ID A0A1L9NZF2_9RHOB Unreviewed; 671 AA.
AC A0A1L9NZF2;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Thiol:disulfide interchange protein DsbD {ECO:0000313|EMBL:OJI94647.1};
DE EC=1.8.1.8 {ECO:0000313|EMBL:OJI94647.1};
GN Name=dsbD_2 {ECO:0000313|EMBL:OJI94647.1};
GN ORFNames=PFRI_11960 {ECO:0000313|EMBL:OJI94647.1};
OS Planktotalea frisia.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Planktotalea.
OX NCBI_TaxID=696762 {ECO:0000313|EMBL:OJI94647.1, ECO:0000313|Proteomes:UP000184514};
RN [1] {ECO:0000313|EMBL:OJI94647.1, ECO:0000313|Proteomes:UP000184514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH6-1 {ECO:0000313|EMBL:OJI94647.1,
RC ECO:0000313|Proteomes:UP000184514};
RA Poehlein A., Bakenhus I., Voget S., Brinkhoff T., Simon M.;
RT "Genome sequence of Planktotalea frisia SH6-1.";
RL Submitted (OCT-2016) 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:OJI94647.1}.
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DR EMBL; MLCB01000091; OJI94647.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L9NZF2; -.
DR STRING; 696762.PFRI_11960; -.
DR OrthoDB; 9811036at2; -.
DR Proteomes; UP000184514; Unassembled WGS sequence.
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 CDD; cd02953; DsbDgamma; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR003834; Cyt_c_assmbl_TM_dom.
DR InterPro; IPR035671; DsbD_gamma.
DR InterPro; IPR028250; DsbDN.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
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.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
PE 4: Predicted;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000313|EMBL:OJI94647.1};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000184514};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 272..296
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 317..350
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 356..380
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 401..428
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 434..454
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 474..492
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 498..518
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 28..132
FT /note="Thiol:disulfide interchange protein DsbD N-terminal"
FT /evidence="ECO:0000259|Pfam:PF11412"
FT DOMAIN 279..473
FT /note="Cytochrome C biogenesis protein transmembrane"
FT /evidence="ECO:0000259|Pfam:PF02683"
SQ SEQUENCE 671 AA; 71452 MW; 01B7DE4483D39D27 CRC64;
MSVAASTDTY ENTAISARLI SVENGVATNS GTLSLGLDIK LAEGWKAYWR SPGEVGLPPE
ISWDGSTNLA TAQILWPAPE RFTAFGIENF GYNKRVVLPI QAVLETAGQA VELQAGVTLL
TCSTVCVPHD FNLALTIPAG AGIDAASAAL ISEFAERVPL GPDAADIEVE TAVIADGALY
VTARSANAFV NPDVFPEMGP TFTFGKPDIR TNSAGTELWA KLPLLASEEQ LPLLQVTVTD
GSRAVTAMPE WSNTVPDAPF ELVANLPDLA QILAIAAFAF LGGLILNVMP CVLPVLSIKL
TSVLNHGDKP SHEVRNGFLM SALGVLVFMW VLSAGILVLQ SVGITVGWGL QFQNPVFLTI
MFLVLTVFAA NLFGIFEISL PSGLQSRLAR SSVRDGYIGD FATGAFAAVL ATPCSAPFLG
TAVAFALSGR PIDVIIVFTA LGLGLSLPYL LFAWKPGMVR LLPKPGRWML VVKWVLAGLL
AGTAIWLLWV LMGVSGVRVA VSVLVLAVLF VLFATIRLPG RYTRTAALAA VAVLSLALPG
TLTPPPTIKE IGQDWVTFDR SEIPRLISQG QTVFVDVTAD WCLTCKANKT LVLDRVPVVD
RLRDEKVVAM QADWTRPNPD ISRYLEAHNR FGIPFNIVYG PNAPDGIILS EVLTSDAVLN
ALDAAALATD K
//
