ID A0A165JY96_9BURK Unreviewed; 750 AA.
AC A0A165JY96;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Protein-disulfide reductase {ECO:0000313|EMBL:KZT14821.1};
GN ORFNames=A1D30_16650 {ECO:0000313|EMBL:KZT14821.1};
OS Acidovorax sp. GW101-3H11.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=1813946 {ECO:0000313|EMBL:KZT14821.1, ECO:0000313|Proteomes:UP000077219};
RN [1] {ECO:0000313|Proteomes:UP000077219}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GW101-3H11 {ECO:0000313|Proteomes:UP000077219};
RA Ray J., Price M., Deutschbauer A.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KZT14821.1, ECO:0000313|Proteomes:UP000077219}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GW101-3H11 {ECO:0000313|EMBL:KZT14821.1,
RC ECO:0000313|Proteomes:UP000077219};
RX PubMed=29769716; DOI=10.1038/s41586-018-0124-0;
RA Price M.N., Wetmore K.M., Waters R.J., Callaghan M., Ray J., Liu H.,
RA Kuehl J.V., Melnyk R.A., Lamson J.S., Suh Y., Carlson H.K., Esquivel Z.,
RA Sadeeshkumar H., Chakraborty R., Zane G.M., Rubin B.E., Wall J.D.,
RA Visel A., Bristow J., Blow M.J., Arkin A.P., Deutschbauer A.M.;
RT "Mutant phenotypes for thousands of bacterial genes of unknown function.";
RL Nature 557:503-509(2018).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:KZT14821.1}.
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DR EMBL; LUKZ01000014; KZT14821.1; -; Genomic_DNA.
DR RefSeq; WP_063461606.1; NZ_LUKZ01000014.1.
DR AlphaFoldDB; A0A165JY96; -.
DR STRING; 1813946.A1D30_16650; -.
DR Proteomes; UP000077219; 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 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}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..750
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007860469"
FT TRANSMEM 352..374
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 395..414
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 434..455
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 476..498
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 510..534
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 546..566
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 572..593
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 600..618
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 625..750
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 750 AA; 78051 MW; ACABA45F20DCC017 CRC64;
MPSRPLYRLA VTLFLIAASA LWTGANAQFS PKTSGQGTSV VTTPYVRAEL LAHAPQGVAP
GQPLWLGLQI THQPEWHTYW KNPGDSGLPT DLAWTLPAGL DAGEIAWPLP KKIPIGTLAN
YGYEGTVLLP VPVTVASSFA PGPLVKDATI QLRASWLVCR KECIPEEGEF TLQLPIQSTT
ALSGAAFEAS AQAHPRPVLA GTTGIVPDSQ AQLAAEGNTL NVSVQGLPVA LRGKTLDLFP
ETAEVIDNAA SWKQRWNGSV WTAQIPLSAQ RSASPSLMPV VLAEQSPAHA TGPDTRNGYR
AELKVLGTWP PVASMTAVSP ALEAALKANA AQAGGAVTSA AGSGASSLTL TAALLGALLG
GLILNLMPCV FPVLAIKVVG FTQHAQDRRA HRISGIAYTA GVVLSFIALG ALMLGLRAAG
EAVGWGFQLQ SPAVVASLAA LFTLIALNLA GVFEFGHFLP SSVASLQARH PVADSFLTGV
LAVAVASPCT APFMGASLGL TATLPAPQAL AVFAALGLGL ALPYLAASFV PAVARALPRP
GAWMDTFRKL MAFPMLATVV WLVWVLGQQS GIDGAGALLI LLVGLSLVVW ALSLAGRARV
WMATVSIAAM ALLVWAFAPH ITHIPTAQAA TPSTQASATG WQPWAPGAAE QIVAGGRPVF
VDFTAAWCVT CQYNKKTTLA HADVLADLQT KNVALLRADW TRRDPAITAA LASLGRSGVP
VYVFYRPGKP PVVLTEVLSV DEVRATIAQL
//
