CYDB_BACSU
ID CYDB_BACSU Reviewed; 338 AA.
AC P94365;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Cytochrome bd ubiquinol oxidase subunit 2;
DE EC=7.1.1.7 {ECO:0000250|UniProtKB:P0ABK2};
DE AltName: Full=Cytochrome d ubiquinol oxidase subunit II;
GN Name=cydB; Synonyms=yxkL; OrderedLocusNames=BSU38750;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / BGSC1A1;
RX PubMed=8969509; DOI=10.1099/13500872-142-11-3113;
RA Yoshida K., Shindo K., Sano H., Seki S., Fujimura M., Yanai N., Miwa Y.,
RA Fujita Y.;
RT "Sequencing of a 65 kb region of the Bacillus subtilis genome containing
RT the lic and cel loci, and creation of a 177 kb contig covering the gnt-
RT sacXY region.";
RL Microbiology 142:3113-3123(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a ubiquinol + 4 H(+)(in) + O2(in) = 2 a ubiquinone + 4
CC H(+)(out) + 2 H2O(in); Xref=Rhea:RHEA:40527, Rhea:RHEA-COMP:9565,
CC Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976; EC=7.1.1.7;
CC Evidence={ECO:0000250|UniProtKB:P0ABK2};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000250|UniProtKB:P0ABK2};
CC Note=Binds 1 protoheme IX center (heme b595) per heterodimer, in
CC conjunction with CydA. {ECO:0000250|UniProtKB:P0ABK2};
CC -!- COFACTOR:
CC Name=heme d cis-diol; Xref=ChEBI:CHEBI:62814;
CC Evidence={ECO:0000250|UniProtKB:P0ABK2};
CC Note=Binds 1 iron-chlorin (heme d or cytochrome d) per heterodimer, in
CC conjunction with CydA. {ECO:0000250|UniProtKB:P0ABK2};
CC -!- SUBUNIT: Heterodimer of subunits I and II.
CC {ECO:0000250|UniProtKB:P0ABK2}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cytochrome ubiquinol oxidase subunit 2
CC family. {ECO:0000305}.
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DR EMBL; D83026; BAA11728.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15901.1; -; Genomic_DNA.
DR PIR; B69611; B69611.
DR RefSeq; NP_391754.1; NC_000964.3.
DR RefSeq; WP_003244559.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; P94365; -.
DR SMR; P94365; -.
DR STRING; 224308.BSU38750; -.
DR PaxDb; P94365; -.
DR PRIDE; P94365; -.
DR EnsemblBacteria; CAB15901; CAB15901; BSU_38750.
DR GeneID; 937412; -.
DR KEGG; bsu:BSU38750; -.
DR PATRIC; fig|224308.179.peg.4194; -.
DR eggNOG; COG1294; Bacteria.
DR InParanoid; P94365; -.
DR OMA; FLWGVAF; -.
DR PhylomeDB; P94365; -.
DR BioCyc; BSUB:BSU38750-MON; -.
DR BioCyc; MetaCyc:BSU38750-MON; -.
DR BRENDA; 7.1.1.7; 658.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0070069; C:cytochrome complex; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009055; F:electron transfer activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016682; F:oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor; IBA:GO_Central.
DR GO; GO:0019646; P:aerobic electron transport chain; IBA:GO_Central.
DR InterPro; IPR003317; Cyt-d_oxidase_su2.
DR PANTHER; PTHR43141; PTHR43141; 1.
DR Pfam; PF02322; Cyt_bd_oxida_II; 1.
DR PIRSF; PIRSF000267; Cyt_oxidse_sub2; 1.
DR TIGRFAMs; TIGR00203; cydB; 2.
PE 3: Inferred from homology;
KW Cell membrane; Electron transport; Heme; Iron; Membrane; Metal-binding;
KW Oxidoreductase; Reference proteome; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..338
FT /note="Cytochrome bd ubiquinol oxidase subunit 2"
FT /id="PRO_0000183924"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 256..276
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 338 AA; 37861 MW; 13A57464E0F986BF CRC64;
MASLHDLWFI LVAVLFVGFF FLEGFDFGVG MATRFLGHNE LERRVLINTI GPFWDANEVW
LLTGAGAIFA AFPNWYATML SGYYIPFVIV LLALMGRGVA FEFRGKVDHL KWVKVWDWVV
FFGSLIPPFV LGVLFTTLFR GMPIDADMNI HAHVSDYINV YSILGGVTVT LLCFQHGLMF
ITLRTIGDLQ NRARKMAQKI MGVVFVAVLA FAALSAYQTD MFTRRGEITI PLAVLIVICF
MLAAVFIRKK KDGWTFGMTG AGLALTVGMI FISLFPRVMV SSLHSAYDLT VANASSGDYS
LKVMSIAALT LLPFVIGSQI WSYYVFRKRV SHKEPMTY
