ID A0A1H3Q6X7_9BACI Unreviewed; 1036 AA.
AC A0A1H3Q6X7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, 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=SAMN05421736_10617 {ECO:0000313|EMBL:SDZ08459.1};
OS Evansella caseinilytica.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Evansella.
OX NCBI_TaxID=1503961 {ECO:0000313|EMBL:SDZ08459.1, ECO:0000313|Proteomes:UP000198935};
RN [1] {ECO:0000313|Proteomes:UP000198935}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SP {ECO:0000313|Proteomes:UP000198935};
RA Varghese N., Submissions S.;
RL Submitted (OCT-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};
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DR EMBL; FNPI01000006; SDZ08459.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3Q6X7; -.
DR STRING; 1503961.SAMN05421736_10617; -.
DR Proteomes; UP000198935; Unassembled WGS sequence.
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; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
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, ECO:0000313|EMBL:SDZ08459.1};
KW 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:UP000198935};
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 7..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 206..229
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 236..252
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 272..292
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 301..323
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 329..351
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 358..376
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 396..413
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 442..660
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 706..821
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 932..1031
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 1017..1036
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 754
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1036 AA; 117531 MW; 64919C5304DE23B3 CRC64;
MSKRNTVLVV SSFLLVIISL RVLWFIHQLP LNQPFAEQGI LDLQHVSLTD KNTVVLDGEW
VFYPNVYAEP EELVDADDRQ TIQVPYGWKE SSAFIGEKEQ WGTYELWIHA PNPLERYSLK
LSRVYESFRL YANGELVEQR QSPVNMYNPQ QSVLTPAIAT VESDEKGMIH LVLTVYDSEQ
TMEAGVLNTI HFGTETAVTR KHVTSVALQI MVAAIMLLHG IYASILFFIR PKKIELLHYM
MAVLLSACAV LLSDDRLLLL WLPLDYDTFV KLAYLSYTGL SFFFVLFVRY LFSNNHRNHK
IFWLVSLLCA TYGLFIVLVP GITVREWSLL LLFVLAIPFG AILLLIIQVL LKKEKDSLFL
LLAAISILSS IFWSSFVGRV HHFNWGIISA VNPDFYPIDL LLAFLAFSCF WFIRFFRAHD
ENSELVKKLQ KEHVAKDQFL ANTSHELRNP LHGMINIAQS VKEQEGSRLT AQGRKNMELL
LTVSRRMSYL LNDLVDVTKM KQNKVSLNRQ PVDLLSVITS VVHIQQFMME AKRIRFQLEI
PENFPPVYAD ETRLAQIIFN LLHNAVKFTE DGTIVIEAEL VRKRAIITVK DTGIGMDQET
QKRIFLPYEQ GQEDSFDQYG GLGLGLSICQ QLVAMHDGTL SVTSTPLKGS EFTVTLPIAG
SAEKRREQQV KPAVKISGVA AKESVATNLP AAVAEKDKLL VQGKPKILAV DDDPMNIHVL
QNILSPEEYF METATSGKEV LQRLEEGWDL IIADVMMPEM TGYELTEAIR KQFSISELPV
LLLTARSSPE EIYTGFLSGA NDYLVKPIDS LELKVRIHAV IDLKHSIQER LRMEAAWLHA
QIQPHFLFNT LNTIASLSEI DTPRMAALLE HFGRFLQKSF DEKNLDALVP LSHELAILEA
YVYIEQERFG DRVTVHWEKE QDAACQLPPL SIQPLVENAI RHGILKKAEG GNIYIRIKQQ
KQTVKIAIAD DGVGMSKETM KKVLTRVPDQ TRGVGLLNTD TRLKQLYGKG LEITSKPGEG
TEISFQVPLT PEREHH
//
