ID A0A0A2MAJ3_9FLAO Unreviewed; 695 AA.
AC A0A0A2MAJ3;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Thiol:disulfide interchange protein DsbD {ECO:0000313|EMBL:KGO85310.1};
GN ORFNames=Q765_16970 {ECO:0000313|EMBL:KGO85310.1};
OS Flavobacterium rivuli WB 3.3-2 = DSM 21788.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1121895 {ECO:0000313|EMBL:KGO85310.1, ECO:0000313|Proteomes:UP000030152};
RN [1] {ECO:0000313|EMBL:KGO85310.1, ECO:0000313|Proteomes:UP000030152}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WB 3.3-2 {ECO:0000313|EMBL:KGO85310.1,
RC ECO:0000313|Proteomes:UP000030152};
RA Zeng Z., Chen C.;
RL Submitted (SEP-2013) 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:KGO85310.1}.
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DR EMBL; JRLX01000024; KGO85310.1; -; Genomic_DNA.
DR RefSeq; WP_020214318.1; NZ_KB899973.1.
DR AlphaFoldDB; A0A0A2MAJ3; -.
DR STRING; 1121895.GCA_000378485_03155; -.
DR eggNOG; COG4232; Bacteria.
DR OrthoDB; 9811036at2; -.
DR Proteomes; UP000030152; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000030152};
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..695
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001992070"
FT TRANSMEM 225..246
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 307..328
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 340..361
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 381..405
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 417..435
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 455..475
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 487..508
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 38..140
FT /note="Thiol:disulfide interchange protein DsbD N-terminal"
FT /evidence="ECO:0000259|Pfam:PF11412"
FT DOMAIN 229..410
FT /note="Cytochrome C biogenesis protein transmembrane"
FT /evidence="ECO:0000259|Pfam:PF02683"
FT REGION 182..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 695 AA; 76178 MW; 0D81F3B30D15323D CRC64;
MKKLATLFFL LFAMFISQAQ VKEPVKWTSK IEKKSATEYI LVFSATIEND WHMYSQFSDE
NGAIPLEVVF NNAKGNYTAV GKAAESKTEK AFNDVFGVTE TFWSHNAQLK QTVKITNPAN
EVIQVELDYQ VCKEVCIQGS NLFEFNTKSL AAKEVKNFSA VSVTTTKKDE LTAVKADTAI
QSSTTQVTEQ PSTAQDTAKT ATASATSKTE KSKPADEEST SPLKIFLLTL LAGIGVTFTP
CVFPMIPMTV SFFIKQNASK SKGKFNALFY GICIIAIYVL LSVPFHVFEG LDKNIFADIS
TNVYLNIFFF LIFVTFAISF FGAFEITIPS SIANKADSAS NLGGLIGVFF MALTLIIVSF
SCTGPVLSFV FGTVLSSDGG AVLLTLGMFG FGLGLALPFM VFALFPSLMS GLPKSGGWLN
TVKVVFGFIE LALAFKFLSN ADLVLQLHYL EREVFIAIWV AIFTALALYL FGKFLMPHDS
PVPFLSVGRM LLGVIAFAFT VYLVPGLWGA PLKLLSGITP PLNYSESPLG FGGSANIAGA
TSNKLPDGAK VAVHGIIAFE DYDKGLAYAK QVNKPILLDF TGRACVNCRK MEEGVWVDPE
VLAILKNDVV LISLYGDEQI ELPENEQFIS KFSGRKITTV GKKWSDFQLG RYNSNARPFY
VLMGLDEKNL NEPVAYTPDI KEYLAWLQQG VENFK
//
