ID G0L6Y2_ZOBGA Unreviewed; 655 AA.
AC G0L6Y2;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Thiol:disulfide interchange protein {ECO:0000313|EMBL:CAZ98736.1};
DE EC=1.8.1.8 {ECO:0000313|EMBL:CAZ98736.1};
GN Name=dsbD {ECO:0000313|EMBL:CAZ98736.1};
GN OrderedLocusNames=zobellia_4601 {ECO:0000313|EMBL:CAZ98736.1};
OS Zobellia galactanivorans (strain DSM 12802 / CCUG 47099 / CIP 106680 /
OS NCIMB 13871 / Dsij).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Zobellia.
OX NCBI_TaxID=63186 {ECO:0000313|EMBL:CAZ98736.1, ECO:0000313|Proteomes:UP000008898};
RN [1] {ECO:0000313|Proteomes:UP000008898}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij
RC {ECO:0000313|Proteomes:UP000008898};
RG Genoscope - CEA;
RT "Complete genome sequence of Zobellia galactanivorans Dsij.";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CAZ98736.1, ECO:0000313|Proteomes:UP000008898}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij
RC {ECO:0000313|Proteomes:UP000008898};
RX PubMed=22513138; DOI=10.1111/j.1462-2920.2012.02751.x;
RA Thomas F., Barbeyron T., Tonon T., Genicot S., Czjzek M., Michel G.;
RT "Characterization of the first alginolytic operons in a marine bacterium:
RT from their emergence in marine Flavobacteriia to their independent
RT transfers to marine Proteobacteria and human gut Bacteroides.";
RL Environ. Microbiol. 14:2379-2394(2012).
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DR EMBL; FP476056; CAZ98736.1; -; Genomic_DNA.
DR RefSeq; WP_013995923.1; NC_015844.1.
DR AlphaFoldDB; G0L6Y2; -.
DR STRING; 63186.ZOBELLIA_4601; -.
DR KEGG; zga:ZOBELLIA_4601; -.
DR PATRIC; fig|63186.3.peg.4510; -.
DR HOGENOM; CLU_015841_0_0_10; -.
DR OrthoDB; 9811036at2; -.
DR Proteomes; UP000008898; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0047134; F:protein-disulfide reductase (NAD(P)) activity; IEA:UniProtKB-EC.
DR GO; GO:0017004; P:cytochrome complex assembly; IEA:InterPro.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR003834; Cyt_c_assmbl_TM_dom.
DR InterPro; IPR028250; DsbDN.
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 Oxidoreductase {ECO:0000313|EMBL:CAZ98736.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008898};
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..655
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003402737"
FT TRANSMEM 194..215
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 236..255
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 275..296
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 317..340
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 360..383
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 395..413
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 428..445
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 465..484
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 36..146
FT /note="Thiol:disulfide interchange protein DsbD N-terminal"
FT /evidence="ECO:0000259|Pfam:PF11412"
FT DOMAIN 202..402
FT /note="Cytochrome C biogenesis protein transmembrane"
FT /evidence="ECO:0000259|Pfam:PF02683"
SQ SEQUENCE 655 AA; 73451 MW; C293238E845DA8A8 CRC64;
MKHIIVFISL FFSFLSLFGQ DDDNPVKWSQ EVRKINDTDY ELVLKGDIYE GWHIYSQFTS
EGGSLPSEFT YKKAGETYEL LGETTESETV VEYSDIFEVD ETFFKGSAIF TQKIRLLDPS
VNQIDINFFY QICKEVCIPV DEDFSFVLDG GVAVTENKTI DERSKQLSSA LKLDLKNKEA
LKDVKEDIGT GSSLWMVFGL GFLGGLIALL TPCVFPMIPL TVSFFTKHSK QKSKGVVNAL
LYGFFIVLIY FLLSLPFHVF DSVDSQILNT IATNIWLNIA FFLIFVFFSF SFFGYYELTL
PSSWANKMDA ASSKIGGVIG IFFMAVTLAI VSFSCTGPIL GGLLGSTVLE EGDVAMNLSA
GMTGFGVALA LPFALFALFP AWLNSLPKSG GWMTTVKVVL GFLELALALK FLSNADLVGN
WGILKREIFL AIWVVLYVLL TLYLFGIFRF PHDGPKAKLS MGRKAVGLLS MGVSIYILLG
LLGVSNLKLL SGFPPPAFYS VSETESDCPL GINCFKDFEE GVAYAKKVDK PILLDFTGWA
CVNCRKMEEN VWSEPDIYSI LNEDYVLISL YVDDRKELPE TEKFDFQYDS GRIKHIETVG
QKWGTFQSVN FNAASQPFYV LMTPDLEILS HPVQYTDSET YRKWLQFGLA RYKEK
//
