HUPR_RHOCA
ID HUPR_RHOCA Reviewed; 492 AA.
AC P26408; Q6LDK4;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Hydrogenase transcriptional regulatory protein HupR1;
GN Name=hupR1;
OS Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=1061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33303 / B10;
RX PubMed=1885559; DOI=10.1128/jb.173.18.5928-5932.1991;
RA Richaud P., Colbeau A., Toussaint B., Vignais P.M.;
RT "Identification and sequence analysis of the hupR1 gene, which encodes a
RT response regulator of the NtrC family required for hydrogenase expression
RT in Rhodobacter capsulatus.";
RL J. Bacteriol. 173:5928-5932(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8497190; DOI=10.1111/j.1365-2958.1993.tb01199.x;
RA Colbeau A., Richaud P., Toussaint B., Caballero F.J., Elster C.,
RA Delphin C., Smith R.L., Chabert J., Vignais P.M.;
RT "Organization of the genes necessary for hydrogenase expression in
RT Rhodobacter capsulatus. Sequence analysis and identification of two hyp
RT regulatory mutants.";
RL Mol. Microbiol. 8:15-29(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-169.
RC STRAIN=ATCC 33303 / B10;
RX PubMed=2007559; DOI=10.1128/jb.173.7.2401-2405.1991;
RA Xu H.-W., Wall J.D.;
RT "Clustering of genes necessary for hydrogen oxidation in Rhodobacter
RT capsulatus.";
RL J. Bacteriol. 173:2401-2405(1991).
CC -!- FUNCTION: Probable member of the two-component regulatory system
CC involved in the regulation of the [NiFe] hydrogenase activity. HupR1 is
CC probably phosphorylated by the sensory component and then acts in
CC conjunction with sigma-54 as a transcriptional activator.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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DR EMBL; M63670; AAA26104.1; -; Genomic_DNA.
DR EMBL; X61007; CAA43327.1; -; Genomic_DNA.
DR EMBL; M55089; AAA72927.1; -; Genomic_DNA.
DR PIR; S32951; S32951.
DR RefSeq; WP_013066522.1; NZ_VIBE01000017.1.
DR PDB; 2JK1; X-ray; 2.10 A; A=5-140.
DR PDB; 2VUH; X-ray; 2.50 A; B=5-140.
DR PDB; 2VUI; X-ray; 2.90 A; B=5-140.
DR PDBsum; 2JK1; -.
DR PDBsum; 2VUH; -.
DR PDBsum; 2VUI; -.
DR AlphaFoldDB; P26408; -.
DR SMR; P26408; -.
DR GeneID; 31489720; -.
DR OMA; FHKNGAD; -.
DR EvolutionaryTrace; P26408; -.
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; 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; 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; 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; PS00688; SIGMA54_INTERACT_3; 1.
DR PROSITE; PS50045; SIGMA54_INTERACT_4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; ATP-binding; Cytoplasm; DNA-binding;
KW Nucleotide-binding; Phosphoprotein; Transcription;
KW Transcription regulation; Two-component regulatory system.
FT CHAIN 1..492
FT /note="Hydrogenase transcriptional regulatory protein
FT HupR1"
FT /id="PRO_0000081111"
FT DOMAIN 7..121
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DOMAIN 164..393
FT /note="Sigma-54 factor interaction"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT DNA_BIND 452..471
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 255..264
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 STRAND 7..11
FT /evidence="ECO:0007829|PDB:2JK1"
FT HELIX 15..25
FT /evidence="ECO:0007829|PDB:2JK1"
FT TURN 26..28
FT /evidence="ECO:0007829|PDB:2JK1"
FT STRAND 31..36
FT /evidence="ECO:0007829|PDB:2JK1"
FT HELIX 37..46
FT /evidence="ECO:0007829|PDB:2JK1"
FT STRAND 49..56
FT /evidence="ECO:0007829|PDB:2JK1"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:2JK1"
FT HELIX 63..73
FT /evidence="ECO:0007829|PDB:2JK1"
FT STRAND 77..84
FT /evidence="ECO:0007829|PDB:2JK1"
FT HELIX 89..97
FT /evidence="ECO:0007829|PDB:2JK1"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:2JK1"
FT HELIX 110..140
FT /evidence="ECO:0007829|PDB:2JK1"
SQ SEQUENCE 492 AA; 53838 MW; 5BCF1ADCFE83A28A CRC64;
MAASAPAILL VDDEPHSLAA MKLALEDDFD VLTAQGAEAA IAILEEEWVQ VIICDQRMPG
RTGVDFLTEV RERWPETVRI IITGYTDSAS MMAAINDAGI HQFLTKPWHP EQLLSSARNA
ARMFTLAREN ERLSLEMRLL NSTSESRVEK RRRALREGMG FETILRTPNS AMTGAIALAR
QFASFDVPVL LRGEPGSGRA QLARAMHYVS LRSDKPFYEI NLAGLPEDLA MIELFGARRG
VLPGGVAKIG LAQKADRGTL FVAGVEAASP ALQLALLRML ADGAITPLGG QETASTNLRL
ITGAAADLRA MVAEGRFRAD LYYALSAGEI ALPPLRARRG DVALLAQSML AEAAVRHGKQ
ALGFDAAALE FLENYDWPGN LRELHNEVTR MLIFAQDNVL GAELISRHIL QAAPSESGAD
RSAEEVMTAD GTLKDRIELI EMRILRETLT RNRWNKSRAA AELGLSRVGL RAKLDRYGIE
HPAGRVQEEE ED
