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Database: UniProt
Entry: A0A1H8ALT6_9BACL
LinkDB: A0A1H8ALT6_9BACL
Original site: A0A1H8ALT6_9BACL 
ID   A0A1H8ALT6_9BACL        Unreviewed;       534 AA.
AC   A0A1H8ALT6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=SAMN05444955_101196 {ECO:0000313|EMBL:SEM70954.1};
OS   Lihuaxuella thermophila.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Thermoactinomycetaceae;
OC   Lihuaxuella.
OX   NCBI_TaxID=1173111 {ECO:0000313|EMBL:SEM70954.1, ECO:0000313|Proteomes:UP000199695};
RN   [1] {ECO:0000313|EMBL:SEM70954.1, ECO:0000313|Proteomes:UP000199695}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 46701 {ECO:0000313|EMBL:SEM70954.1,
RC   ECO:0000313|Proteomes:UP000199695};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; FOCQ01000001; SEM70954.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H8ALT6; -.
DR   STRING; 1173111.SAMN05444955_101196; -.
DR   OrthoDB; 9792686at2; -.
DR   Proteomes; UP000199695; 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:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd18773; PDC1_HK_sensor; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 2.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR033463; sCache_3.
DR   InterPro; IPR029151; Sensor-like_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR039506; SPOB_a.
DR   PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF17203; sCache_3_2; 1.
DR   Pfam; PF14689; SPOB_a; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00091; PAS; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   SUPFAM; SSF103190; Sensory domain-like; 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:0000313|EMBL:SEM70954.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00022989};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199695};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   DOMAIN          317..529
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   534 AA;  59040 MW;  CD7011161D39D251 CRC64;
     MRKKKKYIRL HSAIALFVCI VVILSLSVTG LLIAEEIADQ TKENLSEKAM DIAKIVGHSP
     LVIEALEGKR DQAEIQSFTS QIQHMTNVRF IVVMDMNGIR KSHPDPDKIG KRFVGRDEVN
     ALHGKEYISV ARGTLGTSLR AFEPIRNADG KQIGVVAVGI MLNHIEEAVA KSTRIVYIGI
     GFGIPVGILG ALVLARKIKT VLLGLEPFQI ASLFQERNAM LESVREGILG VDRDGRIVVA
     NTEAVRMFRK AGIYEDPIGK KAEDYLPGSG LPRVLKSGTS EYDQEQQLNG MVIVVNRVPI
     TVGNQVIGAV ATFRDKTELK QLAEQLTGVK MYAEALRVKT HEFMNKLHVI LGMVQIREYE
     KLSDYIRQIT DLYQMEVGSV TRLVKDPVLA GFLLSKLSYA REQGVKLNIS GECTLPSPAD
     PGIIHHLITI FGNLIDNGIE ALENNEKKEI DVSLGYDGSV FVLSVKDNGR GIPEELREKI
     FEKGFSTKGK NRGYGLFLVR KSVQELGGEL ALTSDAQSTT FTVKLPYEEK DENQ
//
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