ID A4IQQ7_GEOTN Unreviewed; 687 AA.
AC A4IQQ7;
DT 01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE SubName: Full=Sensory box sigma-54 dependent DNA-binding response regulator {ECO:0000313|EMBL:ABO67661.1};
GN OrderedLocusNames=GTNG_2312 {ECO:0000313|EMBL:ABO67661.1};
OS Geobacillus thermodenitrificans (strain NG80-2).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=420246 {ECO:0000313|EMBL:ABO67661.1, ECO:0000313|Proteomes:UP000001578};
RN [1] {ECO:0000313|EMBL:ABO67661.1, ECO:0000313|Proteomes:UP000001578}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NG80-2 {ECO:0000313|EMBL:ABO67661.1,
RC ECO:0000313|Proteomes:UP000001578};
RX PubMed=17372208; DOI=10.1073/pnas.0609650104;
RA Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X.,
RA Han W., Peng X., Liu R., Wang L.;
RT "Genome and proteome of long-chain alkane degrading Geobacillus
RT thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(2007).
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DR EMBL; CP000557; ABO67661.1; -; Genomic_DNA.
DR RefSeq; WP_008879792.1; NC_009328.1.
DR AlphaFoldDB; A4IQQ7; -.
DR KEGG; gtn:GTNG_2312; -.
DR eggNOG; COG3290; Bacteria.
DR eggNOG; COG3829; Bacteria.
DR HOGENOM; CLU_000445_8_1_9; -.
DR Proteomes; UP000001578; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00009; AAA; 1.
DR CDD; cd00130; PAS; 2.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR002197; HTH_Fis.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
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 NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR32071:SF57; SIGMA L-DEPENDENT TRANSCRIPTIONAL REGULATOR YQIR-RELATED; 1.
DR PANTHER; PTHR32071; TRANSCRIPTIONAL REGULATORY PROTEIN; 1.
DR Pfam; PF02954; HTH_8; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00158; Sigma54_activat; 1.
DR PRINTS; PR01590; HTHFIS.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00091; PAS; 2.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 2.
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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000313|EMBL:ABO67661.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 115..185
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 178..230
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 230..290
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 368..598
FT /note="Sigma-54 factor interaction"
FT /evidence="ECO:0000259|PROSITE:PS50045"
SQ SEQUENCE 687 AA; 76314 MW; 2CE7F813955B2A46 CRC64;
MKKVIIIGAD ARGTSLLKLL HEASGFAVMA VIDVDDNAPG LQLARKWGIV AANDWRPWMD
KPLDLIIETT GRADVLEEIR QLAPKGANIV PSAVARMMAE LVEEKEALIA ELKSEATRRA
LIFHSSHDGM IVVDEYAYIT DMNESAAELL EVDKDKVIGE HILSVLPSSG LPRVLKTRQT
EFHQEVELAN GKKLITTRIP IIDESGKLFG ALAVFKDITE LVALAEEITD LKEMRMMLEA
IIHSSEEAIS VVDENGNGIL INPAYTRLTG LTKEEVIGKP ATADIAEGES MHMQVLKTRR
PVRGVRMKVG PKNRDVVVNV APIIVDGVLK GSVGVIHDVS EIQRLTAELN RARQIIRTLE
AKYSFADIIG EADEMKVAIE QAKLAAKTPV TILLRGESGT GKELFAHAIH NASDRKYNKF
IRVNCAAIPE TLLESELFGY EEGAFSGARR GGKRGLFEEA NNGSIFLDEI GELSASTQAK
LLRVLQEREI VRVGGTKPIP INVRVIAATN VNLEKAIADG TFREDLYYRL NRMPIYIPPL
RARKEDIPAL CRHLIQKLNQ DYGRNVEGVT NEAMARLLAY DWPGNVRELE NVLGRAMIFM
KFHEVMIDVE HLPPLATPSP TTVSRVEAEE PLRPLDEMVG EYEARLLERA LRRYHGNKTA
TARALGISVR NLYYKLEKYG LDKKSMQ
//
