ID A0A0R2RVP3_9FLAO Unreviewed; 663 AA.
AC A0A0R2RVP3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Disulfide bond formation protein DsbD {ECO:0000313|EMBL:KRO66422.1};
GN ORFNames=ABR84_01180 {ECO:0000313|EMBL:KRO66422.1};
OS Cryomorphaceae bacterium BACL21 MAG-121220-bin10.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Cryomorphaceae.
OX NCBI_TaxID=1655592 {ECO:0000313|EMBL:KRO66422.1, ECO:0000313|Proteomes:UP000051758};
RN [1] {ECO:0000313|EMBL:KRO66422.1, ECO:0000313|Proteomes:UP000051758}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BACL21 MAG-121220-bin10 {ECO:0000313|EMBL:KRO66422.1};
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:KRO66422.1}.
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DR EMBL; LICC01000055; KRO66422.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2RVP3; -.
DR STRING; 1655592.ABR84_01180; -.
DR Proteomes; UP000051758; 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 Pfam; PF13899; Thioredoxin_7; 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..663
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006423007"
FT TRANSMEM 200..221
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 282..299
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 320..342
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 362..381
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 393..411
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 431..453
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 465..484
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 24..153
FT /note="Thiol:disulfide interchange protein DsbD N-terminal"
FT /evidence="ECO:0000259|Pfam:PF11412"
FT DOMAIN 205..398
FT /note="Cytochrome C biogenesis protein transmembrane"
FT /evidence="ECO:0000259|Pfam:PF02683"
SQ SEQUENCE 663 AA; 73505 MW; 62F132F4CB3898B1 CRC64;
MKAFKLVYLF TLLGVFSAQA QEFLDPVTWQ VSVEPVKNDQ YTIVMEATID SGWHLYSQTQ
FGDQYEGPIR TEFLYNDSDS TFRLSGTTLE PAVAAVFDPV FELDVIYFED HVRFEQTIQV
INPEGLQITA EVYYSVCDAE KCLPPDTKSF SLDLTSGQAL VVQEDLTEYD LIQSQALSLA
LQGRDLFEAD EQEETGLLRL FFLGFIGGLL ALLTPCVFPM IPLTVSFFTK GAQNKAKGTI
NALLYGAFIF LIYFLLSLPF HLLDSVNPEI LNNISTNVTL NVIFFVIFIA FAISFFGYFE
LTLPQSWSAK MDDKANKIGG YIGIFFMALT LAIVSFSCTG PILGTLLGGS LTSDGGAMQL
TIGMSGFGLA LALPFALFAL FPNWLNSLPK SGGWLNTVKV VLGFIEVALA FKFLSNADLV
EHWGLLKREI FIAIWMVCAL GIALYLFGVI RFPHDGPKGQ KIPKGNWLVG LVSVALFVYL
TPGLTNTPAA NLKLLSGFPP PLFYSLYDKG TSAPLGLEAY KDFDQGMAAA RLAGKPVMVD
FTGWACVNCR KMEEQVWSEP EVFSLLSEDY ILISLYVDDR KPLDAAAQFN YAKSNGTVKA
IKTVGDKWAT FQTINFQNNS QPYYVLLDTE LNLLEKPVGY TPDAEAYAQW LNNGLMRYQA
LHP
//