CYDB_ECOL6
ID CYDB_ECOL6 Reviewed; 379 AA.
AC P0ABK3; P11027;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Cytochrome bd-I ubiquinol oxidase subunit 2;
DE EC=7.1.1.7 {ECO:0000250|UniProtKB:P0ABK2};
DE AltName: Full=Cytochrome bd-I oxidase subunit II;
DE AltName: Full=Cytochrome d ubiquinol oxidase subunit II;
GN Name=cydB; OrderedLocusNames=c0812;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC -!- FUNCTION: A terminal oxidase that produces a proton motive force by the
CC vectorial transfer of protons across the inner membrane. It is the
CC component of the aerobic respiratory chain of E.coli that predominates
CC when cells are grown at low aeration. Generates a proton motive force
CC using protons and electrons from opposite sides of the membrane to
CC generate H(2)O, transferring 1 proton/electron.
CC {ECO:0000250|UniProtKB:P0ABK2}.
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 -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC -!- SUBUNIT: Heterodimer of subunits I and II.
CC {ECO:0000250|UniProtKB:P0ABK2}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:P0ABK2}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P0ABK2}.
CC -!- SIMILARITY: Belongs to the cytochrome ubiquinol oxidase subunit 2
CC family. {ECO:0000305}.
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DR EMBL; AE014075; AAN79285.1; -; Genomic_DNA.
DR RefSeq; WP_000568275.1; NC_004431.1.
DR AlphaFoldDB; P0ABK3; -.
DR SMR; P0ABK3; -.
DR STRING; 199310.c0812; -.
DR EnsemblBacteria; AAN79285; AAN79285; c0812.
DR GeneID; 66670997; -.
DR KEGG; ecc:c0812; -.
DR eggNOG; COG1294; Bacteria.
DR HOGENOM; CLU_049294_0_0_6; -.
DR OMA; FLWGVAF; -.
DR BioCyc; ECOL199310:C0812-MON; -.
DR UniPathway; UPA00705; -.
DR Proteomes; UP000001410; Chromosome.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway.
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; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Electron transport; Formylation; Heme;
KW Iron; Membrane; Metal-binding; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..379
FT /note="Cytochrome bd-I ubiquinol oxidase subunit 2"
FT /id="PRO_0000183927"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 9..28
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 29..79
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 80..99
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 100..122
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 123..142
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 143..164
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 165..184
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 185..205
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 206..225
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 226..262
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 263..282
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 283..292
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 293..312
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 313..336
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 337..356
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 357..379
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT MOD_RES 1
FT /note="N-formylmethionine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 379 AA; 42453 MW; A3775AC95F713D0C CRC64;
MIDYEVLRFI WWLLVGVLLI GFAVTDGFDM GVGMLTRFLG RNDTERRIMI NSIAPHWDGN
QVWLITAGGA LFAAWPMVYA AAFSGFYVAM ILVLASLFFR PVGFDYRSKI EETRWRNMWD
WGIFIGSFVP PLVIGVAFGN LLQGVPFNVD EYLRLYYTGN FFQLLNPFGL LAGVVSVGMI
ITQGATYLQM RTVGELHLRT RATAQVAALV TLVCFALAGV WVMYGIDGYV VKSTMDHYAA
SNPLNKEVVR EAGAWLVNFN NTPILWAIPA LGVVLPLLTI LTARMDKAAW AFVFSSLTLA
CIILTAGIAM FPFVMPSSTM MNASLTMWDA TSSQLTLNVM TWVAVVLVPI ILLYTAWCYW
KMFGRITKED IERNTHSLY
