CYDX_ECOLI
ID CYDX_ECOLI Reviewed; 37 AA.
AC P56100; Q2EER0; Q2MBJ7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Cytochrome bd-I ubiquinol oxidase subunit X;
DE EC=7.1.1.7;
DE AltName: Full=Cytochrome bd-I oxidase subunit X;
DE AltName: Full=Cytochrome d ubiquinol oxidase subunit X;
GN Name=cydX; Synonyms=ybgT; OrderedLocusNames=b4515, JW0724;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2843510; DOI=10.1016/s0021-9258(18)37682-8;
RA Green G.N., Fang H., Lin R.-J., Newton G., Mather M., Georgiou C.D.,
RA Gennis R.B.;
RT "The nucleotide sequence of the cyd locus encoding the two subunits of the
RT cytochrome d terminal oxidase complex of Escherichia coli.";
RL J. Biol. Chem. 263:13138-13143(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Kim K., Allen E., Araujo R., Aparicio A.M., Botstein D., Cherry M.,
RA Chung E., Dietrich F., Duncan M., Federspiel N., Kalman S., Komp C.,
RA Lashkari D., Lew H., Lin D., Namath A., Oefner P., Davis R.;
RL Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
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 IDENTIFICATION.
RX PubMed=7984428; DOI=10.1093/nar/22.22.4756;
RA Borodovsky M., Rudd K.E., Koonin E.V.;
RT "Intrinsic and extrinsic approaches for detecting genes in a bacterial
RT genome.";
RL Nucleic Acids Res. 22:4756-4767(1994).
RN [6]
RP IDENTIFICATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9068659; DOI=10.1128/jb.179.6.2077-2080.1997;
RA Muller M.M., Webster R.E.;
RT "Characterization of the tol-pal and cyd region of Escherichia coli K-12:
RT transcript analysis and identification of two new proteins encoded by the
RT cyd operon.";
RL J. Bacteriol. 179:2077-2080(1997).
RN [7]
RP SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=19121005; DOI=10.1111/j.1365-2958.2008.06495.x;
RA Hemm M.R., Paul B.J., Schneider T.D., Storz G., Rudd K.E.;
RT "Small membrane proteins found by comparative genomics and ribosome binding
RT site models.";
RL Mol. Microbiol. 70:1487-1501(2008).
RN [8]
RP INDUCTION BY STRESS.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=19734316; DOI=10.1128/jb.00872-09;
RA Hemm M.R., Paul B.J., Miranda-Rios J., Zhang A., Soltanzad N., Storz G.;
RT "Small stress response proteins in Escherichia coli: proteins missed by
RT classical proteomic studies.";
RL J. Bacteriol. 192:46-58(2010).
RN [9]
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=21778229; DOI=10.1074/jbc.m111.245696;
RA Fontaine F., Fuchs R.T., Storz G.;
RT "Membrane localization of small proteins in Escherichia coli.";
RL J. Biol. Chem. 286:32464-32474(2011).
RN [10]
RP PROBABLE INTERACTION WITH CYDA AND CYDB, SUBUNIT, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF MET-1; PHE-4; ILE-7; LEU-12; CYS-14 AND ALA-21.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=23749980; DOI=10.1128/jb.00324-13;
RA Vanorsdel C.E., Bhatt S., Allen R.J., Brenner E.P., Hobson J.J., Jamil A.,
RA Haynes B.M., Genson A.M., Hemm M.R.;
RT "The Escherichia coli CydX protein is a member of the CydAB cytochrome bd
RT oxidase complex and is required for cytochrome bd oxidase activity.";
RL J. Bacteriol. 195:3640-3650(2013).
CC -!- FUNCTION: Required for correct functioning of cytochrome bd-I oxidase.
CC This protein and AppX may have some functional overlap.
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 -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC -!- SUBUNIT: May be a subunit of cytochrome bd-I ubiquinol oxidase.
CC Probably interacts with CydA and CydB. {ECO:0000269|PubMed:23749980}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Single-pass
CC membrane protein {ECO:0000305}. Note=In sucrose cushions fractionates
CC with both the inner and outer membranes. {ECO:0000269|PubMed:19121005,
CC ECO:0000269|PubMed:21778229}.
CC -!- INDUCTION: Constitutively expressed during aerobic growth
CC (PubMed:19121005), induced in low oxygen, and maybe by SDS/EDTA
CC (envelope stress) (PubMed:19734316) (at protein level).
CC {ECO:0000269|PubMed:19121005, ECO:0000269|PubMed:19734316}.
