APPB_ECOLI
ID APPB_ECOLI Reviewed; 378 AA.
AC P26458; P77278;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Cytochrome bd-II ubiquinol oxidase subunit 2;
DE EC=7.1.1.3 {ECO:0000305};
DE AltName: Full=Cytochrome bd-II oxidase subunit II;
GN Name=appB; Synonyms=cbdB, cyxB; OrderedLocusNames=b0979, JW0961;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=K12;
RX PubMed=1658595; DOI=10.1007/bf00267454;
RA Dassa J., Fsihi H., Marck C., Dion M., Kieffer-Bontemps M., Boquet P.L.;
RT "A new oxygen-regulated operon in Escherichia coli comprises the genes for
RT a putative third cytochrome oxidase and for pH 2.5 acid phosphatase
RT (appA).";
RL Mol. Gen. Genet. 229:341-352(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION AS AN OXIDASE, ACTIVITY REGULATION, AND SUBUNIT.
RX PubMed=8626304; DOI=10.1128/jb.178.6.1742-1749.1996;
RA Sturr M.G., Krulwich T.A., Hicks D.B.;
RT "Purification of a cytochrome bd terminal oxidase encoded by the
RT Escherichia coli app locus from a delta cyo delta cyd strain complemented
RT by genes from Bacillus firmus OF4.";
RL J. Bacteriol. 178:1742-1749(1996).
RN [6]
RP SUBCELLULAR LOCATION, AND TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [7]
RP FUNCTION AS AN OXIDASE, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=19542282; DOI=10.1128/jb.00562-09;
RA Bekker M., de Vries S., Ter Beek A., Hellingwerf K.J., de Mattos M.J.;
RT "Respiration of Escherichia coli can be fully uncoupled via the
RT nonelectrogenic terminal cytochrome bd-II oxidase.";
RL J. Bacteriol. 191:5510-5517(2009).
RN [8]
RP FUNCTION AS AN OXIDASE, FUNCTION IN PROTON TRANSLOCATION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=K12;
RX PubMed=21987791; DOI=10.1073/pnas.1108217108;
RA Borisov V.B., Murali R., Verkhovskaya M.L., Bloch D.A., Han H.,
RA Gennis R.B., Verkhovsky M.I.;
RT "Aerobic respiratory chain of Escherichia coli is not allowed to work in
RT fully uncoupled mode.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:17320-17324(2011).
RN [9]
RP FUNCTION AS AN OXIDASE, FUNCTION IN PROTON TRANSLOCATION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=K12;
RX PubMed=22843529; DOI=10.1128/aem.01507-12;
RA Sharma P., Hellingwerf K.J., de Mattos M.J., Bekker M.;
RT "Uncoupling of substrate-level phosphorylation in Escherichia coli during
RT glucose-limited growth.";
RL Appl. Environ. Microbiol. 78:6908-6913(2012).
RN [10]
RP REVIEW.
RX PubMed=21756872; DOI=10.1016/j.bbabio.2011.06.016;
RA Borisov V.B., Gennis R.B., Hemp J., Verkhovsky M.I.;
RT "The cytochrome bd respiratory oxygen reductases.";
RL Biochim. Biophys. Acta 1807:1398-1413(2011).
CC -!- FUNCTION: A terminal oxidase that catalyzes quinol-dependent, Na(+)-
CC independent oxygen uptake. Prefers menadiol over other quinols although
CC ubiquinol was not tested (PubMed:8626304). Generates a proton motive
CC force using protons and electrons from opposite sides of the membrane
CC to generate H(2)O, transferring 1 proton/electron.
CC {ECO:0000269|PubMed:19542282, ECO:0000269|PubMed:21987791,
CC ECO:0000269|PubMed:22843529, ECO:0000269|PubMed:8626304}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a ubiquinol + n H(+)(in) + O2 = 2 a ubiquinone + n H(+)(out)
CC + 2 H2O; Xref=Rhea:RHEA:30251, Rhea:RHEA-COMP:9565, Rhea:RHEA-
CC COMP:9566, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16389, ChEBI:CHEBI:17976; EC=7.1.1.3;
CC Evidence={ECO:0000305};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000305};
CC Note=May bind up to 3 heme groups per complex. {ECO:0000305};
CC -!- ACTIVITY REGULATION: Inhibited by cyanide; is more sensitive to cyanide
CC than cytochrome bd-I oxidase. {ECO:0000269|PubMed:8626304}.
CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC -!- SUBUNIT: Heterodimer of subunits I and II.
CC {ECO:0000305|PubMed:8626304}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15919996}.
CC -!- INDUCTION: Induced when bacterial cultures reach stationary phase;
CC synthesis is triggered by phosphate starvation or a shift from aerobic
CC to anaerobic conditions. {ECO:0000269|PubMed:1658595}.
CC -!- DISRUPTION PHENOTYPE: 3-fold decreased ubiquinone levels but no change
CC in redox levels of the ubiquinone pool (in aerobically grown minimal
CC medium with glucose). {ECO:0000269|PubMed:19542282,
CC ECO:0000269|PubMed:21987791, ECO:0000269|PubMed:22843529}.
CC -!- SIMILARITY: Belongs to the cytochrome ubiquinol oxidase subunit 2
CC family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought not to translocate protons.
CC {ECO:0000305|PubMed:19542282}.
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DR EMBL; S63811; AAB20285.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74064.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35744.1; -; Genomic_DNA.
DR RefSeq; NP_415498.1; NC_000913.3.
DR RefSeq; WP_000460803.1; NZ_SSZK01000002.1.
DR AlphaFoldDB; P26458; -.
DR SMR; P26458; -.
DR BioGRID; 4260034; 138.
DR ComplexPortal; CPX-269; Cytochrome bd-II ubiquinol oxidase complex.
DR IntAct; P26458; 1.
DR STRING; 511145.b0979; -.
DR PaxDb; P26458; -.
DR PRIDE; P26458; -.
DR EnsemblBacteria; AAC74064; AAC74064; b0979.
DR EnsemblBacteria; BAA35744; BAA35744; BAA35744.
DR GeneID; 66670745; -.
DR GeneID; 947547; -.
DR KEGG; ecj:JW0961; -.
DR KEGG; eco:b0979; -.
DR PATRIC; fig|511145.12.peg.1013; -.
DR EchoBASE; EB1353; -.
DR eggNOG; COG1294; Bacteria.
DR HOGENOM; CLU_049294_0_0_6; -.
DR InParanoid; P26458; -.
DR OMA; TAWAYWV; -.
DR PhylomeDB; P26458; -.
DR BioCyc; EcoCyc:APPB-MON; -.
DR BioCyc; MetaCyc:APPB-MON; -.
DR BRENDA; 7.1.1.3; 2026.
DR BRENDA; 7.1.1.7; 2026.
DR UniPathway; UPA00705; -.
DR PRO; PR:P26458; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0070069; C:cytochrome complex; IDA:ComplexPortal.
DR GO; GO:0005887; C:integral component of plasma membrane; ISM:EcoCyc.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0009486; F:cytochrome bo3 ubiquinol oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0009055; F:electron transfer activity; IDA:EcoCyc.
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; IDA:EcoCyc.
DR GO; GO:0019646; P:aerobic electron transport chain; IDA:EcoCyc.
DR GO; GO:0006119; P:oxidative phosphorylation; IDA:ComplexPortal.
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 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Electron transport; Heme; Iron;
KW Membrane; Metal-binding; Reference proteome; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..378
FT /note="Cytochrome bd-II ubiquinol oxidase subunit 2"
FT /id="PRO_0000183928"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..79
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..99
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 100..122
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 143..164
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 185..205
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..225
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 226..261
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..281
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 282..291
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..311
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 312..335
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 336..355
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 356..378
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CONFLICT 297
FT /note="M -> I (in Ref. 1; AAB20285)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 378 AA; 42424 MW; 8184B10C47660002 CRC64;
MFDYETLRFI WWLLIGVILV VFMISDGFDM GIGCLLPLVA RNDDERRIVI NSVGAHWEGN
QVWLILAGGA LFAAWPRVYA AAFSGFYVAM ILVLCSLFFR PLAFDYRGKI ADARWRKMWD
AGLVIGSLVP PVVFGIAFGN LLLGVPFAFT PQLRVEYLGS FWQLLTPFPL LCGLLSLGMV
ILQGGVWLQL KTVGVIHLRS QLATKRAALL VMLCFLLAGY WLWVGIDGFV LLAQDANGPS
NPLMKLVAVL PGAWMNNFVE SPVLWIFPLL GFFCPLLTVM AIYRGRPGWG FLMASLMQFG
VIFTAGITLF PFVMPSSVSP ISSLTLWDST SSQLTLSIML VIVLIFLPIV LLYTLWSYYK
MWGRMTTETL RRNENELY
