ID A0A0R2S8E8_9FLAO Unreviewed; 582 AA.
AC A0A0R2S8E8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Disulfide bond formation protein DsbD {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=ABR83_03945 {ECO:0000313|EMBL:KRO71196.1};
OS Cryomorphaceae bacterium BACL18 MAG-120924-bin36.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Cryomorphaceae.
OX NCBI_TaxID=1655591 {ECO:0000313|EMBL:KRO71196.1, ECO:0000313|Proteomes:UP000051105};
RN [1] {ECO:0000313|EMBL:KRO71196.1, ECO:0000313|Proteomes:UP000051105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BACL18 MAG-120924-bin36 {ECO:0000313|EMBL:KRO71196.1};
RA Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J.,
RA Andersson A.F.;
RT "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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:KRO71196.1}.
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DR EMBL; LIBP01000192; KRO71196.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2S8E8; -.
DR Proteomes; UP000051105; Unassembled WGS sequence.
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 SUPFAM; SSF52833; Thioredoxin-like; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..582
FT /note="Disulfide bond formation protein DsbD"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006423425"
FT TRANSMEM 218..242
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 263..286
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 339..362
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 374..398
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 410..428
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 448..467
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 479..498
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 36..142
FT /note="Thiol:disulfide interchange protein DsbD N-terminal"
FT /evidence="ECO:0000259|Pfam:PF11412"
FT DOMAIN 226..405
FT /note="Cytochrome C biogenesis protein transmembrane"
FT /evidence="ECO:0000259|Pfam:PF02683"
FT REGION 166..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 582
FT /evidence="ECO:0000313|EMBL:KRO71196.1"
SQ SEQUENCE 582 AA; 62698 MW; 445E63C84FA5557B CRC64;
MNRLFYALAA LLLASSAAFA QILQPVTWST SVRTLDAGKL ELVATAKIDA GWHVYSQFIG
ADGPIPTAFT LPASKDLKTE GPVREPKPIK EFDKNFGMEL AYFAKKADFV ITAKRISNAA
FTYTAEVEFM VCDDERCLPP DYVSLVFKVP AAAEPELVGE SQLNAPKEDP ATAQEPTSQE
PTAVESQEPS GQPAGDQAPA EAQEPAAAEG QEAEAVNLWA LFGAGMLGGF FALIMPCIFP
MIPLTVSFFL KQSKSKADGF RKALLYGLSI NVIYVVLGLL VTIIFGSEAL NAMATNPWFN
LAFFALFVVF AISFFGAFEI TLPSSWVNKA DDQSQRGGLL GIFFMAFTLA LVSFSCTGPL
IGQLLVATAV SGELLGPAIG MFGFSFALSL PFVLFAAFPG WLKGLPKSGG WLNTVKVTLG
FLELAFALKF LSTADMVWQK HWVERELFLA LWVGIAFATA LYLFGVFRMP HDDEPKGGIG
VGRMLTGVVF LVTGFYLLPG IWGAPVKLVA GFPPPSFYAE NPNGMGVSSA PSGEKKPSAK
AHCPLNLPCF NDYESARTYA IEAGKPILLD FTGWGCVNCR KM
//