ID A0A1F3H5P7_9BACT Unreviewed; 681 AA.
AC A0A1F3H5P7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Thiol:disulfide interchange protein {ECO:0000313|EMBL:OFX87129.1};
GN ORFNames=A2W86_08780 {ECO:0000313|EMBL:OFX87129.1};
OS Bacteroidetes bacterium GWD2_45_23.
OC Bacteria; Bacteroidota.
OX NCBI_TaxID=1797330 {ECO:0000313|EMBL:OFX87129.1, ECO:0000313|Proteomes:UP000178053};
RN [1] {ECO:0000313|EMBL:OFX87129.1, ECO:0000313|Proteomes:UP000178053}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OFX87129.1}.
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DR EMBL; MENT01000003; OFX87129.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F3H5P7; -.
DR Proteomes; UP000178053; 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..681
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009489834"
FT TRANSMEM 229..254
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 275..297
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 309..330
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 351..375
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 387..411
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 431..454
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 460..477
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 497..516
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 34..141
FT /note="Thiol:disulfide interchange protein DsbD N-terminal"
FT /evidence="ECO:0000259|Pfam:PF11412"
FT DOMAIN 237..418
FT /note="Cytochrome C biogenesis protein transmembrane"
FT /evidence="ECO:0000259|Pfam:PF02683"
SQ SEQUENCE 681 AA; 74480 MW; 137E8405D661C55A CRC64;
MKRSTALLGL LFLCISMAFS QDEMRWDFSL KDVGNGEIEL VADVQIKQGW YLYDTKIPDG
GPTPTQISFD RIVGAEPIGE FHADTKAKVK YDGIFQMTIG TFQNNARFIQ RLKVTDKAGF
TLQGDVRAQA CDDSSCTPPL PNDFSFTAEH LPATVTVTAT AASTPATATT SETSLSFTPL
TPAQPADSLG TASSVAVTSA GIDSDLLWTP VIEELQDYGM KGSTAGMSLF WIFISGFIGG
LIALITPCVW PMIPMTVSFF LKRNKTEKKK AVTEAMVYGI AIIVIYVVLG LLITGIFGAS
ALNNLATSAL FNLIFFALLV LFAVAFFGGF EMVLPAKWTN KMDERADKTS GALSIFFMAF
TLVLVSFSCT GPIIGTLLVE AAMSGSILGP AIGMLGFAIA LAVPFVLFAI FPSWLSNLPK
SGGWLNSVKV VLGFLELALA LKFLSVADLA YGWGILDREV FLVLWIVIFA LLGIYLLGKI
KFPGDSDLPH VTIPRLFLSI ISLAFAVYMI PGLWGAPLKA ISAFSPPLYT QDFNLYDGEV
HAQTMDYEAG IALAKQQNKP VLIDFSGYGC VNCRKMEASV WTDPRVKDIL ENEYILITLM
VDDKAKLPEI IEVEENGRTT RLKTIGDKWS YLQRHKFGAN AQPYYIALDH DGKPLSPSYA
YDENVERYIE FLQTGLTNFK K
//
