ID A0A099XR19_9FLAO Unreviewed; 811 AA.
AC A0A099XR19;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Protein-disulfide reductase {ECO:0000313|EMBL:KGL58840.1};
DE EC=1.8.1.8 {ECO:0000313|EMBL:KGL58840.1};
GN ORFNames=PHEL85_3111 {ECO:0000313|EMBL:KGL58840.1};
OS Polaribacter sp. Hel1_85.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=1250005 {ECO:0000313|EMBL:KGL58840.1, ECO:0000313|Proteomes:UP000029991};
RN [1] {ECO:0000313|EMBL:KGL58840.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hel1_85 {ECO:0000313|EMBL:KGL58840.1};
RA Xing P., Hahnke R.L., Unfried F., Markert S., Huang S., Barbeyron T.,
RA Harder J., Becher D., Schweder T., Gloenk F.O., Amann R.I., Teeling H.;
RT "Niches of two polysaccharide-degrading Polaribacter strains isolated from
RT the North Sea during a spring diatom bloom.";
RL ISME J. 0:0-0(2014).
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:KGL58840.1}.
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DR EMBL; JPDS01000003; KGL58840.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A099XR19; -.
DR STRING; 1250005.PHEL85_3111; -.
DR eggNOG; COG4232; Bacteria.
DR OrthoDB; 9811036at2; -.
DR Proteomes; UP000029991; 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 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; IPR012336; Thioredoxin-like_fold.
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; 2.
DR Pfam; PF13098; Thioredoxin_2; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000313|EMBL:KGL58840.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 341..366
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 387..408
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 423..444
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 465..488
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 500..525
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 537..555
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 575..594
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 606..629
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 34..140
FT /note="Thiol:disulfide interchange protein DsbD N-terminal"
FT /evidence="ECO:0000259|Pfam:PF11412"
FT DOMAIN 177..285
FT /note="Thiol:disulfide interchange protein DsbD N-terminal"
FT /evidence="ECO:0000259|Pfam:PF11412"
FT DOMAIN 349..530
FT /note="Cytochrome C biogenesis protein transmembrane"
FT /evidence="ECO:0000259|Pfam:PF02683"
FT DOMAIN 678..794
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13098"
SQ SEQUENCE 811 AA; 90850 MW; 05CCB86612B6778E CRC64;
MKNIFIFLFI TFSLGVFSQI EDPIEWSTSV EKISDSEFVL VSTATIEEGW HLYSQNVPED
GPVPTTFTFD DSEQNFSLIE KTIEEKGHTI DDTVFQMKIK FFENKAVFRQ EVKVLSDINT
INGVVEFMVC DDSKCLAPTE IDLKFNIPNE SENPFNSDEG LLNPVKWKTS IEKISKVEYD
LVITAEIDAD WHLYSQHTAD GGALPIEITK SNEKDAYDLV GKAVESDTIK KFNEIFDVQE
TYFDNKAILK QRIKLKNQDI SKVTLNLTGQ VCRKVCIQID EDFTFLLNGK NENSIITSVD
NTSVNNLLYG MNTDGLSFSS DTCKDEIKSN SSEIQSGGKS LWNIFGLGFL GGLLALLTPC
VFPMIPLTVS FFTKKSGQNK GAGISKALLY GFFIFAVYIL LSVPFHLLDS VNPDILNEIS
TNIWLNIIFF IIFVFFAFSF FGYYELTLPA SWTNKTTQGE NSGGFIGIFF MALTLAIVSF
SCTGPILGSL LAGSLTADGG AWQLTAGMAG FGVSLGLPFA LFAMFPNMMN ALPKSGGWLN
TTKVILGFLE LALAFKFLSN ADLVAHWNLL KIEPFLLLWI LIFAGLALYL LGKIKFPHDS
PIKKLSFSRI AGGILVASFV VYLASGFMVN KETKTFTPLT LLSGLAPPVG YSFLYPNDCP
NNLDCFKDLK KGIEYANKVN KPIMLDFTGY ACVNCRKMEE HVWPNKKIDN YLRNDYVLIS
LYVDDKKELP KEEQILVNRI NGGTRKLETY GNKWANYQTQ FFKTNSQPYY VLLNSDGTKI
LNQAVGYTPD ENDYAKFLEC GLEVFKNNNK E
//
