ID   A0A1G7CV27_9BURK        Unreviewed;       766 AA.
AC   A0A1G7CV27;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Thiol:disulfide interchange protein DsbD {ECO:0000313|EMBL:SDE43202.1};
GN   ORFNames=SAMN05192589_11753 {ECO:0000313|EMBL:SDE43202.1};
OS   Paracidovorax valerianellae.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Paracidovorax.
OX   NCBI_TaxID=187868 {ECO:0000313|EMBL:SDE43202.1, ECO:0000313|Proteomes:UP000198781};
RN   [1] {ECO:0000313|EMBL:SDE43202.1, ECO:0000313|Proteomes:UP000198781}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16619 {ECO:0000313|EMBL:SDE43202.1,
RC   ECO:0000313|Proteomes:UP000198781};
RA   de Groot N.N.;
RL   Submitted (OCT-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; FMZC01000017; SDE43202.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G7CV27; -.
DR   STRING; 187868.SAMN05192589_11753; -.
DR   Proteomes; UP000198781; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015036; F:disulfide oxidoreductase activity; IEA:UniProt.
DR   GO; GO:0017004; P:cytochrome complex assembly; IEA:InterPro.
DR   CDD; cd02953; DsbDgamma; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR003834; Cyt_c_assmbl_TM_dom.
DR   InterPro; IPR035671; DsbD_gamma.
DR   InterPro; IPR028250; DsbDN.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR32234:SF3; SUPPRESSION OF COPPER SENSITIVITY PROTEIN; 1.
DR   PANTHER; PTHR32234; 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; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198781};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   TRANSMEM        366..391
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        412..432
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        452..471
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        491..510
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        522..542
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        563..582
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        588..609
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        616..634
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          637..766
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   766 AA;  78959 MW;  E96F145B2E074888 CRC64;
     MSPVPAQEPN PEAAAPTCDM SHRLLQRLLP ALLLIAASAL PISAGAQFGP KTTAATTTAA
     GGSASGSSTV TTPHVQAELV AHAPEGVAPG KPLWLGLSIT HQPEWHTYWM NSGDSGLPTE
     LEWQVPAGIE AGAIAWPVPR KIPIGNLANY GYEGTVLLPV PMTVSSAFAP GPLARTATFH
     LRASWLVCRK ECIPEEGDFT LQLPIRSTTA LNAGAFEAAQ QAHPQPLPAP AGGGAASSAR
     VDGNAIALTV AGLPPALRGQ ALEFFPETTG AIETAADWTQ AWQGDVWTAR VPLSAQRSAS
     PVPMPVVLAH AGRGWRAELP VDGGWPKAAA MASVSPALEA ALRANAAQGG AAPVAPQVTA
     APLATLLAAL AGALLGGLIL NLMPCVFPVL AIKVVGFAQH AQNRRAHRIG GLAYTAGVVL
     SFMALGALML ALRAAGEAVG WGFQLQSPGV VALLAALFTV IGLNLAGVFE FGRFLPSSVA
     TLQARHPAVD AFLTGVLAVA VASPCTAPFM GASLGLTATL PAAQALAVFA ALGVGLALPY
     LAASWVPAVA RALPRPGAWM DTLRRFMAFP MFATVVWLVW VLGQQSGIDG AAALLALLVM
     LAMAVWALTL AGRTRWAIAT ISIAALAYMT AVWGPKVVEI PPLPAATASA AATAGGWRPW
     QAGLPEQLVA QGQPVFVDYT AAWCVTCQYN KKTTLAHEDV LKDFAAKNVA LLRADWTRRD
     PAITAALAQL GRSGVPVYVL QAPGRPPVVL SEILGVQEVR AALAGL
//