ID G8QUT7_SPHPG Unreviewed; 420 AA.
AC G8QUT7;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE SubName: Full=Putative ferric reductase {ECO:0000313|EMBL:AEV28113.1};
GN OrderedLocusNames=SpiGrapes_0250 {ECO:0000313|EMBL:AEV28113.1};
OS Sphaerochaeta pleomorpha (strain ATCC BAA-1885 / DSM 22778 / Grapes).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Sphaerochaetaceae;
OC Sphaerochaeta.
OX NCBI_TaxID=158190 {ECO:0000313|EMBL:AEV28113.1, ECO:0000313|Proteomes:UP000005632};
RN [1] {ECO:0000313|EMBL:AEV28113.1, ECO:0000313|Proteomes:UP000005632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1885 / DSM 22778 / Grapes
RC {ECO:0000313|Proteomes:UP000005632};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Munk A.C., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Ritalahtilisa K.,
RA Loeffler F., Woyke T.;
RT "Complete sequence of Spirochaeta sp. grapes.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP003155; AEV28113.1; -; Genomic_DNA.
DR AlphaFoldDB; G8QUT7; -.
DR STRING; 158190.SpiGrapes_0250; -.
DR KEGG; sgp:SpiGrapes_0250; -.
DR eggNOG; COG4097; Bacteria.
DR HOGENOM; CLU_653648_0_0_12; -.
DR OMA; CGEFHPF; -.
DR Proteomes; UP000005632; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR013112; FAD-bd_8.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR11972; NADPH OXIDASE; 1.
DR PANTHER; PTHR11972:SF153; NADPH OXIDASE 4; 1.
DR Pfam; PF08022; FAD_binding_8; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000005632};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 36..59
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 71..93
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 140..161
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 173..191
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 197..296
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 420 AA; 48027 MW; 9A17B4B675EEF9D1 CRC64;
MHYLLLAIIY LIIPVLHFVS FLFELPFFGI AEGVNYGIAI MAFYTIFNHL LITVKLPLFQ
SIFPYDKNIK LHAFSGIFVL TAVFYHAIFK ILVGKYINLI SWSLLFLTFL LLSLSALWID
TPMTRAFRKK VLKGKQLSYD LLKSIHAYLF PVMGIFLYLH ILDAGLLDTA NAFSSGYARI
FPIVVLLVVL FSKFRKYFLP LVTLTDNRQV GDISILTFTK PKHRKNTYKA GQFGYIQWCQ
KGIGKEEHPF SYLSCPSDES IMLGVKGSGD FTRKIATFTK GYQAKINGGF GNFIPNYAAR
QVVLIGSGIG IVPIISLIRQ MKANPLSQKV ICFLSVMTRE ELLLEKELFA LQDSNLELHC
LIFQEDKILY TAEFFKTYVK EPDLATYYIC SSPNVRNIVL RELEKLEVSA RQCHYEAFSY
//