ID A0A1R1A957_9BACL Unreviewed; 1302 AA.
AC A0A1R1A957;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BK120_15550 {ECO:0000313|EMBL:OME82094.1};
OS Paenibacillus sp. FSL A5-0031.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1920420 {ECO:0000313|EMBL:OME82094.1, ECO:0000313|Proteomes:UP000187447};
RN [1] {ECO:0000313|EMBL:OME82094.1, ECO:0000313|Proteomes:UP000187447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL A5-0031 {ECO:0000313|EMBL:OME82094.1,
RC ECO:0000313|Proteomes:UP000187447};
RA Beno S.M.;
RT "Paenibacillus species isolates.";
RL Submitted (NOV-2016) 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};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OME82094.1}.
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DR EMBL; MRTD01000008; OME82094.1; -; Genomic_DNA.
DR Proteomes; UP000187447; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; cd06225; HAMP; 1.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR CDD; cd18773; PDC1_HK_sensor; 1.
DR CDD; cd00156; REC; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 4.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003660; HAMP_dom.
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; IPR036641; HPT_dom_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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 2.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 291..314
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 315..368
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 366..437
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 455..507
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 504..542
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 576..628
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 646..868
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 887..1008
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1034..1150
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1199..1294
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT COILED 1270..1297
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 940
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1083
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1238
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1302 AA; 147185 MW; D68388F1D6A4CAF9 CRC64;
MSKSGRFGSC VAEGGSGLKK MSLRTKGLIL IVLISFFPLL IAGIGNYSAV KDAMLKSEIE
KTSSMQNKRA NELASWMAIR KAEVIVMSRT EVVRFGTDEE RLHYFGRELV RGGFIYHSIG
YIDESGISLR TDGIRRDMSM ESFFQESITG KVVITDPFKP SFSDATQSFI VVPVYGATNE
LKGVVYASIV MATLRPFIEF TGDQTIIRLF NDEGGIIYSS DNQEIISKGL FHEKSSLSPI
AEKMLGSYEG VSEINIAGRS YAVFHTKVSE TPWRFALQEP MSKLEEEVKP IFWRIFTTIA
VSEVIIVIFF FLYFERIVKR LERILGVTEQ AAAGSFEAEH LEVEPYDEIG QLGHSVNGMM
EHLQEMFDRL EAIINQNQYA FIVLDDQYKV TYLNKTAEEM LGYKTSELAG SATPLLFMDL
DEVRLEAEKL SEQLGRTVQP GLEVFKELRS TSFSYEREWT FIHKNGTRIP TLHSSNGLRD
RNGRFSGVVG MVLDISDRKH VEKARNRLLD IVESAKDLIA SVSSRGKLVY MNGAGREMLG
LQSNADQVHM VEEYSHPEMY SELVRGAALA KEFGYWESDA QLMKRNGEPL YVSMVIVPHK
DEDTGELFFS CIARDISEQK MVQEKLVRAT LEAEEANQAK SRFLALMSHE IRTPLNGIIG
LTQLMRKTGL SSSQKDYMDK MNTSSETLLR IINDILDFSK IEAGKVDIER QPFQPEELMH
RITDQLSVFM GGKEQFEFII DTPEELPQTI IGDALRLEQV LLNLCMNAIK FTNRGKVRLK
LEIVEQTDKG VNVKFIISDT GIGMSEAQVQ KLFKPFTQAD GSTTRKFGGT GLGLVISKSF
VELMGGKLKV TSKALVGSEF YFTLPFTIIH KYTEPRLQVH QDLLEQPVWI VEDDDEMREH
WSDIIESFGL TPIPFHSWKM ARDRLRRIGA GALPKLIVLD MEMPDMYGAE TWLEFHRDAE
LAGVKTIAMT TSYGRDEMMQ LPAEQRPVTL LIKPIMRTAM LRAIESVLDH KGTDGKEQEI
ESVATIQQNV TNTRILLAED NKINQLVAIE ILKERGYEVG LAENGEEVLI KLGEERWDLI
LMDIHMPIMD GSEAVRIIRT QAKYDHIPII AVTANVLRND HERYLKLGMN DVVTKPISSE
RIHNVISYWL KEINGSTIQP VVKSGLNDRS RALEPANIDS LPSIDGMDVE SALARVNGKL
PILLHMMEQF MLDYDSFADQ LRMMVKQSEL TIVKRMAHTL KGAAGYLSAY ELLEAACEVE
RIVKLPELES DNLQKAINQL EVTLKRLLDG LRKAKDVFDN KT
//