APPC_ECOLI
ID APPC_ECOLI Reviewed; 514 AA.
AC P26459;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Cytochrome bd-II ubiquinol oxidase subunit 1;
DE EC=7.1.1.3 {ECO:0000305};
DE AltName: Full=Cytochrome bd-II oxidase subunit I;
GN Name=appC; Synonyms=cbdA, cyxA; OrderedLocusNames=b0978, JW0960;
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, SUBUNIT, AND PROTEIN SEQUENCE
RP OF 496-510.
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.
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 -!- PTM: The N-terminus is blocked.
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 1
CC family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought not to translocate protons.
CC {ECO:0000305|PubMed:19542282}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; S63811; AAB20284.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74063.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35743.1; -; Genomic_DNA.
DR PIR; S17958; S17958.
DR RefSeq; NP_415497.1; NC_000913.3.
DR RefSeq; WP_000263582.1; NZ_LN832404.1.
DR PDB; 7OSE; EM; 3.00 A; A/D=1-514.
DR PDB; 7OY2; EM; 2.06 A; C=1-514.
DR PDBsum; 7OSE; -.
DR PDBsum; 7OY2; -.
DR AlphaFoldDB; P26459; -.
DR SMR; P26459; -.
DR BioGRID; 4260039; 243.
DR ComplexPortal; CPX-269; Cytochrome bd-II ubiquinol oxidase complex.
DR DIP; DIP-9119N; -.
DR IntAct; P26459; 2.
DR STRING; 511145.b0978; -.
DR jPOST; P26459; -.
DR PaxDb; P26459; -.
DR PRIDE; P26459; -.
DR EnsemblBacteria; AAC74063; AAC74063; b0978.
DR EnsemblBacteria; BAA35743; BAA35743; BAA35743.
DR GeneID; 945585; -.
DR KEGG; ecj:JW0960; -.
DR KEGG; eco:b0978; -.
DR PATRIC; fig|511145.12.peg.1012; -.
DR EchoBASE; EB1354; -.
DR eggNOG; COG1271; Bacteria.
DR HOGENOM; CLU_030555_3_1_6; -.
DR InParanoid; P26459; -.
DR OMA; MAIAFWS; -.
DR PhylomeDB; P26459; -.
DR BioCyc; EcoCyc:APPC-MON; -.
DR BioCyc; MetaCyc:APPC-MON; -.
DR BRENDA; 7.1.1.3; 2026.
DR UniPathway; UPA00705; -.
DR PRO; PR:P26459; -.
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:0020037; F:heme binding; 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; IPR002585; Cyt-d_ubiquinol_oxidase_su_1.
DR PANTHER; PTHR30365; PTHR30365; 1.
DR Pfam; PF01654; Cyt_bd_oxida_I; 1.
DR PIRSF; PIRSF006446; Cyt_quinol_oxidase_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane;
KW Direct protein sequencing; Electron transport; Heme; Iron; Membrane;
KW Metal-binding; Reference proteome; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..514
FT /note="Cytochrome bd-II ubiquinol oxidase subunit 1"
FT /id="PRO_0000183922"
FT TOPO_DOM 1..22
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 23..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..94
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 115..129
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 130..149
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 150..187
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 208..219
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 240..392
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 393..412
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 413..470
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 471..490
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 491..514
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT BINDING 19
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255"
FT BINDING 186
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255"
FT BINDING 393
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255"
FT HELIX 4..43
FT /evidence="ECO:0007829|PDB:7OY2"
FT HELIX 46..80
FT /evidence="ECO:0007829|PDB:7OY2"
FT HELIX 82..116
FT /evidence="ECO:0007829|PDB:7OY2"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:7OY2"
FT HELIX 123..152
FT /evidence="ECO:0007829|PDB:7OY2"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:7OY2"
FT TURN 161..164
FT /evidence="ECO:0007829|PDB:7OY2"
FT STRAND 165..169
FT /evidence="ECO:0007829|PDB:7OY2"
FT HELIX 171..175
FT /evidence="ECO:0007829|PDB:7OY2"
FT HELIX 178..208
FT /evidence="ECO:0007829|PDB:7OY2"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:7OSE"
FT HELIX 213..248
FT /evidence="ECO:0007829|PDB:7OY2"
FT HELIX 250..256
FT /evidence="ECO:0007829|PDB:7OY2"
FT STRAND 269..272
FT /evidence="ECO:0007829|PDB:7OSE"
FT TURN 277..280
FT /evidence="ECO:0007829|PDB:7OSE"
FT STRAND 286..288
FT /evidence="ECO:0007829|PDB:7OSE"
FT HELIX 292..297
FT /evidence="ECO:0007829|PDB:7OSE"
FT STRAND 298..301
FT /evidence="ECO:0007829|PDB:7OSE"
FT HELIX 310..332
FT /evidence="ECO:0007829|PDB:7OY2"
FT HELIX 338..347
FT /evidence="ECO:0007829|PDB:7OY2"
FT HELIX 348..350
FT /evidence="ECO:0007829|PDB:7OY2"
FT HELIX 351..360
FT /evidence="ECO:0007829|PDB:7OY2"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:7OY2"
FT HELIX 369..378
FT /evidence="ECO:0007829|PDB:7OY2"
FT HELIX 383..413
FT /evidence="ECO:0007829|PDB:7OY2"
FT TURN 416..418
FT /evidence="ECO:0007829|PDB:7OY2"
FT HELIX 420..428
FT /evidence="ECO:0007829|PDB:7OY2"
FT TURN 429..431
FT /evidence="ECO:0007829|PDB:7OY2"
FT HELIX 432..446
FT /evidence="ECO:0007829|PDB:7OY2"
FT TURN 447..450
FT /evidence="ECO:0007829|PDB:7OY2"
FT STRAND 451..453
FT /evidence="ECO:0007829|PDB:7OY2"
FT TURN 454..456
FT /evidence="ECO:0007829|PDB:7OY2"
FT HELIX 459..462
FT /evidence="ECO:0007829|PDB:7OY2"
FT HELIX 468..499
FT /evidence="ECO:0007829|PDB:7OY2"
FT HELIX 501..503
FT /evidence="ECO:0007829|PDB:7OY2"
SQ SEQUENCE 514 AA; 57920 MW; 2D2FBD43429D960D CRC64;
MWDVIDLSRW QFALTALYHF LFVPLTLGLI FLLAIMETIY VVTGKTIYRD MTRFWGKLFG
INFALGVATG LTMEFQFGTN WSFYSNYVGD IFGAPLAMEA LMAFFLESTF VGLFFFGWQR
LNKYQHLLVT WLVAFGSNLS ALWILNANGW MQYPTGAHFD IDTLRMEMTS FSELVFNPVS
QVKFVHTVMA GYVTGAMFIM AISAWYLLRG RERNVALRSF AIGSVFGTLA IIGTLQLGDS
SAYEVAQVQP VKLAAMEGEW QTEPAPAPFH VVAWPEQDQE RNAFALKIPA LLGILATHSL
DKPVPGLKNL MAETYPRLQR GRMAWLLMQE ISQGNREPHV LQAFRGLEGD LGYGMLLSRY
APDMNHVTAA QYQAAMRGAI PQVAPVFWSF RIMVGCGSLL LLVMLIALVQ TLRGKIDQHR
WVLKMALWSL PLPWIAIEAG WFMTEFGRQP WAIQDILPTY SAHSALTTGQ LAFSLIMIVG
LYTLFLIAEV YLMQKYARLG PSAMQSEQPT QQQG
