ID A0A1U7D3D4_9RHOB Unreviewed; 600 AA.
AC A0A1U7D3D4;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Thiol:disulfide interchange protein DsbD {ECO:0000313|EMBL:APX22580.1};
DE EC=1.8.1.8 {ECO:0000313|EMBL:APX22580.1};
DE Flags: Precursor;
GN ORFNames=Ga0080559_TMP1784 {ECO:0000313|EMBL:APX22580.1};
OS Salipiger profundus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Salipiger.
OX NCBI_TaxID=1229727 {ECO:0000313|EMBL:APX22580.1, ECO:0000313|Proteomes:UP000186559};
RN [1] {ECO:0000313|EMBL:APX22580.1, ECO:0000313|Proteomes:UP000186559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JLT2016 {ECO:0000313|EMBL:APX22580.1,
RC ECO:0000313|Proteomes:UP000186559};
RA Tang K.;
RT "Deep-sea bacteria in the southern Pacific.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP014796; APX22580.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1U7D3D4; -.
DR STRING; 1229727.Ga0080559_TMP1784; -.
DR KEGG; tpro:Ga0080559_TMP1784; -.
DR Proteomes; UP000186559; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0047134; F:protein-disulfide reductase (NAD(P)) activity; IEA:UniProtKB-EC.
DR GO; GO:0017004; P:cytochrome complex assembly; IEA:InterPro.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 2.60.40.1250; Thiol:disulfide interchange protein DsbD, N-terminal domain; 1.
DR InterPro; IPR003834; Cyt_c_assmbl_TM_dom.
DR InterPro; IPR028250; DsbDN.
DR InterPro; IPR036929; DsbDN_sf.
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 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000313|EMBL:APX22580.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000186559};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..600
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010578319"
FT TRANSMEM 196..227
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 239..264
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 276..297
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 317..346
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 352..373
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 394..411
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 417..433
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 440..464
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 478..600
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 129..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 600 AA; 61311 MW; 96DE0198AAD8A46A CRC64;
MMMLRFCLMV FLTTLAAPLA AQSPLPADEA FRLEVAREGD TLVATWEIAE GYYLYRDFMG
AEDGSGAALP MALPDGEMKD DPNFGEVEIF HEGVQARIEG ADGPVTLRWQ GCEEDSICYP
PQTRTIEAGA DGGMSTPGAS PAESTQGFQG SGFTRVGDGA STGTGAEVEP EQTADGGLVL
AKTDGLIERF STGGTLMVVA GFFGLGLLLS LTPCVFPMIP IVAGMVAGGS QRPSARRGAL
LGGAYVLGMA GAFALIGAAA AWSGENLQIA LQSPPAVILT AGLFVLLAVA AFGLFELRMP
AAVTARLNRV EGRRGSLPGA ALLGVTSALI VGPCVTAPLA GALLYIAQSG DLLLGAVALF
ALGLGQGLPL VAVAAFGPQV LPRSGAWMER IRQLFGLVFL GLAVWMLGRI LPGPVTLALW
SALLIGAGAA LFPREAPAPL VAALAVILGF AGALQGVGAA MGAVDPLKPL APLAARDASA
AQADPFATVT GTDGLESALA ASEAPALVYV TADWCTTCRS IERGPLSDPQ VLAALEGVTP
IKVDVSDFDD EAQRALDLLG AAGPPTMVFL DAARAEVPGT RLVGDVHEEA LLAALREAAR
//