ID A0A1Y5KGR1_9BACL Unreviewed; 1030 AA.
AC A0A1Y5KGR1;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-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=B1748_03460 {ECO:0000313|EMBL:OUS77846.1};
OS Paenibacillus sp. MY03.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=302980 {ECO:0000313|EMBL:OUS77846.1, ECO:0000313|Proteomes:UP000195591};
RN [1] {ECO:0000313|EMBL:OUS77846.1, ECO:0000313|Proteomes:UP000195591}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MY03 {ECO:0000313|EMBL:OUS77846.1,
RC ECO:0000313|Proteomes:UP000195591};
RA Liu H., Cheng Y., Gu J.Y., Han W.J.;
RT "Draft genome of a polysaccharide-degrading bacterium Paenibacillus sp.
RT MY03.";
RL Submitted (MAR-2017) 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 -!- 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:OUS77846.1}.
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DR EMBL; MXQD01000004; OUS77846.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y5KGR1; -.
DR OrthoDB; 9809348at2; -.
DR Proteomes; UP000195591; 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; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 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; 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; 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:UP000195591};
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 17..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 218..237
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 249..266
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 286..307
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 314..333
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 339..359
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 371..387
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 447..670
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 702..819
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 840..1026
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT MOD_RES 752
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1030 AA; 115054 MW; B08681B78F6D69FF CRC64;
MELEDWSRMA YMYNKHIVLF GMIVIFGLVN IFSVYQWLSP SDRKIEAVDG LLDARGWSFA
DDGVLELRGE WELYENMLLG PDDFRADAAR LESSREVVQV PGSLKKMFTS GYNNGHGAAT
YRLLLQVNET GIYSLRANKI RLSSRIYING FDIGGNGNPS MAAEQFVPSN APFFGSVMLE
QGVAEIIIQV ASYDYLGGGV VQAPDFGFTN DVKAQLDAAR LADMTLITIM LAFGLYYAGM
FRQWGKERYL MHFCLFCLST GLFFGIDNEI LAMILFPELP FSLLQKLIFI LSLFAFYFFA
TYVHNYLGQQ KNVVFVWLSR FAYVFLALII VLPNRYLTST LWLAIPVQFA VFATIVYSVF
RSRSRGVHGS YYTLLGVFFL IVTWLFAQLR YQLALDNPFY MIVTPLLLVL SQALLMSERL
QENFRKSTQL AEQLLIYDRQ KDDFLVKTSH ELRTPLHGII NLSQSLLDNR DRPLQDDHRD
NIRLLHLMGR RLAGIVHDIL DMNRIKHGQL LIHPTSVNLG NSVQFVMETL SIAPVNKEVR
LVNGLPNELP LVIADENRLK QILHNLLENG LNFTESGTVS IAAKRKDDLL VVTVTDTGIG
IPAQALAEIF QPFVKYEDEG KDPVRRSFGI GLGMGLGITK QLVELHGGKL HVESTVGRGS
TFSFTLPIDK QSEEAAAAME GEPSAIDMMS GVSQGDLEAQ FHVLIVDDEP SNIKVLIDAV
TSLRYGYTAV NSGEEALEAL RGSPKPDLIL LDLMLTGISG REVCRAIRST QGLAELPVLM
LTASGQTGDI VASFAAGAND IVQKPFELAE LKARMQSLLA MKSSSENAIR REMDFLQAQI
TPHFLYNTLN SLVGLSYKDT DKLRETINHL TTYLRSKFTF VFDSEMVALS RELELVKAYT
AIEQLRFGQR LQIHYEADEK LHCMMPPLTL QPIVENAVRH GIGQKPSGGT VQIAVRRIGA
AIEIVVEDDG VGMSEDKLHM LEQGKSGGIG ISNVNRRLQM LYGHRLDISS SEGHGTRVKL
EIPCSAISDE
//
