ID B0RN48_XANCB Unreviewed; 768 AA.
AC B0RN48;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE SubName: Full=Thiol:disulfide interchange protein {ECO:0000313|EMBL:CAP49883.1};
DE EC=1.8.1.8 {ECO:0000313|EMBL:CAP49883.1};
GN Name=dsbD {ECO:0000313|EMBL:CAP49883.1};
GN ORFNames=XCCB100_0549 {ECO:0000313|EMBL:CAP49883.1};
OS Xanthomonas campestris pv. campestris (strain B100).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=509169 {ECO:0000313|EMBL:CAP49883.1, ECO:0000313|Proteomes:UP000001188};
RN [1] {ECO:0000313|EMBL:CAP49883.1, ECO:0000313|Proteomes:UP000001188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B100 {ECO:0000313|EMBL:CAP49883.1,
RC ECO:0000313|Proteomes:UP000001188};
RX PubMed=18304669; DOI=10.1016/j.jbiotec.2007.12.013;
RA Vorholter F.J., Schneiker S., Goesmann A., Krause L., Bekel T., Kaiser O.,
RA Linke B., Patschkowski T., Ruckert C., Schmid J., Sidhu V.K., Sieber V.,
RA Tauch A., Watt S.A., Weisshaar B., Becker A., Niehaus K., Puhler A.;
RT "The genome of Xanthomonas campestris pv. campestris B100 and its use for
RT the reconstruction of metabolic pathways involved in xanthan
RT biosynthesis.";
RL J. Biotechnol. 134:33-45(2008).
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DR EMBL; AM920689; CAP49883.1; -; Genomic_DNA.
DR AlphaFoldDB; B0RN48; -.
DR KEGG; xca:xcc-b100_0549; -.
DR HOGENOM; CLU_014657_2_1_6; -.
DR Proteomes; UP000001188; 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 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 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; 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.
PE 4: Predicted;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000313|EMBL:CAP49883.1};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..768
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002752036"
FT TRANSMEM 372..396
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 417..436
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 456..477
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 498..524
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 530..552
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 572..588
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 594..614
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 626..648
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 36..150
FT /note="Thiol:disulfide interchange protein DsbD N-terminal"
FT /evidence="ECO:0000259|Pfam:PF11412"
FT DOMAIN 193..308
FT /note="Thiol:disulfide interchange protein DsbD N-terminal"
FT /evidence="ECO:0000259|Pfam:PF11412"
FT DOMAIN 380..561
FT /note="Cytochrome C biogenesis protein transmembrane"
FT /evidence="ECO:0000259|Pfam:PF02683"
FT REGION 338..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 768 AA; 81831 MW; 5C376A6FC8F976D4 CRC64;
MKSLSRWIAR CAVLVAPLFV ALPLLLTAPA AQAVTEADLL PVDQAFALSA KADGRDRIAL
TWKIAPGYYL YRHRISVKSG QGFTAGALDL PEGESKHDEF FGQVQTYRTA LQASLAGKAA
PGQRSAILQV QYQGCADAGV CYPPQRRELR VDLPDAPTTA PPRESLGALV PRGPSGARLF
GAPGQTAGVD ALPLPADQAF NFEAIVGDGN SLLLRFTPAP GYYLYRDRTS LSLEGTSDIR
TGLPRWPQGR THRDEHFGDV VVYFDQAEVT LPLLRDRPDP ARVTLVATFQ GCQSDGICYP
PMTRRVRLDL PAGTVSPHNQ ATATPLLISP LSAGEVAAER AAPPAPADAA PGPDATAGNP
ERSRPPHLER NLLAILLLAL AGGLVLNLMP CVLPILSLKV LGLAHSGESR NHARSHAIWY
SLGVLVSFAA IGGLVIGLRA AGQAAGWGFQ LQQPWFVAAL AYLMFAVGLS LSGVFTLGSN
LGGIGQSLAA RNGPLGDFFT GVLACVVASP CIAPFMGTAL AYAFTAPAPL AMLVFLTLGL
GLALPFLLIG FIPSLARRLP TPGAWMETLK QVLAFPMYLT AIWLLWVLGK QRGVDALALM
LVGATLLALG LWWFERSRWN SHRLGMGLAA AMLVLAIVPV VAVTRLSLPR ATATEGSVTY
TPELLDRLRA DNRVVFVNMT ADWCVTCKAN EKNVLSSTDF RDALRRVDAV YMKGDWTNVD
PKISAFLDQH QAVGVPLYVV YGPGAPPAVL PTVLTGAITE DALLRAAR
//
