ID A0A376BNA8_9NEIS Unreviewed; 605 AA.
AC A0A376BNA8;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
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 ECO:0000313|EMBL:SSY71141.1};
GN ORFNames=NCTC10283_01281 {ECO:0000313|EMBL:SSY71141.1};
OS Alysiella crassa.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Alysiella.
OX NCBI_TaxID=153491 {ECO:0000313|EMBL:SSY71141.1, ECO:0000313|Proteomes:UP000254209};
RN [1] {ECO:0000313|EMBL:SSY71141.1, ECO:0000313|Proteomes:UP000254209}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC10283 {ECO:0000313|EMBL:SSY71141.1,
RC ECO:0000313|Proteomes:UP000254209};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|ARBA:ARBA00000696, ECO:0000256|HAMAP-
CC 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:0000256|ARBA:ARBA00001346, ECO:0000256|HAMAP-
CC Rule:MF_00399};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429, ECO:0000256|HAMAP-Rule:MF_00399};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004429,
CC ECO:0000256|HAMAP-Rule:MF_00399}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. DsbD subfamily.
CC {ECO:0000256|ARBA:ARBA00007241, ECO:0000256|HAMAP-Rule:MF_00399}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00399}.
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DR EMBL; UFSO01000002; SSY71141.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A376BNA8; -.
DR STRING; 1120980.GCA_000745955_00933; -.
DR OrthoDB; 9811036at2; -.
DR Proteomes; UP000254209; Unassembled WGS sequence.
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; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 2.60.40.1250; Thiol:disulfide interchange protein DsbD, N-terminal domain; 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; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBD; 1.
DR PANTHER; PTHR32234:SF0; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBD; 1.
DR Pfam; PF02683; DsbD; 1.
DR Pfam; PF11412; DsbD_N; 1.
DR Pfam; PF13098; Thioredoxin_2; 1.
DR SUPFAM; SSF74863; Thiol:disulfide interchange protein DsbD, N-terminal domain (DsbD-alpha); 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519, ECO:0000256|HAMAP-
KW Rule:MF_00399};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_00399};
KW Cytochrome c-type biogenesis {ECO:0000256|ARBA:ARBA00022748,
KW ECO:0000256|HAMAP-Rule:MF_00399};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|HAMAP-
KW Rule:MF_00399};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982, ECO:0000256|HAMAP-
KW Rule:MF_00399};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00399};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00399};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00399};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284, ECO:0000256|HAMAP-
KW Rule:MF_00399}; Reference proteome {ECO:0000313|Proteomes:UP000254209};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|HAMAP-Rule:MF_00399};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_00399};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_00399};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00399}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT CHAIN 25..605
FT /note="Thiol:disulfide interchange protein DsbD"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT /id="PRO_5017095731"
FT TRANSMEM 195..216
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT TRANSMEM 237..261
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT TRANSMEM 273..298
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT TRANSMEM 319..347
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT TRANSMEM 359..379
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT TRANSMEM 391..408
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT TRANSMEM 414..433
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT TRANSMEM 445..463
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT DOMAIN 468..605
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DISULFID 124..130
FT /note="Redox-active"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT DISULFID 523..526
FT /note="Redox-active"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
SQ SEQUENCE 605 AA; 64889 MW; 5BCA829DC61BB56B CRC64;
MKTALYQTLG AMLAMFGLAS GAAANNLNSD ELLPPEQAFI PSVEVGADGS IKTTFKVADG
YYLYQSKISA QANEQTLTEP QFSAGKEKED EFFGKQTVYY QNAQVSWQHA NTQPYKLTLH
YQGCADAGVC YPPVATNFDI QGEGVYQTEV AQADNPVAAF VKKPQGATDS LGNQTVAPHS
SAPANKQFSL SRDTLFLNLF WFFVAGLGLS FTACMYPLLP IVSSIIVGDK SGSKKRAFVL
SFVYVQGLAL TYTLVGVLAG MTGALLTVWL QQAWVVLSAS ALMVVLALSM FGLFNIQLPA
AVQSYFQNQS NQLSGGKVVS VFVMGMLSAL IVGPCVAPPL AFALGYIGQT GDALLGGMAL
YALAIGTGVP LMVIGTFGGH VLPRAGDWMN GIKYAFGVIL LAVAVYLATP FIGYAWAAGL
YTALLILPAL YMAWRLKHFS GSLKAITACL AALLAMGGVW FGVQSARGQE TGLHSFLTLH
PPMHGATHGE RFTDVAKLKS AMQAALQADP NTPILLDFYA DWCVSCKEME AKTFNRPEVQ
AAVPMARMFQ IDVTANTAEH QALLKEYGLF GPPALFVLKS DGSRSDGLLG YLAADEFVAW
YRQRQ
//
