ID Q04RG3_LEPBJ Unreviewed; 440 AA.
AC Q04RG3;
DT 14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 14-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Protein-disulfide reductase {ECO:0000313|EMBL:ABJ76507.1};
GN Name=dsbD {ECO:0000313|EMBL:ABJ76507.1};
GN OrderedLocusNames=LBJ_1993 {ECO:0000313|EMBL:ABJ76507.1};
OS Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197).
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=355277 {ECO:0000313|EMBL:ABJ76507.1, ECO:0000313|Proteomes:UP000000656};
RN [1] {ECO:0000313|EMBL:ABJ76507.1, ECO:0000313|Proteomes:UP000000656}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JB197 {ECO:0000313|EMBL:ABJ76507.1,
RC ECO:0000313|Proteomes:UP000000656};
RX PubMed=16973745; DOI=10.1073/pnas.0603979103;
RA Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A., Cullen P.A.,
RA Davis J., Johnson M., Kuczek E., Alt D.P., Peterson-Burch B., Coppel R.L.,
RA Rood J.I., Davies J.K., Adler B.;
RT "Genome reduction in Leptospira borgpetersenii reflects limited
RT transmission potential.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(2006).
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DR EMBL; CP000350; ABJ76507.1; -; Genomic_DNA.
DR AlphaFoldDB; Q04RG3; -.
DR KEGG; lbj:LBJ_1993; -.
DR HOGENOM; CLU_014657_3_1_12; -.
DR Proteomes; UP000000656; Chromosome 1.
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 InterPro; IPR003834; Cyt_c_assmbl_TM_dom.
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; PF13899; Thioredoxin_7; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 40..61
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 154..179
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 191..216
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 228..245
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 257..277
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 289..308
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 46..236
FT /note="Cytochrome C biogenesis protein transmembrane"
FT /evidence="ECO:0000259|Pfam:PF02683"
SQ SEQUENCE 440 AA; 48441 MW; B6E97083975A0D58 CRC64;
MSALFLGLPL SAETLSGSWF SGIRKSISEG ISSGTFDWTS GFLLIAGGVL ASLLPCVYPL
YPITVGIVRA RGEGSPRILH PAIYYFGLIT IYASFGLIAG LSGGAFNVIL RYPIVNLALS
VLIFLLALGS LDLIHLPFFQ SKEVKTVQGC GGTFFLGMGA GLLSSPCVGP VVVAILLRIT
VDSGAISVDS VLLAVFKMFL FGVGLGFPFL MIGVFGLSLP KSGKWMRWIQ WVLGIFVLYF
SYAYFQKSLL GWEISDSLIP LSAFGILFLL LCIYFFLPEE WDRYVRMKKT LFLGGVVLSA
VGLVILFTQN LRGSNSVSAM EIETRGNLSW FRSTSKAYKE AAITGKKMFV DFYADWCTNC
NAFEELTQSD SVLNEALQGV VLLKIKDQDP IFETYVKDSR FEELKIGLPF FVILDAEGNL
LYKNTDYQDT ETMIQTLKQP
//
