ID   HOXA_CUPNH              Reviewed;         482 AA.
AC   P29267; Q7WXU1;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 2.
DT   03-AUG-2022, entry version 161.
DE   RecName: Full=Hydrogenase transcriptional regulatory protein HoxA;
GN   Name=hoxA; OrderedLocusNames=PHG019;
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=2001989; DOI=10.1128/jb.173.6.1845-1854.1991;
RA   Eberz G., Friedrich B.;
RT   "Three trans-acting regulatory functions control hydrogenase synthesis in
RT   Alcaligenes eutrophus.";
RL   J. Bacteriol. 173:1845-1854(1991).
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: Probable member of the two-component regulatory system
CC       involved in the regulation of the hydrogenase activity. HoxA is
CC       probably phosphorylated by a sensory component (which could be HoxX)
CC       and then acts in conjunction with sigma-54 as a transcriptional
CC       activator.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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DR   EMBL; M64593; AAA21971.1; -; Genomic_DNA.
DR   EMBL; AY305378; AAP85775.1; -; Genomic_DNA.
DR   PIR; A38533; A38533.
DR   RefSeq; WP_011153944.1; NZ_CP039289.1.
DR   AlphaFoldDB; P29267; -.
DR   SMR; P29267; -.
DR   STRING; 381666.PHG019; -.
DR   EnsemblBacteria; AAP85775; AAP85775; PHG019.
DR   GeneID; 39976594; -.
DR   KEGG; reh:PHG019; -.
DR   PATRIC; fig|381666.6.peg.15; -.
DR   eggNOG; COG2204; Bacteria.
DR   HOGENOM; CLU_000445_0_6_4; -.
DR   OMA; ILCDQRM; -.
DR   OrthoDB; 123059at2; -.
DR   Proteomes; UP000008210; Plasmid megaplasmid pHG1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR002197; HTH_Fis.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   InterPro; IPR002078; Sigma_54_int.
DR   InterPro; IPR025662; Sigma_54_int_dom_ATP-bd_1.
DR   InterPro; IPR025943; Sigma_54_int_dom_ATP-bd_2.
DR   InterPro; IPR025944; Sigma_54_int_dom_CS.
DR   Pfam; PF02954; HTH_8; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   Pfam; PF00158; Sigma54_activat; 1.
DR   PRINTS; PR01590; HTHFIS.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF46689; SSF46689; 1.
DR   SUPFAM; SSF52172; SSF52172; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
DR   PROSITE; PS00675; SIGMA54_INTERACT_1; 1.
DR   PROSITE; PS00676; SIGMA54_INTERACT_2; 1.
DR   PROSITE; PS00688; SIGMA54_INTERACT_3; 1.
DR   PROSITE; PS50045; SIGMA54_INTERACT_4; 1.
PE   3: Inferred from homology;
KW   Activator; ATP-binding; Cytoplasm; DNA-binding; Nucleotide-binding;
KW   Phosphoprotein; Plasmid; Reference proteome; Transcription;
KW   Transcription regulation; Two-component regulatory system.
FT   CHAIN           1..482
FT                   /note="Hydrogenase transcriptional regulatory protein HoxA"
FT                   /id="PRO_0000081109"
FT   DOMAIN          7..121
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   DOMAIN          167..394
FT                   /note="Sigma-54 factor interaction"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT   DNA_BIND        456..475
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000250"
FT   BINDING         193..200
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT   BINDING         265..274
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT   MOD_RES         55
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   CONFLICT        468
FT                   /note="V -> G (in Ref. 1; AAA21971)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   482 AA;  53587 MW;  622CFA9496CA8BE6 CRC64;
     MSDKQATVLV VDDETRSQDA LRRTLDEEFR VLTVSSADEA RALLLRQPVS VILCDQRMPG
     LTGVEFLKEV RERWPEIVRI VISGYTDSED IIAGVNEAGI YQYILKPWVP DHLIDTVRQA
     VEAQGLQGDM HRLDLELRTS TPVLRQRSSQ KLASAQSAFN FERIVRAPGS PLDAVCEVAA
     RVARYDLPVM VLGESGTGKE LLARAIHYAS PRAARAFVSE NCAAVPDNLL ESELFGHKRG
     AFTGAYEDHA GLFQRANGGT IFLDEIGDTS PAFQVKLLRV LQEGEVRPVG SPRWIPVDVR
     VIAATHCNLE SDVHAGRFRE DLYYRIAGVT ISMPPLRERS GDLQPIAAKL LEQVAQELAR
     PGLYFGGDAL AAMMAYPWPG NIRELRNEIY RAVALSSGEE IRAQLFSRKV LHGQPGTVKR
     GPHVQTFPQS GTLQERLDAI EAVVLKEALL RHRWNKTHAA KELGLSRVGL RQKLLRFGLE
     EK