ID A0A1Q3S741_9FLAO Unreviewed; 668 AA.
AC A0A1Q3S741;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Thiol:disulfide interchange protein {ECO:0000313|EMBL:OJV72214.1};
GN ORFNames=BGO42_03235 {ECO:0000313|EMBL:OJV72214.1};
OS Flavobacterium sp. 40-81.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1896169 {ECO:0000313|EMBL:OJV72214.1, ECO:0000313|Proteomes:UP000185767};
RN [1] {ECO:0000313|EMBL:OJV72214.1, ECO:0000313|Proteomes:UP000185767}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=40-81 {ECO:0000313|EMBL:OJV72214.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-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:OJV72214.1}.
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DR EMBL; MKTM01000012; OJV72214.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q3S741; -.
DR STRING; 1896169.BGO42_03235; -.
DR Proteomes; UP000185767; 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 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}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..668
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012140090"
FT TRANSMEM 198..223
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 244..266
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 278..299
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 320..342
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 354..378
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 390..408
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 428..449
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 461..481
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 22..146
FT /note="Thiol:disulfide interchange protein DsbD N-terminal"
FT /evidence="ECO:0000259|Pfam:PF11412"
FT DOMAIN 206..396
FT /note="Cytochrome C biogenesis protein transmembrane"
FT /evidence="ECO:0000259|Pfam:PF02683"
SQ SEQUENCE 668 AA; 73644 MW; 0C873EEBF5CDB5B9 CRC64;
MKKLTSLLLL FFTFLSTQAQ ILDPVKWKTS VEKKSDNEVV LVFEAAIDNE WHMYSQFTPE
GGALPTVFTY KDSKGNYEIV GKTKESEYKK VFNDVFEVDE YYFANKARFT QTIKVTNPNL
KSVKAAISYQ VCKEACIQQD KTFEFVLPAL KIAAYEATAG SVSDTLQTAA TVDTAAVKET
VAAVDTAKPI GKKEEQKGLF TIFIIAFFSG FAALLTPCVF PMIPMTVSFF TKQSKTKAQG
IKNAVIYGIS IILIYVLLGS LVTAIFGADA LNALSTNVWF NIIFFILLVV FASSFLGAFE
IMLPNSWANK VDRQADRGGI IGILFMALAL AIVSFSCTGP IVGTLLVEAA SKGGIAPIVG
MLGFSLALAL PFMLFAMFPG WLNSLPKSGG WLNTVKVVLG FLELALAFKF LSNADLVLQL
HLLEREVFLA IWIAIFGVLA LYLFGKITLP HDSPLSHISV GRLYMGLLVL MFTVYLIPGL
WGAPLKLISG FPPPMTYSES PYGVGNAKGG SSTASEKLPD GAKLGAHDIM AFTDYEKGMA
YAKSVNKPVL LDFTGFACVN CRKMEDFVWS KPEILAVLKE KVVLISLYVD DKRELPKNEQ
YVSKETGKEI VTVGNKWSDF QITHYKANAQ PYYIILDNQE NRLSEPVGYT PDAEEYKLWL
DTAIAKYK
//