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Database: UniProt
Entry: A0A1E4HG57_9GAMM
LinkDB: A0A1E4HG57_9GAMM
Original site: A0A1E4HG57_9GAMM 
ID   A0A1E4HG57_9GAMM        Unreviewed;       710 AA.
AC   A0A1E4HG57;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=Protein-disulfide reductase {ECO:0000313|EMBL:ODT95862.1};
GN   ORFNames=ABS82_06790 {ECO:0000313|EMBL:ODT95862.1};
OS   Rhodanobacter sp. SCN 67-45.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Rhodanobacter.
OX   NCBI_TaxID=1660133 {ECO:0000313|EMBL:ODT95862.1, ECO:0000313|Proteomes:UP000094158};
RN   [1] {ECO:0000313|EMBL:ODT95862.1, ECO:0000313|Proteomes:UP000094158}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=26031303; DOI=10.1111/1462-2920.12936;
RA   Kantor R.S., van Zyl A.W., van Hille R.P., Thomas B.C., Harrison S.T.,
RA   Banfield J.F.;
RT   "Bioreactor microbial ecosystems for thiocyanate and cyanide degradation
RT   unravelled with genome-resolved metagenomics.";
RL   Environ. Microbiol. 17:4929-4941(2015).
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:ODT95862.1}.
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DR   EMBL; MEFB01000031; ODT95862.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E4HG57; -.
DR   Proteomes; UP000094158; 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   Gene3D; 2.60.40.1250; Thiol:disulfide interchange protein DsbD, N-terminal domain; 2.
DR   InterPro; IPR003834; Cyt_c_assmbl_TM_dom.
DR   InterPro; IPR035671; DsbD_gamma.
DR   InterPro; IPR028250; DsbDN.
DR   InterPro; IPR036929; DsbDN_sf.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
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; 2.
DR   Pfam; PF13899; Thioredoxin_7; 1.
DR   SUPFAM; SSF74863; Thiol:disulfide interchange protein DsbD, N-terminal domain (DsbD-alpha); 2.
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..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..710
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5009151782"
FT   TRANSMEM        332..356
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        377..396
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        416..437
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        458..484
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        490..516
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        537..555
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        567..584
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          580..710
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   710 AA;  74731 MW;  C150FA5F01009A98 CRC64;
     MRSLSAGPMF ARLLLGVGLL LAGLPALAQD TDALLPVTEA YQLSADAGTP GVLKLHWKVA
     PDYYLYRGRM KFKAGDGVTL GQAQLPEGRK YHDEYLGDVE TYHHDIDASI PYTVATGTTR
     LKLSVQYQGC HEVDPKICYP PHTEQLDLAL PTATAPTAPA GSLGAALDQL GRGGQSAATG
     VTRAPLPPEQ AFRFEALAQS PQQLLLRWTM PAGYYLYRDH TTLKLRKADG VQLGTPAWPA
     GVRHQDPQFG EVTVYFDQVE VPVALEGVPA RSGPLTLEAT FQGCQDGGLC YPLMTRTVQL
     DPGSGTVATG MPTSAARELP PATNGGPLRT SLFAALALAL GGGLILNLMP CVLPVLSIKA
     VGVLESGENP ATRRSHALFY TAGVLCSFAA LGLGILALRS AGHALGWGTQ LQQPVVVGVL
     ACVMLAVGLS MSGVVQFGAS LGNTGAGLAR RAGPAGDFFT GVLAVVVASP CTAPFMGGAL
     AYAFTAPMLS ALLVFLMLGI GLALPFLAIG FVPAVARWLP KPGRWMETLK QVLGADAVGL
     VLVAMVLLAM TLWWFERSRS RGVVSKLAVA VLAVATLVPM SLLSQVPPPT AARMADGVVP
     YSAEKLAALR EAGTPVFVDM TADWCVTCKA NEHTVLDTAR FRDLLQRTGA VYMKGDWTDV
     NPAISAFLAE YHSPGVPLYV VFPKDGGPGR QLSTVLTASM VERALTDAAR
//
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