ID A0A0U5J7Y7_9CLOT Unreviewed; 431 AA.
AC A0A0U5J7Y7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Thiol-disulfide oxidoreductase ResA {ECO:0000313|EMBL:CUX16830.1};
GN Name=resA {ECO:0000313|EMBL:CUX16830.1};
GN ORFNames=BN3456_00181 {ECO:0000313|EMBL:CUX16830.1};
OS Clostridium sp. C105KSO13.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1776045 {ECO:0000313|EMBL:CUX16830.1, ECO:0000313|Proteomes:UP000198973};
RN [1] {ECO:0000313|EMBL:CUX16830.1, ECO:0000313|Proteomes:UP000198973}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C105KSO131 {ECO:0000313|EMBL:CUX16830.1};
RA McClelland M., Jain A., Saraogi P., Mendelson R., Westerman R.,
RA SanMiguel P., Csonka L.;
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; FBWL01000117; CUX16830.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U5J7Y7; -.
DR STRING; 1776045.BN3456_00181; -.
DR OrthoDB; 9809733at2; -.
DR Proteomes; UP000198973; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0016209; F:antioxidant activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0017004; P:cytochrome complex assembly; IEA:InterPro.
DR CDD; cd02966; TlpA_like_family; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR003834; Cyt_c_assmbl_TM_dom.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR31272; CYTOCHROME C-TYPE BIOGENESIS PROTEIN HI_1454-RELATED; 1.
DR PANTHER; PTHR31272:SF4; CYTOCHROME C-TYPE BIOGENESIS PROTEIN HI_1454-RELATED; 1.
DR Pfam; PF00578; AhpC-TSA; 1.
DR Pfam; PF02683; DsbD; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000198973};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 58..87
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 93..116
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 137..158
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 178..200
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 212..231
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 281..427
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 250..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..283
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 431 AA; 47402 MW; 3BEDC0E6556171D9 CRC64;
MGFSLDVSVP VFTVFLQGLL SFFSPCVLPL IPLYISYLSG GTKIKGEDGK IHYDRKKVIL
NTLFFVIGIS FTFFVLGLGA SALGSVFKGN QVLFARIGGI VVIAFGLYQL GIFGTSKVLG
GEHRLPLKLD GLAMSPWTAL IMGVTFSFAW TPCVGPALSS VLVMTASANT KTLGFVLIGV
YTLGFVLPFL AVGVFSTTLL DLFQKHGNVV KYTVKAGGVL MILIGVMMFT GKMNAITGYL
SSIQTSREQE KIQEEKKSQK KDSIDRDSQE KDSQGKASEE GASQEDAIDF ELEDQYGEIH
KLSDYKGKTV FMNFWATWCP PCRAEMPDIQ KLYESYQREE DPDVIILGIA APGYGQEQNE
EGVKSFLQEN GYTYPVLMDI GGSLFEQYGI YSYPTTFMIN AEGNIFGYVS GQLTDDMMES
IIEQTMEGKK D
//
