ID F5LPU1_9BACL Unreviewed; 1137 AA.
AC F5LPU1;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=HMPREF9413_5299 {ECO:0000313|EMBL:EGL15668.1};
OS Paenibacillus sp. HGF7.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=944559 {ECO:0000313|EMBL:EGL15668.1, ECO:0000313|Proteomes:UP000003445};
RN [1] {ECO:0000313|EMBL:EGL15668.1, ECO:0000313|Proteomes:UP000003445}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HGF7 {ECO:0000313|EMBL:EGL15668.1,
RC ECO:0000313|Proteomes:UP000003445};
RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton 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:EGL15668.1}.
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DR EMBL; AFDH01000112; EGL15668.1; -; Genomic_DNA.
DR RefSeq; WP_009675879.1; NZ_AFDH01000112.1.
DR AlphaFoldDB; F5LPU1; -.
DR OrthoDB; 9790669at2; -.
DR Proteomes; UP000003445; 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; 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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 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; 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 PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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}; Reference proteome {ECO:0000313|Proteomes:UP000003445};
KW 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 33..55
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 57..110
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 457..687
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 750..863
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 872..988
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1018..1135
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 280..440
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 799
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 921
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1068
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1137 AA; 126176 MW; 30C937FDF4780E6D CRC64;
MNIKGKVWLG TAVSILVIGG LTAMACIFLD GVFLALSLIL GLIGLATGVY LITGIHRGIN
KGMHRVSQIV GDIAQGTVNP SDRSAEAGDE FGQLAQSFRS LAVDLYTKTE EERILRLEAE
EQAWINVHVT EMAILLQGSV QIATASRIFI GKLASCVQAA YGALYVQKDG LLQFAAGYAY
DDTAAERRQP IALGSGLVGQ SALDKKTILL HDLPDGYVKV HSALGDTKPA ALIIVPVCYE
DEVVAVIELA SLRDFTPKER QLIDLTTANM GILLNTLADV VRIGELLKET QLQKEELEAQ
TEELQSQTEE LQAQTEELQM QAEELESQTE ELQAQTEELQ MQADSLHTSN ERLQEEMKLT
ELQKEEIKQQ ADELKAQAEE LFESNKQLQE QMELTELQKT EISEQADELK EQAEELLASN
ENLKQQVELT ERQKIEIKEQ ADEIFMAAQY KSEFLANVSH ELRTPLNSLL ILSQILAENK
EGNLHSRQLE YIHTIFSAGK DLLTLIDEIL DLAKLEVGKM TAVVEPTYLK DVSSHLYRHF
EQQAKEKNIH FDIHSDRRLP ESILTDGHRL QQILNNLLSN ALKFTEKGAV TLSIHGASAP
TGREGQAAAE EIVFSVTDTG IGIPASKLES IFEAFQQADG TTSRKYGGTG LGLTICRELA
ALLGGRIEVS SAEGEGSTFS LHLPAAQPGT AVSQAAAASD TMSAASEQAK RGKSSFQESF
VPDISISNPK LLQLAEMEDD RDNLQPGDTL LLIIEEDAEF ASTLLNLARQ RNFKAIVASQ
GDQGLALAHA YKPDAILLDI QLPVLDGWSI ISRLKGRPEL RHIPIHVIST AEENQQGLAM
GALAFWKKPN DVHELEAAFL QIESYIRRRT KSLLIVEDNP VLRSSVVAFI AHPDVNIVAV
ATGREALEQL ASHHFDCMVL DLGLSDISGF DLLEQVKTNR KLQTLPVIIF TGKELSKQDE
QRLHHYAESI VIKNVRSMER LYDETALYLH RKHADLPADK QELIEKLHNP EAAFQDKNIL
LVDDDMRNIF ALSSVLEGYN MNIQFAQNGK EALIILRNHP EVDLVFMDIM MPEMDGYETM
REIRKMPEFE KLVIIALTAR AMDEDRVKCL QAGASDYISK PINTTQLVSM LKTWLIT
//