CC -!- DISRUPTION PHENOTYPE: Slow growth in aerobic liquid culture, forms
CC mixed colonies on aerobic solid media, increased sensitivity to
CC reductant (beta-mercapoethanol). Reduced cytochrome bd-I oxidase
CC activity. {ECO:0000269|PubMed:23749980}.
CC -!- SIMILARITY: Belongs to the cytochrome ubiquinol oxidase subunit X
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=J03939; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; J03939; -; NOT_ANNOTATED_CDS; Unassigned_DNA.
DR EMBL; U30934; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U00096; ABD18645.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76359.1; -; Genomic_DNA.
DR RefSeq; WP_000270282.1; NZ_STEB01000035.1.
DR RefSeq; YP_588444.1; NC_000913.3.
DR PDB; 6RKO; EM; 2.68 A; X=1-37.
DR PDB; 6RX4; EM; 3.30 A; C=1-37.
DR PDBsum; 6RKO; -.
DR PDBsum; 6RX4; -.
DR AlphaFoldDB; P56100; -.
DR SMR; P56100; -.
DR BioGRID; 4259450; 12.
DR ComplexPortal; CPX-268; Cytochrome bd-I ubiquinol oxidase complex.
DR IntAct; P56100; 2.
DR MINT; P56100; -.
DR STRING; 511145.b4515; -.
DR TCDB; 3.D.4.3.2; the proton-translocating cytochrome oxidase (cox) superfamily.
DR PaxDb; P56100; -.
DR PRIDE; P56100; -.
DR EnsemblBacteria; ABD18645; ABD18645; b4515.
DR EnsemblBacteria; BAE76359; BAE76359; BAE76359.
DR GeneID; 1450246; -.
DR GeneID; 66670996; -.
DR KEGG; ecj:JW0724; -.
DR KEGG; eco:b4515; -.
DR PATRIC; fig|511145.12.peg.766; -.
DR EchoBASE; EB4075; -.
DR eggNOG; COG4890; Bacteria.
DR HOGENOM; CLU_207013_1_0_6; -.
DR PhylomeDB; P56100; -.
DR BioCyc; EcoCyc:MON0-2663; -.
DR BioCyc; MetaCyc:MON0-2663; -.
DR BRENDA; 7.1.1.7; 2026.
DR UniPathway; UPA00705; -.
DR PRO; PR:P56100; -.
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:0019867; C:outer membrane; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0016679; F:oxidoreductase activity, acting on diphenols and related substances as donors; IMP:EcoCyc.
DR GO; GO:0019646; P:aerobic electron transport chain; IC:ComplexPortal.
DR GO; GO:0006119; P:oxidative phosphorylation; IC:ComplexPortal.
DR InterPro; IPR011724; Cyd_oper_YbgT.
DR InterPro; IPR012994; YbgT_YccB.
DR Pfam; PF08173; YbgT_YccB; 1.
DR TIGRFAMs; TIGR02106; cyd_oper_ybgT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Electron transport;
KW Membrane; Reference proteome; Stress response; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..37
FT /note="Cytochrome bd-I ubiquinol oxidase subunit X"
FT /id="PRO_0000168701"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MUTAGEN 1
FT /note="M->Q: Does not restore reductant (beta-
FT mercapoethanol) resistance."
FT /evidence="ECO:0000269|PubMed:23749980"
FT MUTAGEN 4
FT /note="F->A: Does not restore reductant (beta-
FT mercapoethanol) resistance."
FT /evidence="ECO:0000269|PubMed:23749980"
FT MUTAGEN 7
FT /note="I->A: Does not restore reductant (beta-
FT mercapoethanol) resistance."
FT /evidence="ECO:0000269|PubMed:23749980"
FT MUTAGEN 12
FT /note="L->A: Does not restore reductant (beta-
FT mercapoethanol) resistance."
FT /evidence="ECO:0000269|PubMed:23749980"
FT MUTAGEN 14
FT /note="C->S: Restores reductant (beta-mercapoethanol)
FT resistance."
FT /evidence="ECO:0000269|PubMed:23749980"
FT MUTAGEN 21
FT /note="A->G: Does not restore reductant (beta-
FT mercapoethanol) resistance."
FT /evidence="ECO:0000269|PubMed:23749980"
FT HELIX 6..9
FT /evidence="ECO:0007829|PDB:6RKO"
FT HELIX 10..27
FT /evidence="ECO:0007829|PDB:6RKO"
SQ SEQUENCE 37 AA; 4042 MW; FCA4CC0A727F668B CRC64;
MWYFAWILGT LLACSFGVIT ALALEHVESG KAGQEDI
