DSBD1_PSEAE
ID DSBD1_PSEAE Reviewed; 591 AA.
AC Q9HUW5; O30556;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Thiol:disulfide interchange protein DsbD 1 {ECO:0000255|HAMAP-Rule:MF_00399};
DE EC=1.8.1.8 {ECO:0000255|HAMAP-Rule:MF_00399};
DE AltName: Full=Protein-disulfide reductase 1 {ECO:0000255|HAMAP-Rule:MF_00399};
DE Short=Disulfide reductase 1 {ECO:0000255|HAMAP-Rule:MF_00399};
DE Flags: Precursor;
GN Name=dsbD1 {ECO:0000255|HAMAP-Rule:MF_00399}; Synonyms=dipZ;
GN OrderedLocusNames=PA4845;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=9353916; DOI=10.1099/00221287-143-10-3111;
RA Page M.D., Saunders N.F.W., Ferguson S.J.;
RT "Disruption of the Pseudomonas aeruginosa dipZ gene, encoding a putative
RT protein-disulfide reductase, leads to partial pleiotropic deficiency in c-
RT type cytochrome biogenesis.";
RL Microbiology 143:3111-3122(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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; AF010322; AAB84084.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG08230.1; -; Genomic_DNA.
DR PIR; E83039; E83039.
DR RefSeq; NP_253532.1; NC_002516.2.
DR RefSeq; WP_003112327.1; NZ_QZGE01000002.1.
DR AlphaFoldDB; Q9HUW5; -.
DR SMR; Q9HUW5; -.
DR STRING; 287.DR97_2196; -.
DR PaxDb; Q9HUW5; -.
DR PRIDE; Q9HUW5; -.
DR EnsemblBacteria; AAG08230; AAG08230; PA4845.
DR GeneID; 879570; -.
DR KEGG; pae:PA4845; -.
DR PATRIC; fig|208964.12.peg.5077; -.
DR PseudoCAP; PA4845; -.
DR HOGENOM; CLU_014657_3_0_6; -.
DR InParanoid; Q9HUW5; -.
DR OMA; YRHRFQF; -.
DR PhylomeDB; Q9HUW5; -.
DR BioCyc; PAER208964:G1FZ6-4959-MON; -.
DR Proteomes; UP000002438; 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:0015035; F:protein-disulfide reductase activity; IBA:GO_Central.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
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; 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; 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..18
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT CHAIN 19..591
FT /note="Thiol:disulfide interchange protein DsbD 1"
FT /id="PRO_0000007381"
FT TOPO_DOM 19..175
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT TOPO_DOM 197..213
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT TOPO_DOM 235..251
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT TOPO_DOM 273..295
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 296..316
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT TOPO_DOM 317..338
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 339..359
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT TOPO_DOM 360..365
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 366..386
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT TOPO_DOM 387..392
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 393..413
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT TOPO_DOM 414..423
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 424..444
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT TOPO_DOM 445..591
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 452..589
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT DISULFID 134..140
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT DISULFID 191..313
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT DISULFID 504..507
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00399"
FT CONFLICT 19
FT /note="Missing (in Ref. 1; AAB84084)"
FT /evidence="ECO:0000305"
FT CONFLICT 26
FT /note="G -> A (in Ref. 1; AAB84084)"
FT /evidence="ECO:0000305"
FT CONFLICT 53
FT /note="Missing (in Ref. 1; AAB84084)"
FT /evidence="ECO:0000305"
FT CONFLICT 59..60
FT /note="LR -> C (in Ref. 1; AAB84084)"
FT /evidence="ECO:0000305"
FT CONFLICT 65
FT /note="E -> A (in Ref. 1; AAB84084)"
FT /evidence="ECO:0000305"
FT CONFLICT 157..158
FT /note="PA -> D (in Ref. 1; AAB84084)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="S -> T (in Ref. 1; AAB84084)"
FT /evidence="ECO:0000305"
FT CONFLICT 342
FT /note="G -> A (in Ref. 1; AAB84084)"
FT /evidence="ECO:0000305"
FT CONFLICT 352..354
FT /note="FGA -> LR (in Ref. 1; AAB84084)"
FT /evidence="ECO:0000305"
FT CONFLICT 372..373
FT /note="NA -> T (in Ref. 1; AAB84084)"
FT /evidence="ECO:0000305"
FT CONFLICT 404..405
FT /note="GG -> R (in Ref. 1; AAB84084)"
FT /evidence="ECO:0000305"
FT CONFLICT 446..465
FT /note="GESDPIHPLGRSVPSIHAGP -> AGRTRSIRWAARCRRSIGA (in Ref.
FT 1; AAB84084)"
FT /evidence="ECO:0000305"
FT CONFLICT 492..494
FT /note="GKP -> QA (in Ref. 1; AAB84084)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 591 AA; 62907 MW; FA161AEDD58B2DC2 CRC64;
MRRLLTLILL LVALPAGAGL FDSRPGASLG GGLDGGGFLK VDQAFKPSVE RSDAQHVLLR
FVNAEGYYLY RHRFQFKVEP AQVSLGQVQL PAGKQHHDEY FGDTEVYYNI VDLEIPLNNP
ARQPYTLVVT YQGCADKGLC YPPETRRFDI DGGAATPAAS DAAGKGPLEH KGKRSLLFFF
LAGLTLTFTP CVLPMLPILS GVVLRGRPGG GRGFVLSLAY VLPMALCFAL LGALMGMFGA
SLNLQAQLQS PWVLVPFAAF FALFAVAMFG FFELRLPGFI REPLDRLAGD ARGGSILGAA
TLGVLSSLLV SPCVSAPLAA SLLYISASGD AWGGGLQLFA LGLGMGTPLV VFGAGGGALL
PKSGAWMNGV RNAFGVLLLA VAVWLLERVV SGPVALMLWG MLAGGAGLAL GALEFTPKSA
ARRLLQLLGL MFLTYAVAAW IGALQGESDP IHPLGRSVPS IHAGPPSTPG EWQNLTTPAQ
LDAALAEARQ AGKPVLLDWY ADWCISCKVI ERQVLTDPTV QARLPAYRLL RFDITESNPA
QRGLLDRYNL FGPPAILFFA PGGDEWSDLR VIGEIDAAGL AERLRRAATR Q
