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Database: UniProt
Entry: A0A3B0CIG5_9BACL
LinkDB: A0A3B0CIG5_9BACL
Original site: A0A3B0CIG5_9BACL 
ID   A0A3B0CIG5_9BACL        Unreviewed;       605 AA.
AC   A0A3B0CIG5;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   18-JUN-2025, entry version 31.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=D7M11_11535 {ECO:0000313|EMBL:RKN84820.1};
OS   Paenibacillus ginsengarvi.
OC   Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Paenibacillaceae;
OC   Paenibacillus.
OX   NCBI_TaxID=400777 {ECO:0000313|EMBL:RKN84820.1, ECO:0000313|Proteomes:UP000282311};
RN   [1] {ECO:0000313|EMBL:RKN84820.1, ECO:0000313|Proteomes:UP000282311}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 13059 {ECO:0000313|EMBL:RKN84820.1,
RC   ECO:0000313|Proteomes:UP000282311};
RX   PubMed=17684262; DOI=10.1099/ijs.0.64906-0;
RA   Yoon M.H., Ten L.N., Im W.T.;
RT   "Paenibacillus ginsengarvi sp. nov., isolated from soil from ginseng
RT   cultivation.";
RL   Int. J. Syst. Evol. Microbiol. 57:1810-1814(2007).
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: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
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:RKN84820.1}.
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DR   EMBL; RBAH01000007; RKN84820.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3B0CIG5; -.
DR   OrthoDB; 9813151at2; -.
DR   Proteomes; UP000282311; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000156; F:phosphorelay response regulator activity; IEA:TreeGrafter.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0030295; F:protein kinase activator activity; IEA:TreeGrafter.
DR   GO; GO:0007234; P:osmosensory signaling via phosphorelay pathway; IEA:TreeGrafter.
DR   CDD; cd06225; HAMP; 1.
DR   CDD; cd00075; HATPase; 1.
DR   CDD; cd00082; HisKA; 1.
DR   FunFam; 3.30.565.10:FF:000006; Sensor histidine kinase WalK; 1.
DR   FunFam; 1.10.287.130:FF:000001; Two-component sensor histidine kinase; 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   Gene3D; 3.30.450.20; PAS domain; 1.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR003661; HisK_dim/P_dom.
DR   InterPro; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR041328; HisK_sensor.
DR   InterPro; IPR052545; Light-responsive_reg.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR42878:SF3; HISTIDINE PROTEIN KINASE SAES; 1.
DR   PANTHER; PTHR42878; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF18698; HisK_sensor; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
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; SSF158472; HAMP domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000282311};
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        12..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        176..195
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          197..249
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          378..602
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          237..268
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   605 AA;  67531 MW;  ECF4473E7A227F4E CRC64;
     MWTWKSVVGK LWMTIIGLVA VVLVINGIFM GQFLDTNFAN SKDQERSLQK LASKVSADLT
     LHRDEFLYVN AVAELLDAQD AAMIVLNDKL DEMIPASKVT QIPKLNALSL FEPDQLRQVL
     GGSTRPSIYF DGQSGRRFLA VAVPQYEADK SRAIGVVILY QAQIALDYTQ AYFQNLFVIA
     GIIGFLLTTL FAFFLSSRIT QPLLQMKKAA DFITLGEYKT RVPVTSSDEI GQLAVAINQM
     TERLDHTINA LNQEKEHLSS VLRSMTDAVI TLDADGCVVL TNPQGEKLVK EWHEIGWEDS
     SGDHSGKMRA PDPLQPLFED VVKSNRDIAS TIRVRSSVYS VVMAPLYSIE GLRGTVAVLR
     DVTEEHRLDK LRKDFVANVS HELRTPLSML QGYSEALLDD IAATPEERRE LAQVIHDESL
     RMGRLVKDLL DLARMEAGHM EMSFREFELE PLLQRVHRKF GALCKERGIS LKLNVHPIDI
     TMRHADEDRL EQVLTNLLDN AIRHTPEGAW VEIRVNTQME QQGETVVIEI ADGGRGIPPE
     DLPFIFERFY KADKARTRGS SGGTGLGLAI VKNIVDAHQA TIGAQSELGQ GTTFTIQLPN
     RARSV
//
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