HOXA_BRADU
ID HOXA_BRADU Reviewed; 485 AA.
AC P31908;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 28-FEB-2003, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Hydrogenase transcriptional regulatory protein HoxA;
GN Name=hoxA; OrderedLocusNames=bll6925;
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium.
OX NCBI_TaxID=224911;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CB1809;
RX PubMed=8510650; DOI=10.1007/bf00281623;
RA van Soom C., Verreth C., Sampaio M.J., Vanderleyden J.;
RT "Identification of a potential transcriptional regulator of hydrogenase
RT activity in free-living Bradyrhizobium japonicum strains.";
RL Mol. Gen. Genet. 239:235-240(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(2002).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA78991.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; Z17373; CAA78991.1; ALT_FRAME; Genomic_DNA.
DR EMBL; BA000040; BAC52190.1; -; Genomic_DNA.
DR PIR; S35232; S35232.
DR RefSeq; NP_773565.1; NC_004463.1.
DR RefSeq; WP_011089663.1; NZ_CP011360.1.
DR AlphaFoldDB; P31908; -.
DR SMR; P31908; -.
DR STRING; 224911.27355206; -.
DR PRIDE; P31908; -.
DR EnsemblBacteria; BAC52190; BAC52190; BAC52190.
DR GeneID; 64026681; -.
DR KEGG; bja:bll6925; -.
DR PATRIC; fig|224911.44.peg.6959; -.
DR eggNOG; COG2204; Bacteria.
DR HOGENOM; CLU_000445_0_6_5; -.
DR InParanoid; P31908; -.
DR OMA; ILCDQRM; -.
DR PhylomeDB; P31908; -.
DR Proteomes; UP000002526; Chromosome.
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; Reference proteome; Transcription;
KW Transcription regulation; Two-component regulatory system.
FT CHAIN 1..485
FT /note="Hydrogenase transcriptional regulatory protein HoxA"
FT /id="PRO_0000081110"
FT DOMAIN 6..120
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DOMAIN 166..392
FT /note="Sigma-54 factor interaction"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT DNA_BIND 451..470
FT /note="H-T-H motif"
FT /evidence="ECO:0000250"
FT REGION 404..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 192..199
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT BINDING 264..273
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT MOD_RES 54
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT CONFLICT 291..293
FT /note="QRV -> ARC (in Ref. 1; CAA78991)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 485 AA; 54058 MW; C31765087F290740 CRC64;
MSIQGTILVV DDEVRSQEAL RRVLREDFEV LCVGNATDAE KLLEGEIVHA ILCDQRMPHE
SGVSFLKRVR ELWPDPVRMI ISGYSESEDI IAGLNEAGIY QYITKPWQPD QLVETVKEAV
QLYRLQKETE TAGVDVKATS GHIKKVVSVK RGVAKQLYDF DRIVHSTESP MHAVIELGRR
AADYDISVLI TGESGTGKEL LARAIHYGSA RANRAFVVEN CGALPDELLE SELFGCKKGA
FTGAYQDRIG LFEVADGGTI FLDEIGETSP AFQVKLLRVL QESEIRPLGA QRVRKVDVRV
VAATNRDLEA EVEAGRFRRD LYYRLAAFPV HMPALRERPM DIPLIAEGVL SAVKSSFNRP
NLRFARSALE EFGKYHWPGN VRELQNEIQR MAVLADRDEL AAPPLLGRRN GKRSAPLPAH
GRLNGSASLK DKVEDLEKSV IMNCLERNDG NISRVASELG LSRVGLRNKL SRYDLRKNAK
GDAFS
