ID A0A0C5WJT8_9FLAO Unreviewed; 658 AA.
AC A0A0C5WJT8;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Thiol:disulfide interchange protein DsbD {ECO:0000313|EMBL:AJR03010.1};
GN ORFNames=AW14_04565 {ECO:0000313|EMBL:AJR03010.1};
OS Siansivirga zeaxanthinifaciens CC-SAMT-1.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Siansivirga.
OX NCBI_TaxID=1454006 {ECO:0000313|EMBL:AJR03010.1, ECO:0000313|Proteomes:UP000032229};
RN [1] {ECO:0000313|EMBL:AJR03010.1, ECO:0000313|Proteomes:UP000032229}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-SAMT-1 {ECO:0000313|EMBL:AJR03010.1,
RC ECO:0000313|Proteomes:UP000032229};
RA Young C.-C., Hameed A., Huang H.-C., Shahina M.;
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP007202; AJR03010.1; -; Genomic_DNA.
DR RefSeq; WP_044637716.1; NZ_CP007202.1.
DR AlphaFoldDB; A0A0C5WJT8; -.
DR STRING; 1454006.AW14_04565; -.
DR KEGG; sze:AW14_04565; -.
DR PATRIC; fig|1454006.5.peg.892; -.
DR HOGENOM; CLU_015841_0_0_10; -.
DR OrthoDB; 9811036at2; -.
DR Proteomes; UP000032229; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 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.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000032229};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..658
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002184419"
FT TRANSMEM 183..207
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 228..250
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 262..283
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 304..331
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 343..363
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 375..393
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 413..430
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 442..466
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 33..141
FT /note="Thiol:disulfide interchange protein DsbD N-terminal"
FT /evidence="ECO:0000259|Pfam:PF11412"
FT DOMAIN 190..379
FT /note="Cytochrome C biogenesis protein transmembrane"
FT /evidence="ECO:0000259|Pfam:PF02683"
SQ SEQUENCE 658 AA; 72172 MW; 2D9AFB999A76C9FE CRC64;
MKKFLLLLSV FITSFLSQAQ VLEPVKWSTS VEKISDTEYE LISKATIEKG WHLYSQTVPE
DGPIATTFTY DDSEGNFKIS GNTSEEEGHT VDDPVFGMKI KFFEKSATFK QKVSIEGDVK
TINAFVEFMV CDDTRCLPPT EVDLVFNVSN EPKTAITEVK QQNTEDAAVN TGNTEDNPAE
KGLWSIFFIA FFSGFAALLT PCVFPMIPMT VSFFTKQSKT KAAGIRNAII YGVSIIVIYV
LLGILVSLIF GADALNALST NVWFNIAFFI LLLIFAASFL GAFEIMLPNK WANKVDSQAD
RGGLIGIFFM ALALAIVSFS CTGPIVGTLL VQAAAGGSQT GPIVGMLGFS LAIALPFALF
AAFPGWLNSL PKSGGWLNTV KVVLGFLELA LAFKFLSNAD LVLQAHLLER EVFIAIWIAI
FGALAFYLFG KIQLPHDSPV TYISVGRLSL GLVVLSFTIY MIPGLWGAPL NLISAFPPPQ
HYSESPYGVG YTKVGSSAAT ASHDALPDGA HLMAPHDILA FNDYDKGLAY AKQVGKPVMI
DFTGHACVNC RKMENNVWIK PHILDILKND VVLISLYVDD KRPLAEGDVV ESKLNPGKKL
KYIGQKWSEL QTIKYKANTQ PMYVLMDHNE ENLIDPVAYT PDVDAYHNWL KTGVSNFK
//