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Database: UniProt
Entry: D3EEZ1_GEOS4
LinkDB: D3EEZ1_GEOS4
Original site: D3EEZ1_GEOS4 
ID   D3EEZ1_GEOS4            Unreviewed;       450 AA.
AC   D3EEZ1;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=GYMC10_5977 {ECO:0000313|EMBL:ACX68182.1};
OS   Geobacillus sp. (strain Y412MC10).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=481743 {ECO:0000313|EMBL:ACX68182.1, ECO:0000313|Proteomes:UP000002381};
RN   [1] {ECO:0000313|Proteomes:UP000002381}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y412MC10 {ECO:0000313|Proteomes:UP000002381};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA   Brumm P., Mead D.;
RT   "Complete sequence of Geobacillus sp. Y412MC10.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACX68182.1, ECO:0000313|Proteomes:UP000002381}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y412MC10 {ECO:0000313|EMBL:ACX68182.1,
RC   ECO:0000313|Proteomes:UP000002381};
RX   PubMed=23408395; DOI=10.4056/sigs.2605792;
RA   Mead D.A., Lucas S., Copeland A., Lapidus A., Cheng J.F., Bruce D.C.,
RA   Goodwin L.A., Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C.S.,
RA   Tapia R., Land M., Hauser L.J., Chang Y.J., Kyrpides N.C., Ivanova N.N.,
RA   Ovchinnikova G., Woyke T., Brumm C., Hochstein R., Schoenfeld T., Brumm P.;
RT   "Complete Genome Sequence of Paenibacillus strain Y4.12MC10, a Novel
RT   Paenibacillus lautus strain Isolated from Obsidian Hot Spring in
RT   Yellowstone National Park.";
RL   Stand. Genomic Sci. 6:381-400(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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; CP001793; ACX68182.1; -; Genomic_DNA.
DR   RefSeq; WP_015737803.1; NZ_VEAV01000004.1.
DR   AlphaFoldDB; D3EEZ1; -.
DR   STRING; 481743.GYMC10_5977; -.
DR   KEGG; gym:GYMC10_5977; -.
DR   HOGENOM; CLU_000445_89_6_9; -.
DR   Proteomes; UP000002381; Chromosome.
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; cd00082; HisKA; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 6.10.340.10; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 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; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR45436:SF5; SENSOR HISTIDINE KINASE TRCS; 1.
DR   PANTHER; PTHR45436; SENSOR HISTIDINE KINASE YKOH; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ACX68182.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
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        7..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        152..170
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          177..231
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          239..450
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   450 AA;  50483 MW;  2C00B9CF75EE346F CRC64;
     MKLSSKIHLY SSVLMAAILI VMNLSVYYVF SKMTVDSQLE QAEAEAGSIV RSIAHSAATI
     PIDDLLRSYV PADGKIQFVP ADSKAKSPYV TSSGEDMDEL KLPYNANKQV EQIRYEGMRY
     VLVSLPVIWS DGAVYNIQIS RSLAATMETL QVLRIVLVAV TAIALVPVII STRILGRLIV
     QPITALIRTM REIRQSGRFR RIELKETSKD ELVEMGAAFN DMITLLESNH ARQEQFVSNA
     SHELKTPLTI IESYASLLKR RGLDRPELFM ESVEAIHSEA IRMKEMTEQL LLLARNQDQW
     QVEMEQVDLA ALSESSARAF RDAYNRTVEV EADGEVLGWT DSRRLKQLLF ILLDNARKYS
     DEHIVIQVGR KPSEVYIRVI DRGIGIAKEE LEHVFDRFYR VDEARTRRGG GAGLGLSLAK
     DIAEAISAEL ELESLPGVGT TATIRLQKSK
//
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