ID A0A1B1Q4B7_9CHLB Unreviewed; 700 AA.
AC A0A1B1Q4B7;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Thiol:disulfide interchange protein DsbD {ECO:0000313|EMBL:ANT65665.1};
DE EC=1.8.1.8 {ECO:0000313|EMBL:ANT65665.1};
GN Name=dsbD_2 {ECO:0000313|EMBL:ANT65665.1};
GN ORFNames=Ptc2401_01934 {ECO:0000313|EMBL:ANT65665.1};
OS Prosthecochloris sp. CIB 2401.
OC Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC Prosthecochloris.
OX NCBI_TaxID=1868325 {ECO:0000313|EMBL:ANT65665.1, ECO:0000313|Proteomes:UP000092496};
RN [1] {ECO:0000313|EMBL:ANT65665.1, ECO:0000313|Proteomes:UP000092496}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIB 2401 {ECO:0000313|EMBL:ANT65665.1,
RC ECO:0000313|Proteomes:UP000092496};
RA Nabhan S., Bunk B., Sproeer C., Bryant D.A., Overmann J.;
RT "Genome Sequence of Prosthecochloris phaeum CIB2401 of the phylum
RT Chlorobi.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP016432; ANT65665.1; -; Genomic_DNA.
DR RefSeq; WP_068867816.1; NZ_CP016432.1.
DR AlphaFoldDB; A0A1B1Q4B7; -.
DR STRING; 1868325.Ptc2401_01934; -.
DR KEGG; proc:Ptc2401_01934; -.
DR PATRIC; fig|1868325.3.peg.1901; -.
DR InParanoid; A0A1B1Q4B7; -.
DR OrthoDB; 9811036at2; -.
DR Proteomes; UP000092496; 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 CDD; cd02953; DsbDgamma; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR035671; DsbD_gamma.
DR InterPro; IPR028250; DsbDN.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR32234:SF3; SUPPRESSION OF COPPER SENSITIVITY PROTEIN; 1.
DR PANTHER; PTHR32234; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBD; 1.
DR Pfam; PF11412; DsbD_N; 1.
DR Pfam; PF13899; Thioredoxin_7; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 4: Predicted;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000313|EMBL:ANT65665.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000092496};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 275..302
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 322..343
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 363..382
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 402..425
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 437..459
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 480..499
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 505..524
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 536..553
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 558..691
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 700 AA; 75298 MW; E6C201319BF90049 CRC64;
MKNITIVVVL FLQLLFPFRQ SAQAFLLQPD EPPVQAELFS VAHEPGGRLL VGLRMQMLPG
WHVYWKYPGE VGLPVSISWS LPDGYRAGDL MFPHPERFEF EGMTGYGYSG EVVLFSTIEP
EAGDVLSSGI FPLTTEIEWL ACGEFCMPGS VRLELLSPEP DLQFASLARK WIDRLPKKHG
EYDQLLQLSS SREKGGVTVV KLEYMGAGEL RDFYPYAPPE GISCVDVSVD GKLIELSLEG
DVAGVVLGGV AVSTKGVFDV ATPALGVGQG GMPGILTLVL MLCFAFGGGV LLNVMPCVLP
VLGLKVFSLV GPHGEESATG RYLSLFFAAG VLFSFWVMAG FVWVLQGMGE QIGWGFQFQS
PAFIMFIAGL VFAFGLNLFG IFEFSAPVVS GKVGKLASNK DIAGSFVSGV LATTLATPCT
APFLGTALGF AFTQPPLLIL VFFTVIALGM AAPYVLLAWH PAWLKFLPRP GQWMFIFKQV
MGFVLFAVVI WLASILGSHG GADGILALLL LLFCISIIVW GAAAVAGPGS SGRKRLGVWS
LAIVLMLSAW QFFSAGAVQQ AGREPAGGAY EDANGVTWHD FSPGLLAAYR ENRQTVLIDF
TADWCLTCKA LEAGVLGNPR VAETLARLGI EAVRADWTTR NDDITALLQR FGRSGVPLLV
VIPKGDLEHA EVLPEVVSVG MLLEALERAV PAASELDHHM
//
