ID F3MEW3_9BACL Unreviewed; 1219 AA.
AC F3MEW3;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=HMPREF9412_4638 {ECO:0000313|EMBL:EGG34106.1};
OS Paenibacillus sp. HGF5.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=908341 {ECO:0000313|EMBL:EGG34106.1, ECO:0000313|Proteomes:UP000004272};
RN [1] {ECO:0000313|EMBL:EGG34106.1, ECO:0000313|Proteomes:UP000004272}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HGF5 {ECO:0000313|EMBL:EGG34106.1,
RC ECO:0000313|Proteomes:UP000004272};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (FEB-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};
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:EGG34106.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AEXS01000143; EGG34106.1; -; Genomic_DNA.
DR RefSeq; WP_009594103.1; NZ_AEXS01000143.1.
DR AlphaFoldDB; F3MEW3; -.
DR OrthoDB; 9790669at2; -.
DR Proteomes; UP000004272; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd19411; MCP2201-like_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; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 3.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR024478; HlyB_4HB_MCP.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR047347; YvaQ-like_sensor.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF12729; 4HB_MCP_1; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 3.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 3.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 3.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF90257; Myosin rod fragments; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 3.
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};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, 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 6..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 208..261
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 548..779
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 832..945
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 954..1070
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1100..1217
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 437..538
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 881
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1003
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1150
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1219 AA; 137485 MW; C5897455EDC59E3B CRC64;
MKLKSKLVIG FTTLLALMLV LTLIGYDRIS YMNNQMDQIF QERYQKVRNS SGMRGEVNNM
ARELTNMILS NDPSTYTVSK QEIETMTAQA EEYFRAIKES VNTAEEQQLL VRIERAVNEY
IVYQNKTLEL LSTSDADGAN ALRNSTGQSV QEEMLISLNE LSSYENQKIN DDIAAAKAAY
DRSVQMFIYI MAGGLLIGML VILWILPSIT RGINVVSMML KSFGEGRLKA IRRIKVTSKD
EFGDVARVFK DLSEDIIEKQ RIEETYLQAQ RDQSWLNSNM ARVTELLEGI NSLEEVGQRF
ISEFTPILGA HYGAIYIRQE DKHPNKLEMK GSYAHEGGEE PKVAFMIGEG LVGQAALDKK
PVVLKGAPEG YMNVESAWGS SKPVSIMIYP LLFENEVLGV VELASFEETT TLQEQLMSQL
SQSLGIILNN ITGRLRVEQL LRESQAMTEE LQVQSEELQT QQEELRRTNE NLEEQTNALK
RSEDLLQRQQ EELEHYNTEL VAKTRALEEQ VQEVEEKNDE IEKARMQLEQ QAKQLSITTK
YKSEFMANMS HELRTPLNSL LILSQLLSEN KDGNLSSKQI EYAQTIYMSG SDLLKMIDEI
LDLSKVDAGK MEINYEDVQL PDIEAFVEQN FAAVASRKHI NLGVRIEEEL PQSIVTDSHR
VKQILRNLLS NAFKFTNSGS VELLVEKADK DKLPVYLNAE SDYVSFAVKD TGIGIPADKT
DLIFEAFQQV DGTTSRKYGG TGLGLSISRE LSRLLGGGIT VESEEGKGSC FTLFLPASHP
EVADGAKEAA AAMEAPPESS LIVPKAKMVT KEVQPAIQVD DDRNQLGPTD KVLLIIEDDV
KFARILLDMA RGRGFKALVA LQGDIGLEMA KSYRPDAIIL DIQLPVIDGW SVMGELKSSA
VTRHIPVHVI SVVDEVKQGL MMGAIAYLKK PSSREALEDA FTHIQSYAEK SMKHLLIVED
DDIQRNSIIE LIGHDDVSIT AASTGAEALS ELRKQRYDCM VLDLMLTDMT GFELLDQIRD
DENLVDLPII IYTGKDLDSK EEMQLRKYAE SIIIKDVKSP ERLLDETTLF LHRVEADLPE
DKRKILQKLH NKEELFEGKK ILLVDDDIRN VFALSSVLEG YNMEVTFAEN GREAIELLQQ
NPDFDLVLMD MMMPEMDGYE AMRRLREMPE FDKLPIIALT AKAMKEDRAK CIEAGASDYM
KKPIQTEQLL SLMRVWLYS
//
