ID A0A0Q7J352_9BACL Unreviewed; 1251 AA.
AC A0A0Q7J352;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ASD40_18030 {ECO:0000313|EMBL:KQX45755.1};
OS Paenibacillus sp. Root444D2.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1736538 {ECO:0000313|EMBL:KQX45755.1, ECO:0000313|Proteomes:UP000051657};
RN [1] {ECO:0000313|EMBL:KQX45755.1, ECO:0000313|Proteomes:UP000051657}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root444D2 {ECO:0000313|EMBL:KQX45755.1,
RC ECO:0000313|Proteomes:UP000051657};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQX45755.1, ECO:0000313|Proteomes:UP000051657}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root444D2 {ECO:0000313|EMBL:KQX45755.1,
RC ECO:0000313|Proteomes:UP000051657};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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}.
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:KQX45755.1}.
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DR EMBL; LMEO01000051; KQX45755.1; -; Genomic_DNA.
DR RefSeq; WP_057307141.1; NZ_LMEO01000051.1.
DR AlphaFoldDB; A0A0Q7J352; -.
DR STRING; 1736538.ASD40_18030; -.
DR Proteomes; UP000051657; 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; cd06225; HAMP; 1.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR CDD; cd12914; PDC1_DGC_like; 1.
DR CDD; cd12912; PDC2_MCP_like; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 1.10.8.500; HAMP domain in histidine kinase; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 4.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR033479; dCache_1.
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; IPR036641; HPT_dom_sf.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF6; RESPONSE REGULATORY DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF02743; dCache_1; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF13426; PAS_9; 2.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 2.
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; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 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 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:UP000051657};
KW 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 275..298
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 300..353
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 440..492
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 489..559
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 631..852
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 866..983
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1009..1126
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1149..1248
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 915
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1059
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1188
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1251 AA; 140700 MW; 416EBA4E1307CA50 CRC64;
MSSSLRFKLV SLLVLITCIS LTVVGITNYR LSKDKLIHQM KEQSITSVTN SAQNLYDFLS
IRLAEVELIS RVDVMKHGTL EERLQFLTQE LKTGANRYHS MGIIDLNGYL TLTSGQTLYI
TGERRFQEAL NGKTFISDPE IGKLTGKYII SITAPVFNEK NEVTSIINIS LDAEQTFFEH
LHTPLEKGEI LIVNHEGLVL YHTDTPLILN LNIFTEYPSL VPAFQNALQT NEGFLDESFN
GGQKARWFYA RVPKLDWYLA YSVPLSAFEA PTSPLLWSTI GLIVMTAVVI FILIYLTANT
LIIKRIKQIL HVTESVAAGN FYIKPLIFKS KDELGALAHS VNGMIENLRE LFEPFEAFIH
HNQYAMIVTD PSFIVNHLNS RAVQLLGYSL AEVHKKATPL LWLDEEQLIE RAAQYSSELG
EYVPADCTAL VIRSLRHLKE DSEWIWHHKD GTRFFVQVSV SSITNPNGEL KGFVFIARDI
SDIKESNEFR ERLLTIVESA RDSILSFDEK GFIFYMNQAC KSTVGLDKQQ TVGKHFSEYV
DIQNDINFEE GLNTAIREGF WEFEAEVLTK EQRQIFISVI IVPHFPADKG ERYFSAITRD
ITDQVHSKEE LIRAKQEADE ANLAKGIFLA RMSHEIRTPL NGIVGLSYLM ERTHMSPLQR
DYISKIVRSS VSLSNIINDI LDFSKLEVDK LAIEHHAFQL DETIDRVCET LSVLLGHKPV
DFICDIHDNV PLGLIGDSLR MYQVLLNLTS NAIKFTEQGT VMLRVNVEQL REEEVRIGFT
VSDTGIGMDE EHLSKLFQPF VQVDEVTSRK FGGTGLGLVI SKNIIENMGG TIEVSSQPEL
GSEFRISLPF SLSLQPMKSQ AVLPLRALIV EDHPGLNQVL AHTLQSMCTE AAGVYSWKEA
RNAIDVIPVD VILLDMEAVD MYGEEVWLGM LEACNRMNIL TIIYTTLSGR DALEQLPAPS
APHAILVKPI SRIVLYQTLQ TLTGTHAEKE LISTTDFTQT AETMTKFQRI LLVEDNEINQ
TVARSLLESR LNCDVQLASN GFEALNDLEN NDYDLILMDI HMPVLDGIET TKRIRLEPKW
MHIPIIALTA DSTLEKRLDC IRAGMNEVIS KPIIPSRLFA AVDAVLSEKN RMAVPGLDIE
EALGRLSGKT EIYHEMLRKF HSQSAPIVAQ LTLAIQKGDY AEAINQLHAL RGSSSNLSAN
RVFAAATALE EMLEHHAGPD ESNASMIQNQ LQSVAIALEE VFHSIQKLLL D
//
