ID Q7M860_WOLSU Unreviewed; 375 AA.
AC Q7M860;
DT 15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2003, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=CYTOCHROME BD OXIDASE SUBUNIT II EC 1.10.3 {ECO:0000313|EMBL:CAE10865.1};
DE EC=1.10.3.- {ECO:0000313|EMBL:CAE10865.1};
GN Name=CYDB {ECO:0000313|EMBL:CAE10865.1};
GN OrderedLocusNames=WS1852 {ECO:0000313|EMBL:CAE10865.1};
OS Wolinella succinogenes (strain ATCC 29543 / DSM 1740 / LMG 7466 / NCTC
OS 11488 / FDC 602W) (Vibrio succinogenes).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Wolinella.
OX NCBI_TaxID=273121 {ECO:0000313|Proteomes:UP000000422};
RN [1] {ECO:0000313|EMBL:CAE10865.1, ECO:0000313|Proteomes:UP000000422}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29543 / DSM 1740 / CCUG 13145 / JCM 31913 / LMG 7466 /
RC NCTC 11488 / FDC 602W {ECO:0000313|Proteomes:UP000000422};
RX PubMed=14500908; DOI=10.1073/pnas.1932838100;
RA Baar C., Eppinger M., Raddatz G., Simon JM., Lanz C., Klimmek O.,
RA Nandakumar R., Gross R., Rosinus A., Keller H., Jagtap P., Linke B.,
RA Meyer F., Lederer H., Schuster S.C.;
RT "Complete genome sequence and analysis of Wolinella succinogenes.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:11690-11695(2003).
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; BX571662; CAE10865.1; -; Genomic_DNA.
DR RefSeq; WP_011139648.1; NC_005090.1.
DR AlphaFoldDB; Q7M860; -.
DR STRING; 273121.WS1852; -.
DR KEGG; wsu:WS1852; -.
DR eggNOG; COG1294; Bacteria.
DR HOGENOM; CLU_733472_0_0_7; -.
DR Proteomes; UP000000422; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR003317; Cyt-d_oxidase_su2.
DR NCBIfam; TIGR00203; cydB; 1.
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 Oxidoreductase {ECO:0000313|EMBL:CAE10865.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000422};
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 87..104
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 125..150
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 170..194
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 215..234
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 254..274
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 286..312
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 332..355
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 375 AA; 42005 MW; BD6DDE97654AC1A6 CRC64;
MFESWSLEAL QVYWWVIVSL LGGLLVFMMF VQGGQTLLFF LSENELEKSV LINSLGRKWE
LTFTTLVLFG GACFAAFPLF YATSFGGAYW VWLLILFCFI IQAVSYEYRR KPDNFLGQKS
YEAFLYINGA LAPFLIGAAV STFFSGSPFA LSENFFPLWQ TPFRGLETLL VPYVYLLGLA
LFFLSRIGAS LYFINHVNEV SIRQKARKAV LRNTLYFLPF FLAFLGWILT KEGWSYDLSG
GVSVESYKYA KNLLALPWIG VMMIAGVGGV LLGIYQGALT ESSRGIFAFG AGVVLCVMGV
FLLAGLNGTP FYPSYTHPED SLTIKNASSS HYTLSVMAYV SLLVPLVLGY ITYVWRLMDK
KKITTHEVGG DSHLY
//
