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CYDX_BRUA2
ID   CYDX_BRUA2              Reviewed;          51 AA.
AC   Q2YKD6;
DT   13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2013, sequence version 2.
DT   25-MAY-2022, entry version 66.
DE   RecName: Full=Cytochrome bd ubiquinol oxidase subunit X;
DE            EC=7.1.1.7;
GN   Name=cydX; Synonyms=ybgT; OrderedLocusNames=BAB2_0726;
OS   Brucella abortus (strain 2308).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=359391;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2308;
RX   PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005;
RA   Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
RA   Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT   "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL   Infect. Immun. 73:8353-8361(2005).
RN   [2]
RP   FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, INDUCTION, OPERON STRUCTURE, AND
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=2308;
RX   PubMed=22919638; DOI=10.3389/fcimb.2012.00047;
RA   Sun Y.H., de Jong M.F., den Hartigh A.B., Roux C.M., Rolan H.G.,
RA   Tsolis R.M.;
RT   "The small protein CydX is required for function of cytochrome bd oxidase
RT   in Brucella abortus.";
RL   Front. Cell. Infect. Microbiol. 2:47-47(2012).
CC   -!- FUNCTION: Required for correct functioning of cytochrome bd oxidase.
CC       {ECO:0000269|PubMed:22919638}.
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 ubiquinol oxidase.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000305|PubMed:22919638}; Single-pass membrane protein
CC       {ECO:0000305|PubMed:22919638}.
CC   -!- INDUCTION: Expressed in stationary phase. Part of the cydB-cydX operon.
CC       {ECO:0000269|PubMed:22919638}.
CC   -!- DISRUPTION PHENOTYPE: Highly attenuated in macrophage-like line J774
CC       and female BALB/c ByJ mouse infections. Loss of viability in stationary
CC       phase growth in culture. Increased sensitivity to H(2)O(2), acid pH,
CC       highly sensitive to the combination of NaN(3) plus NiSO(4).
CC       {ECO:0000269|PubMed:22919638}.
CC   -!- SIMILARITY: Belongs to the cytochrome ubiquinol oxidase subunit X
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAJ12892.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AM040265; CAJ12892.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_002972046.1; NZ_KN046823.1.
DR   AlphaFoldDB; Q2YKD6; -.
DR   SMR; Q2YKD6; -.
DR   STRING; 359391.BAB2_0726; -.
DR   EnsemblBacteria; CAJ12892; CAJ12892; BAB2_0726.
DR   GeneID; 45125847; -.
DR   GeneID; 55592190; -.
DR   KEGG; bmf:BAB2_0726; -.
DR   PATRIC; fig|359391.11.peg.421; -.
DR   HOGENOM; CLU_207013_0_0_5; -.
DR   UniPathway; UPA00705; -.
DR   Proteomes; UP000002719; Chromosome II.
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:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway.
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   Cell inner membrane; Cell membrane; Electron transport; Membrane;
KW   Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW   Transport; Virulence.
FT   CHAIN           1..51
FT                   /note="Cytochrome bd ubiquinol oxidase subunit X"
FT                   /id="PRO_0000424362"
FT   TOPO_DOM        1..3
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        4..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        27..51
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305|PubMed:22919638"
SQ   SEQUENCE   51 AA;  5876 MW;  3EBD961C5F792D07 CRC64;
     MWYFSWLLGL PLAAAFAVLN AMWYELMDDR ARKRLAADPT AELALEGNKH H
 
 
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