ID A0A2S2DSI4_9BACT Unreviewed; 657 AA.
AC A0A2S2DSI4;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Protein-disulfide reductase {ECO:0000313|EMBL:AWL08262.1};
DE EC=1.8.1.8 {ECO:0000313|EMBL:AWL08262.1};
GN Name=dsbD {ECO:0000313|EMBL:AWL08262.1};
GN ORFNames=HME7025_00389 {ECO:0000313|EMBL:AWL08262.1};
OS Aquirufa nivalisilvae.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae; Aquirufa.
OX NCBI_TaxID=2516557 {ECO:0000313|EMBL:AWL08262.1, ECO:0000313|Proteomes:UP000245468};
RN [1] {ECO:0000313|Proteomes:UP000245468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HME7025 {ECO:0000313|Proteomes:UP000245468};
RA Kim H., Kang H., Joh K.;
RT "Pseudarcicella sp. HME7025 Genome sequencing and assembly.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP029346; AWL08262.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S2DSI4; -.
DR KEGG; psez:HME7025_00389; -.
DR OrthoDB; 9811036at2; -.
DR Proteomes; UP000245468; Chromosome.
DR GO; GO:0016020; C: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 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 Oxidoreductase {ECO:0000313|EMBL:AWL08262.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000245468};
KW Signal {ECO:0000256|SAM:SignalP}; 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..657
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015547463"
FT TRANSMEM 188..209
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 229..251
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 263..284
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 305..331
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 343..363
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 383..406
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 412..429
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 449..470
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 39..148
FT /note="Thiol:disulfide interchange protein DsbD N-terminal"
FT /evidence="ECO:0000259|Pfam:PF11412"
FT DOMAIN 196..389
FT /note="Cytochrome C biogenesis protein transmembrane"
FT /evidence="ECO:0000259|Pfam:PF02683"
SQ SEQUENCE 657 AA; 72557 MW; 9E007F4C94ADA560 CRC64;
MKYKLLILSL FLFVLSPVLA QKLTPAKWSW TLEPAKPSVG QEAEIVFQVK IEKGWYLYSS
DFDKDLGPVV TTVTIKNPVG FELVGGLKAI NPHSKFDKEI WNGTYTYFTE KGEFRQKIKI
TAENWKIEGN YDSQTCSNES GLCVPIKGPF VIASSATASD VLTDEAKKKI PESVVTASAS
PVAPNESLWQ FFWIAMGAGL LALLTPCVYP LIPMTVSFFT KQKGGKGLAF LYGSFIVLIY
VFFGTLLAFF AGASFANFLS THWIPNLLFF VIFIFFGISF LGAFEIVLPS GMVNSVDAKS
DKGGIIGVFF MAFTLVLVSF SCTGPLAGSI LIAASQGAFV KPIIGMLGFS LAFAIPFTLF
AIFPGFMQKL PKSGNWMNEV KVVLGFLEIA LAFKFLSVAD QVYHWHLLDR EIFLAIWIAI
FSALTLYLFG KISLPHDGPA GKLSIPRTLF ATAILAFVVY LIPGMFGAPL KGLSGWLPPM
SSQDFKGNSG EVSIKPGSTG VVKYGDFLEL PLGLTGFFDY QEAKAYAVQV GKPLFIDFTG
HGCVNCRKME EYVWSDPKVL KRLQEEYVIV ALYCDDKTEL PADQWYVSKV DGQEKKTLGD
QNLDFQISRF NSNAQPHYVL LDPRKEGAPM VTPVAFDANV DHFVAFLDKG VRQYKLN
//
