ID A0A1H8HH93_9BACL Unreviewed; 952 AA.
AC A0A1H8HH93;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN05518847_103191 {ECO:0000313|EMBL:SEN55404.1};
OS Paenibacillus sp. OV219.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1884377 {ECO:0000313|EMBL:SEN55404.1, ECO:0000313|Proteomes:UP000199330};
RN [1] {ECO:0000313|EMBL:SEN55404.1, ECO:0000313|Proteomes:UP000199330}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OV219 {ECO:0000313|EMBL:SEN55404.1,
RC ECO:0000313|Proteomes:UP000199330};
RA de Groot N.N.;
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};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; FOCJ01000003; SEN55404.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8HH93; -.
DR STRING; 1884377.SAMN05518847_103191; -.
DR OrthoDB; 9809348at2; -.
DR Proteomes; UP000199330; 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 GO; GO:0071555; P:cell wall organization; 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; 1.10.1760.20; -; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR011620; Sig_transdc_His_kinase_LytS_TM.
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; PF07694; 5TM-5TMR_LYT; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
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; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SEN55404.1};
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|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 68..92
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 104..120
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 126..144
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 156..178
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 323..544
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 563..680
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 704..820
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 858..949
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT COILED 816..843
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 613
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 753
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 897
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 952 AA; 106197 MW; F84B8D4FB2D011E2 CRC64;
MLRDLILNFA ILSVYLFFVS PFFIRDERSP KSTWKYKLTV GAVFGLLGII LLFFSINFSS
NAPLNMRGIA LMMASYFGGP LGATVELIVV YVGRLLKEGS IDPLQMAIGF SAAIGTGYLF
QRFKHYWSRW IIGSLFLLNY YYFALWLTNQ ISLETVWSYI ISQACYSLFI AAFLYYLIHN
HHNKKRIAQV EQDMISMLRM QPGLTFRFQR KHGTYYYNLA EGQLLKHLGL LPSMLFNKSF
AETSLFQDDF ADFLDQNYAR FSIDETISYE TTMAGTAVHV TLQPVIQNGQ LIDIIGNAIN
ITDLQKRKEA DDSNRAKSQF LAQMSHEIRT PINAIVGLNY ILQQSRLDNQ QRGYIDKIIT
AAKSLLAIVN DILDFSKIEA GKIVLEKVEF DLYEVLHNVS NMMSFKANEK GLRFHFFVHP
DVPQMLVGDP FRVLQIVLNL ANNAVKFTSQ GQITISVNRI SQRDQASMLA FTIRDTGIGM
NDEQLGSLFK EFTQADMTTT RKFGGTGLGL IISKNLAELM GGTIEVESKV GNGSCFTFTA
PFTAAAASAA SVQEVSPQLT FLRVLIICDD SQMQQVLRSQ LEQFQFVVST AESVDDALQN
IARGGMYDLI FLDWRLEGVN VLQLADTIHE TFTSPSQSII LISAYHESEL QMAAQSDSVA
KTLLHPISQS QLYNEIITLF RPHFSTKRST SDYSIQFASL KDATLLLVED NEINQLVAKE
LLREVGIEAD VASNGEIAVR YAKERRYDAI LMDLQMPVMD GYEATKAIRQ SAEGKTIPII
AMTADAMKGV EDQVLSIGMD GYLTKPFDPI DLYSMLQRVL KRTQELELAT EAAEAEVAAA
KAEPHLDQAT AAGRLGGNSA LYRQIIGLFI NKHALSLHEA REAFTAGDTK SAVLHVHTLK
GVASNIGADR LAALMAKLQA ALQADEHAEA SVLLLEAELE LQAVLLEASW IE
//
