ID U2GAQ9_9BURK Unreviewed; 569 AA.
AC U2GAQ9;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=Cytochrome c-type biogenesis protein DsbD, protein-disulfide reductase {ECO:0000313|EMBL:ERJ40185.1};
GN ORFNames=L810_5052 {ECO:0000313|EMBL:ERJ40185.1};
OS Burkholderia sp. AU4i.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=1335308 {ECO:0000313|EMBL:ERJ40185.1, ECO:0000313|Proteomes:UP000016616};
RN [1] {ECO:0000313|EMBL:ERJ40185.1, ECO:0000313|Proteomes:UP000016616}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AU4i {ECO:0000313|EMBL:ERJ40185.1,
RC ECO:0000313|Proteomes:UP000016616};
RA Devi U., Khatri I., Kumar N., Kumar L., Singh D., Sharma D.,
RA Subramanian S., Saini A.K.;
RT "Genome Assembly of Burkholderia vietnamiensis AU4i.";
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
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:ERJ40185.1}.
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DR EMBL; ASSI01000034; ERJ40185.1; -; Genomic_DNA.
DR AlphaFoldDB; U2GAQ9; -.
DR PATRIC; fig|1335308.3.peg.1322; -.
DR Proteomes; UP000016616; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma 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; 1.
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; 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; 1.
DR Pfam; PF13899; Thioredoxin_7; 1.
DR SUPFAM; SSF74863; Thiol:disulfide interchange protein DsbD, N-terminal domain (DsbD-alpha); 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 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 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 TRANSMEM 149..172
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 193..219
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 225..249
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 270..298
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 304..325
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 337..360
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 366..386
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 398..419
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 440..564
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 569 AA; 60327 MW; F42FB63578252342 CRC64;
MTVSLASPME VVLDFKTKPG YYLYRDRISF AVDGTLVKPD SMPPSESKND PTFGVVQVYH
QPVRIRLPLS AAITSSAMLT VTSQGCADVG VCYPPQTRRF RIAADGAVTL AALVGSANAA
DFPVVEKSRQ SAVPGLPLRP ANGIGIAELL GFLVAGLLMA GTVCMYPLIP IVTAVINGTR
ERLPVWRGVS LSFAYVQGLA MTYAAAGTIA AVVGIPLVAV TQKPWLLATF GALMLILALG
MFGVFRLQLP TGWQTRFAGW SRRLPGGRVG PVFVMGMLSA LIVGPCSTPA LAGALVYIAN
SHDIAGGTLA LYLMGIGIGI PLLLVGTFGT RLLPKSGHWM VAVQNTLGVM LLAAALWFVY
SLLPVWLLMS LVALLLTACG MMLRAIDPLP AGATGIARVG KALGVLLLVA GIAEFVGVAS
GNFDMLMPLG GLTRMSASAG GGASSAARFD TITSNAKLDE ALKLARGTPV MVDFYADWCI
TCKELERFTF TDARVMDEFT HWKLLRIDVT KNTEADTAML RRFGLFGPPA LIFFDKTGRE
QPDAQLVGFI GADAFLAHLK RLQSSDVAQ
//
