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
//