FT /note="Thiol:disulfide interchange protein DsbD"
FT /id="PRO_0000007380"
FT TOPO_DOM 20..177
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 199..229
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 251..253
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 254..274
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 275..295
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 296..316
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 317..336
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 337..357
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 358..367
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 368..388
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 389..394
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 395..415
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 416..419
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 420..440
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 441..576
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 433..570
FT /note="Thioredoxin"
FT DISULFID 120..125
FT /note="Redox-active"
FT /evidence="ECO:0000250"
FT DISULFID 193..315
FT /note="Redox-active"
FT /evidence="ECO:0000250"
FT DISULFID 485..488
FT /note="Redox-active"
FT /evidence="ECO:0000250"
SQ SEQUENCE 576 AA; 64465 MW; 98507447D5EDFA41 CRC64;
MKKIFFIFFL IWTSLSVNAG VFDKKNAFLK AEQAFVFTES QQNDRLSLNW DIASGYYLYK
KSLEIKGENG QLFIPQLPLA EIHQDDFFGD VEIYRHQLTF SLPFTQLSAT KQVEITYQGC
TEGFCYPPET RVIALTSLER ESGQISSAVL KEESVLSELP LAEQDRLAAK LIESKYAVFW
FFLFGLGLAF TPCVLPMLPL LSAIVIGREQ RPSTAKAFGL SVVYVQGMAL TYTLLGLIVA
AIGLPFQVAL QSPYVLLTLS AIFVLLALSM FGLFTLQLPV SLQTKLTQYS QQQKSGVFGG
VFVMGMIAGL VASPCTSAPL SGALLYVAQS GDLFTGAITL YLLALGMGLP LIFITVFGNN
ILPKSGNWMI QVKNAFGFVL LALPIFLISR VFPEIEMPLW FSLAFAFSLW LLYQFRNNKG
VWVFTFILGV MGYLYYSYAM NRHTPAHQTT SLSQFERITS YAQLQQVLSK NPNSLAMLDL
YADWCVACKE FETHTFSDVA VQKAFTDVLL LQVDMTKNSE ANRELMQKLH VIGLPTLIFF
NQQGQEIEGS RITGFMQASP FVDWLQKMKS IQPISQ
