ID A0A089IJ58_9BACL Unreviewed; 1031 AA.
AC A0A089IJ58;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=H70737_06670 {ECO:0000313|EMBL:AIQ22563.1};
OS Paenibacillus sp. FSL H7-0737.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1536775 {ECO:0000313|EMBL:AIQ22563.1, ECO:0000313|Proteomes:UP000029519};
RN [1] {ECO:0000313|EMBL:AIQ22563.1, ECO:0000313|Proteomes:UP000029519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL H7-0737 {ECO:0000313|EMBL:AIQ22563.1,
RC ECO:0000313|Proteomes:UP000029519};
RA den Bakker H.C., Tsai Y.-C., Martin N., Korlach J., Wiedmann M.;
RT "Comparative genomics of the Paenibacillus odorifer group.";
RL Submitted (AUG-2014) 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; CP009279; AIQ22563.1; -; Genomic_DNA.
DR RefSeq; WP_042185731.1; NZ_CP009279.1.
DR AlphaFoldDB; A0A089IJ58; -.
DR KEGG; paej:H70737_06670; -.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG2972; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_011115_1_0_9; -.
DR Proteomes; UP000029519; 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; 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}; 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:UP000029519};
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 210..233
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 240..256
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 276..292
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 304..325
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 331..350
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 362..378
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 390..407
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 437..655
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 697..813
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 924..1023
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT MOD_RES 746
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1031 AA; 116557 MW; 73DE2756A2AE0BDB CRC64;
MTKRKLFLII VLFLTILTGF RFLWVWASPH AIQPQLVKGV LDLRNKDLNQ DKLLTLKGQW
EFYPNTLLPT FNKESLNKAP PKKYIQVPDQ WNDAIHNGEK SALGYGSYRL RILVDKNEKQ
SYGILISGVR TSSEIYINGE LLGNSGSPSA NKEDYVARVL PYSVTFTTDK TEIEIVIHVA
NYSLAHTGGI FKPILFGNEK TLTHQRIVSI GLQLLLCVVL LLHAVYAAIL YTIGPRQKML
IYFFLLVISA ITTVLIDDDK LLLHMLPLNY QWSLKLLIIS NIMAFIFILL TSKQLMFHNL
KIKSVRILTS LSLVHILFIL LGPVVHYYES YTLLFFINIF VLSLEVVVLF LKSALKNNDG
SIFLLLSILA IINSNHWGLF KNFDLVDVTY YPFDLIIAFL CFATFGFKRY FWNTKQTENL
AKSLQRTVTQ KDDFLANTSH ELKNPLHSII NIAETVLDSE RDSLMHQNAS NLELLITVGR
RMSLLINDLL DQSQLRESNI QLQLRNVPIQ SVAVGVLDML KFLTEGKHIT LISEIPDSFP
SIVADEKRLI QILFNLLQNA VKYTSVGSVR VHANIHKGVA RIHITDTGIG MNEETQLRAF
QPYEQGDSSV TAISGGIGLG LSICKQLVEL HGGEISVKSS LGKGSTFTFT MPLSDSNIQK
FNLEFSTVTE YTDKLSHISL SEFNTTSATS TDGRRPKILA VDDDPVNLKI LTSVLSIKDY
EMVTVTSGID ALIKLDTDQW DLIITDVMMP QMSGYELTQR IRERFTIAEL PILLLTARSQ
PEDIYTGFVS GANDYVMKPM NAMELRGRVR SLTDLKQSVN ERLRLEAAYL QAQIQPHFLF
NTLNSISALA SFDTQRMGHL IDAFSSYLRL SFNFLNAEPM IPIEHELELV RAYLYIEKER
FEDRMTINWE LTENLHFQLP PLTIQPLVEN AVRHGILSRS KGGTLSISIK ELADDIEITI
ADNGKGMTSE QLQQLLSSQS NVTRGIGFLN THKRLLRVYA KGLQIKSKEG LGTSVSFIIP
SEKRNMNHKN T
//
