ID A0A3Q8S589_9BACL Unreviewed; 1020 AA.
AC A0A3Q8S589;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=EIM92_14915 {ECO:0000313|EMBL:AZK47290.1};
OS Paenibacillus lentus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1338368 {ECO:0000313|EMBL:AZK47290.1, ECO:0000313|Proteomes:UP000273145};
RN [1] {ECO:0000313|EMBL:AZK47290.1, ECO:0000313|Proteomes:UP000273145}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25539 {ECO:0000313|EMBL:AZK47290.1,
RC ECO:0000313|Proteomes:UP000273145};
RA Kook J.-K., Park S.-N., Lim Y.K.;
RT "Genome sequencing of Paenibacillus lentus DSM25539(T).";
RL Submitted (NOV-2018) 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; CP034248; AZK47290.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3Q8S589; -.
DR KEGG; plen:EIM92_14915; -.
DR OrthoDB; 9809348at2; -.
DR Proteomes; UP000273145; Chromosome.
DR GO; GO:0016020; C: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; cd00082; HisKA; 1.
DR CDD; cd17574; REC_OmpR; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 2.
DR InterPro; IPR011623; 7TMR_DISM_rcpt_extracell_dom1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR008979; Galactose-bd-like_sf.
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; IPR010559; Sig_transdc_His_kin_internal.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43047:SF83; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF07695; 7TMR-DISM_7TM; 1.
DR Pfam; PF02518; HATPase_c; 2.
DR Pfam; PF06580; His_kinase; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 2.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 2.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
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}; Reference proteome {ECO:0000313|Proteomes:UP000273145};
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 214..235
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 242..258
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 278..296
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 308..329
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 335..352
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 364..385
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 438..656
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 696..812
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 852..1020
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT MOD_RES 745
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1020 AA; 116113 MW; 1969B14029E8D649 CRC64;
MIRRKILLVS LLFLSVLTGF RFIWLHFFTT PSHPTAVQGK LDLRDWKQLT NHTVRLDGEW
EFYPNTFFMQ NSEISTALED PIDYIPVPDS WKFPKKQSTN PYYGFGSYRL RILVDPNQGK
SYAFHITSIT ASSKMYVNGQ LIGQTGQPAK HKEAYEPLDT PYTAYYTLEE NADVLNVVIQ
VANFDNVRKG GMVRSIKFGL ESVLNREMNF ANDMVRLACV AYMIHALYGI VLFFIGNRDK
RLLYFSGMIT CIVLGTLLDG ERLLLVWLPF NYQWSIKILF ISMISGGYFL IQTLRYHLPY
WLKTTGSLLY VIICFASILS VLLLPASYIS MLQPFYILIM FIPCLLAPVV MFSSTTESSR
ENIFLLLAAI AAISSLIWLF ILYALRIEMM SYPFDLIIAT ICFAAFWFKR YFQVLDDSQK
LTRKLQRADK HKDDFLTTVA HELRNPLHGI LNILQSVSER EKETLGHKST KDLELLMMVG
QRMSFMLNDL LDLGRLKENR IKLQPTPVSI HSLTATVINM LQFMTEGKPI RFSNRIPNNF
PYVMADENRL IQILVNLLHN SIKYSYAGEV SIHASVEKEW AKVSVVDSGI GMEPEVLERI
FEPYEQAVQG ISALGGGFGL GLNICKQLVE LHGGTMTARS KSNEGSVFTF TLKLADTSKL
TFEPVTSPYS YVFPTSPSEA DLETSAMRER ANDRIRLLAV DDDSVNLKVL ESIFASESYE
VITATSGQEA LLKLGGCDFD LVISDVMMPN MSGYELTSRI RERYSLSELP VLLLTAYNRD
EDIEAGFRVG ANDYVTKPMK ATELKSRVLS LTKLKRSVNE RLRIEAAWLQ AQIKPHFILN
TFTAIAELSR VDMERMDALV EELDNFIRLS IDFQNSDQAA SLEHELSLVQ SYLYIQKERF
GDRLQVIWEV DNSIQIEIPP LTIQPLVENA VIHGVLDRLA GGEVRICIKQ SEHEVEVRIS
DNGKGMEDER LQHILERQVD NRTGIGLHNT DRRLKQLYGS GFKIDSKPGE GTTVSFSIKK
//
