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Database: UniProt
Entry: I3E0D9_BACMT
LinkDB: I3E0D9_BACMT
Original site: I3E0D9_BACMT 
ID   I3E0D9_BACMT            Unreviewed;       734 AA.
AC   I3E0D9;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=PB1_06342 {ECO:0000313|EMBL:EIJ79960.1};
OS   Bacillus methanolicus PB1.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=997296 {ECO:0000313|EMBL:EIJ79960.1, ECO:0000313|Proteomes:UP000010523};
RN   [1] {ECO:0000313|EMBL:EIJ79960.1, ECO:0000313|Proteomes:UP000010523}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PB1 {ECO:0000313|EMBL:EIJ79960.1,
RC   ECO:0000313|Proteomes:UP000010523};
RX   PubMed=22610424; DOI=10.1128/AEM.00703-12;
RA   Heggeset T.M., Krog A., Balzer S., Wentzel A., Ellingsen T.E.,
RA   Brautaset T.;
RT   "Genome Sequence of Thermotolerant Bacillus methanolicus: Features and
RT   Regulation Related to Methylotrophy and Production of L-Lysine and L-
RT   Glutamate from Methanol.";
RL   Appl. Environ. Microbiol. 78:5170-5181(2012).
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:EIJ79960.1}.
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DR   EMBL; AFEU01000002; EIJ79960.1; -; Genomic_DNA.
DR   RefSeq; WP_003351366.1; NZ_AFEU01000002.1.
DR   AlphaFoldDB; I3E0D9; -.
DR   STRING; 997296.PB1_06342; -.
DR   PATRIC; fig|997296.3.peg.1351; -.
DR   eggNOG; COG4191; Bacteria.
DR   eggNOG; COG4585; Bacteria.
DR   OrthoDB; 9781904at2; -.
DR   Proteomes; UP000010523; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   CDD; cd16917; HATPase_UhpB-NarQ-NarX-like; 1.
DR   CDD; cd00130; PAS; 3.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 3.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013655; PAS_fold_3.
DR   InterPro; IPR011712; Sig_transdc_His_kin_sub3_dim/P.
DR   NCBIfam; TIGR00229; sensory_box; 3.
DR   PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF07730; HisKA_3; 1.
DR   Pfam; PF08447; PAS_3; 2.
DR   Pfam; PF13426; PAS_9; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00086; PAC; 3.
DR   SMART; SM00091; PAS; 3.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 3.
DR   PROSITE; PS50112; PAS; 3.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EIJ79960.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   DOMAIN          10..80
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          83..135
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          129..202
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          205..257
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          258..328
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          331..382
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          632..722
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          373..400
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   734 AA;  84954 MW;  995F7BFC5DCD5A7B CRC64;
     MNYDHDVINE DEKYKIVAEN TSDIIVLVDN EAIVRYVSPS FQQTLGYTIK EYEGMDAFDI
     IPPEDRDRVR SSHFQAIQTK TPVVLEYRLI HSQGSIIHVE ARVKPVLDRD GNVKYVVAVV
     RDITERKKTE QLLENILESV NAAVWSTEKD FSYYTFCSES IEKISGIPRR EIMFKPIRLH
     DHIHPDDNEM LMGEVKNSLD RGIPVNKVIR FIHVEGETRW GRLIVHPYMD NTGTIERFDG
     IILDITELKR SELALEESEQ RYKSLFENNL DGVFSIDLNG YFVNANQAFE KITGIKIDQL
     PDRCFIGLIY DEDHMSVYHI LSEVMKKQEP RDVECRIIRS GYGEKIVNIT FVPIFLSGEL
     NGVHGIVKDI TERKREEMEL IQSEERYKSL QQSINRFSND LANVMKVTEL ENRLIEEVKK
     VLPVNSVSIE ELPRGHESVL RNMNEIWIKI AEKEQPVYLR IEINQSLLKI EEEWLETAVH
     YVTILYDNLQ LIEDLMKRLE DMVTNNQTPK WMLKLLFKLS EKERALLSSD LHDSVLQDLI
     IWYRKLESLR SSTSFSEETH GKLIQIEEGL LDAIHQIRIT CNELRPPFLL KMGLVESLKS
     LFSYARMFSN YEIEFSSMNL ENPLHEDQIL GIYRIVQELL NNASKHSKAS KVTMKLTGYE
     EHIHFSYSDN GVGMDLSVFE GSFKHMGIAG IKNRVLSLEG EVEIKSAPQE GFHVNIIVPT
     TTPQKGDHYG NIIG
//
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