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Database: UniProt
Entry: A0A0W0W0V8_9GAMM
LinkDB: A0A0W0W0V8_9GAMM
Original site: A0A0W0W0V8_9GAMM 
ID   A0A0W0W0V8_9GAMM        Unreviewed;       596 AA.
AC   A0A0W0W0V8;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
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=lidC {ECO:0000313|EMBL:KTD26069.1};
GN   Synonyms=dsbD {ECO:0000256|HAMAP-Rule:MF_00399};
GN   ORFNames=Lisr_1210 {ECO:0000313|EMBL:KTD26069.1};
OS   Legionella israelensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=454 {ECO:0000313|EMBL:KTD26069.1, ECO:0000313|Proteomes:UP000054761};
RN   [1] {ECO:0000313|EMBL:KTD26069.1, ECO:0000313|Proteomes:UP000054761}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bercovier 4 {ECO:0000313|EMBL:KTD26069.1,
RC   ECO:0000313|Proteomes:UP000054761};
RA   Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA   Pupko T., Shuman H.A., Segal G.;
RT   "Genomic analysis of 38 Legionella species identifies large and diverse
RT   effector repertoires.";
RL   Submitted (NOV-2015) 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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KTD26069.1}.
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DR   EMBL; LNYH01000058; KTD26069.1; -; Genomic_DNA.
DR   RefSeq; WP_058501566.1; NZ_UGOE01000002.1.
DR   AlphaFoldDB; A0A0W0W0V8; -.
DR   STRING; 454.Lisr_1210; -.
DR   PATRIC; fig|454.4.peg.1304; -.
DR   OrthoDB; 9811036at2; -.
DR   Proteomes; UP000054761; 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; IPR036249; Thioredoxin-like_sf.
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; PF13899; Thioredoxin_7; 1.
DR   SUPFAM; SSF74863; Thiol:disulfide interchange protein DsbD, N-terminal domain (DsbD-alpha); 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 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:UP000054761};
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..25
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT   CHAIN           26..596
FT                   /note="Thiol:disulfide interchange protein DsbD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT                   /id="PRO_5008997565"
FT   TRANSMEM        179..211
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT   TRANSMEM        223..247
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT   TRANSMEM        259..281
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT   TRANSMEM        302..332
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT   TRANSMEM        338..361
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT   TRANSMEM        373..393
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT   TRANSMEM        399..419
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT   TRANSMEM        431..450
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT   DOMAIN          447..590
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DISULFID        119..125
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT   DISULFID        198..320
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
FT   DISULFID        505..508
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00399"
SQ   SEQUENCE   596 AA;  65039 MW;  4D19ECC4B24D6B36 CRC64;
     MLRWLWLAVC CCVSLTVYSN TPAPAAEVFQ VETKTVDPNT FLVNWQIKPG YFLYANRIKL
     TEPLDNNAQL NIIQFPKAEK KTDRQGKTFS IYRNELSLPV AVLGTQPGEA VVSLHYQGCA
     EDGFCYPPEK RQIKLTINEN KELVSASLEP LPAADKTIIA EQQTREAISK EEAVFAHNWP
     FIILSFFGFG LLLAFTPCVL PMVPVLSGII VGHGENMTTG KAFFLSLSYV LSMAVTYAIV
     GAVVALLGSN LQVIMQSAWS ITAFSLLFIL LSLSMFGFYE LRLPASWQAK LASVSRNQTS
     GHYLGAAVMG CLSTLILSPC VTAPLIGALS YIAHSGNLIL GSLALFFLGL GMGTPLLLLG
     TSAGKLLPKA GPWMNAVKSF FGFLLLAMAI YLIQRLLPAF VVMILWAALL IFAGIYSGAL
     TTQASNKFSQ GIGVILFVYG LLILIGASMG SHNPVQPLQP VMTQGFLVPA EANIKKPVTT
     IAETKQAIEQ AQGKPVLVDF YADWCNSCKV MEATTFKDPS VIKALKNFVI LKADVTANNR
     EEKALLEHYN VVAPPTFLFF DKEGNEIKPL RTVGEIEAES FLKKIKAYHQ LTAKES
//
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