ID   CBXXP_CUPNH             Reviewed;         317 AA.
AC   Q04540;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Protein CbxX, plasmid;
GN   Name=cbxXP; Synonyms=cfxXP; OrderedLocusNames=PHG425;
OS   Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS   / H16 / Stanier 337) (Ralstonia eutropha).
OG   Plasmid megaplasmid pHG1.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=381666;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1429456; DOI=10.1128/jb.174.22.7337-7344.1992;
RA   Kusian B., Yoo J.-G., Bednarski R., Bowien B.;
RT   "The Calvin cycle enzyme pentose-5-phosphate 3-epimerase is encoded within
RT   the cfx operons of the chemoautotroph Alcaligenes eutrophus.";
RL   J. Bacteriol. 174:7337-7344(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
RX   PubMed=12948488; DOI=10.1016/s0022-2836(03)00894-5;
RA   Schwartz E., Henne A., Cramm R., Eitinger T., Friedrich B., Gottschalk G.;
RT   "Complete nucleotide sequence of pHG1: a Ralstonia eutropha H16 megaplasmid
RT   encoding key enzymes of H(2)-based lithoautotrophy and anaerobiosis.";
RL   J. Mol. Biol. 332:369-383(2003).
CC   -!- FUNCTION: Seems to be necessary for the expression of RuBisCO.
CC   -!- SIMILARITY: Belongs to the CbxX/CfxQ family. {ECO:0000305}.
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DR   EMBL; M64172; AAA98229.1; -; Genomic_DNA.
DR   EMBL; AY305378; AAP86174.1; -; Genomic_DNA.
DR   RefSeq; WP_011154337.1; NZ_CP039289.1.
DR   AlphaFoldDB; Q04540; -.
DR   SMR; Q04540; -.
DR   STRING; 381666.PHG425; -.
DR   EnsemblBacteria; AAP86174; AAP86174; PHG425.
DR   GeneID; 39976483; -.
DR   KEGG; reh:PHG425; -.
DR   PATRIC; fig|381666.6.peg.353; -.
DR   eggNOG; COG0464; Bacteria.
DR   HOGENOM; CLU_008749_1_0_4; -.
DR   OMA; HRPDNER; -.
DR   OrthoDB; 1115436at2; -.
DR   Proteomes; UP000008210; Plasmid megaplasmid pHG1.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041627; AAA_lid_6.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR000470; CbxX/CfqX_mono.
DR   InterPro; IPR000641; CbxX/CfxQ.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF17866; AAA_lid_6; 1.
DR   PRINTS; PR00819; CBXCFQXSUPER.
DR   PRINTS; PR00820; CBXXCFQX.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR02880; cbbX_cfxQ; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Nucleotide-binding; Plasmid; Reference proteome.
FT   CHAIN           1..317
FT                   /note="Protein CbxX, plasmid"
FT                   /id="PRO_0000063033"
FT   BINDING         85..92
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   317 AA;  34946 MW;  717360719A2D4444 CRC64;
     MSAPETTAPL QPPAAQAASL PGSLAESLAS SGITELLAQL DRELIGLKPV KARIRDIAAL
     LLVDKLRAAR GFSAGAPSLH MCFTGNPGTG KTTVAMRMAQ ILHQLGYVRR GHLVAVTRDD
     LVGQYIGHTA PKTKEILKKA LGGVLFIDEA YYLYRPENER DYGQEAIEIL LQVMENNRDD
     LVVILAGYKD RMDRFFESNP GMSSRVAHHV DFPDYQLDEL RQIADLMLAE MQYRFDDESR
     AVFADYLARR MAQPHFANAR SVRNALDRAR LRHASRLLDD AGTVADDRTL TTITASDLLA
     SRVFSKAAPA AQTPAKE