ID A0A0S7BXB3_9BACT Unreviewed; 385 AA.
AC A0A0S7BXB3;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Cytochrome bd-type quinol oxidase, subunit 2 {ECO:0000313|EMBL:GAP42834.1};
GN ORFNames=TBC1_11974 {ECO:0000313|EMBL:GAP42834.1};
OS Lentimicrobium saccharophilum.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Lentimicrobiaceae;
OC Lentimicrobium.
OX NCBI_TaxID=1678841 {ECO:0000313|EMBL:GAP42834.1};
RN [1] {ECO:0000313|EMBL:GAP42834.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TBC1 {ECO:0000313|EMBL:GAP42834.1};
RA Tourlousse D.M., Matsuura N., Sun L., Toyonaga M., Kuroda K., Ohashi A.,
RA Cruz R., Yamaguchi T., Sekiguchi Y.;
RT "Draft Genome Sequence of Bacteroidales Strain TBC1, a Novel Isolate from a
RT Methanogenic Wastewater Treatment System.";
RL Genome Announc. 3:e01168-15(2015).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the cytochrome ubiquinol oxidase subunit 2
CC family. {ECO:0000256|ARBA:ARBA00007543}.
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DR EMBL; DF968182; GAP42834.1; -; Genomic_DNA.
DR RefSeq; WP_062039261.1; NZ_DF968182.1.
DR AlphaFoldDB; A0A0S7BXB3; -.
DR STRING; 1678841.TBC1_11974; -.
DR PATRIC; fig|1678841.3.peg.1098; -.
DR OrthoDB; 9776710at2; -.
DR Proteomes; UP000053091; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR003317; Cyt-d_oxidase_su2.
DR PANTHER; PTHR43141:SF5; CYTOCHROME BD-I UBIQUINOL OXIDASE SUBUNIT 2; 1.
DR PANTHER; PTHR43141; CYTOCHROME BD2 SUBUNIT II; 1.
DR Pfam; PF02322; Cyt_bd_oxida_II; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000053091};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 12..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 87..104
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 125..144
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 183..206
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 258..283
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 295..315
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 345..364
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 385 AA; 43590 MW; 3E2DB86CC1D48F66 CRC64;
MFETFELLTL QQYWWIIISL LASLLVFLMF VQGGQTLIYT LGKTDTERSM IVNTLGRKWE
LTFTTLVTFG GAFFASFPLF YSTSFGGAYW VWMAILFAFI IQAISYEYRS KPNNFLGKRT
FETFLFINGA LGTILIGTAV GTFFNGAMFS VDKLNLTNIY DSAISRWETP FHGLEAVLNF
HNVALGLSVF FLARVLGILY IVNSVSDENI HGRARKQMLY NALPFLVFFL YFVIHLLLKQ
GFAVNPDTGE VFMEKFKYFH NLIQMPVVLV LFLAGVVGVL AGIGRFLFCR SNRGIWFTGA
GTVLAVFALF LIAGLNNTAF YPSLHNLQHS LTIRNSSSSH YTLTAMSYVS LFVPVVITYI
FFAWKSINNK PIEKAELDEE GTHIY
//
