ID G4HFI5_9BACL Unreviewed; 1009 AA.
AC G4HFI5;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=PaelaDRAFT_2746 {ECO:0000313|EMBL:EHB64502.1};
OS Paenibacillus lactis 154.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=743719 {ECO:0000313|EMBL:EHB64502.1, ECO:0000313|Proteomes:UP000003891};
RN [1] {ECO:0000313|EMBL:EHB64502.1, ECO:0000313|Proteomes:UP000003891}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=154 {ECO:0000313|EMBL:EHB64502.1,
RC ECO:0000313|Proteomes:UP000003891};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Land M.L., Hauser L., Siebers A., Thelen M., Hugenholtz P.,
RA Allgaier M., Woyke T.J.;
RT "The draft genome of Paenibacillus lactis 154.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
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DR EMBL; AGIP01000005; EHB64502.1; -; Genomic_DNA.
DR RefSeq; WP_007129916.1; NZ_AGIP01000005.1.
DR AlphaFoldDB; G4HFI5; -.
DR STRING; 743719.PaelaDRAFT_2746; -.
DR PATRIC; fig|743719.3.peg.2774; -.
DR eggNOG; COG2202; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR OrthoDB; 9815750at2; -.
DR Proteomes; UP000003891; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 5.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.10.70.100; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 6.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 5.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08447; PAS_3; 2.
DR Pfam; PF13188; PAS_8; 1.
DR Pfam; PF13426; PAS_9; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 5.
DR SMART; SM00091; PAS; 6.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 6.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 4.
DR PROSITE; PS50112; PAS; 4.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EHB64502.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 133..194
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 203..255
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 376..447
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 450..501
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 502..572
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 574..625
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 626..701
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 705..756
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 770..993
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 1009 AA; 114365 MW; 5E620897BC45FC00 CRC64;
MRNFTEDWFW EPMFNKLPVG AVLISLKTEQ IVMMNERFCE ILGSTRSELL TRKPRELLVL
KGLSQKALQR IESYDVANGL QEKISFQSAD GRAMSITAEF SLLASPANGK EPLILCCIDR
AEIKEAPLPM IRQEELLALI LKSGQDLISI SNADGIIEYI SPSATHLLGY RQEEMVGRHR
AEFYHSADSE EMKQPGKLFS DSEIFNRRIR HKDGHYLWFE TSFHVIRGAE GQITKVLAIA
RNITKRKIDE DTLARAQRIA KIGSWRWDLV TRTLSFSEEI RRIYGYQLEP VERDHKSLLS
AVVTEDRKRL RRAILSAIKG QPDEIIYRIQ VEGGTIRTLR AQWEVSARSE GKPIELVGMA
QDITEESLIA QQLVENEKKY RLITENSLDF ISRNTIDDCT FLYCSPSCYS LLGYSPEELV
GTSAFDYVYP EDIGPLKAYL QRTLDETSLT PITFRYLHKD GRHIWFEVNC KFITGQDGHR
EIISIARDIS ERKRIEFKLK ESEQRYRSLF EYNPLAVYSM NLEGEYLTAN PNLQKLTGYS
LDELVGMYYG PIVADKDLPR TQYHFNQAKE GNPQSYDLSI IHKDGHPIEI NTVNIPIIVD
EEVVGVYGIT RDITERNRSM EEIKKLSREL TLLLNTVSEG IIGLDINGKV AFINPAGASM
LGEDAGDVIG RSCDQIIREI RHDGSFYRGR NSPLEMALLQ GTPLLRTEIV LWRRDGTSFL
ANYQVNPIWD RGERKGAVMV FRDITDEKEI IRAKESAERA DQAKTEFLTM MSHELRTPMN
GIMGMIDLLK TTDLDEEQAN YTDILKESGE SLLHILNDIL DFSRIETGKM SIGEEPIDVR
SLLGSVVDLF NAKASEKGLT LSWSVNEDSV PDVIVADPLR LRQVLVNLIS NAIKFTEQGS
VTLTADAVRR IGTRELTLTI RVTDTGIGIP ADRQHQLFLS FTQLHPSLNR KYGGTGLGLA
ISKKLVELMG GIIGVDSREF GGSTFYFSIP TRAVEPKDTS LTPVEEAYE
//
