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Database: UniProt
Entry: A0A494XGM3_9BACL
LinkDB: A0A494XGM3_9BACL
Original site: A0A494XGM3_9BACL 
ID   A0A494XGM3_9BACL        Unreviewed;       798 AA.
AC   A0A494XGM3;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=D7Z26_18895 {ECO:0000313|EMBL:RKP49897.1};
OS   Cohnella endophytica.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Cohnella.
OX   NCBI_TaxID=2419778 {ECO:0000313|EMBL:RKP49897.1, ECO:0000313|Proteomes:UP000282076};
RN   [1] {ECO:0000313|EMBL:RKP49897.1, ECO:0000313|Proteomes:UP000282076}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M2MS4P-1 {ECO:0000313|EMBL:RKP49897.1,
RC   ECO:0000313|Proteomes:UP000282076};
RA   Tuo L.;
RT   "Cohnella sp. M2MS4P-1, whole genome shotgun sequence.";
RL   Submitted (OCT-2018) 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}.
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:RKP49897.1}.
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DR   EMBL; RBZM01000008; RKP49897.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A494XGM3; -.
DR   OrthoDB; 9806130at2; -.
DR   Proteomes; UP000282076; 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:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 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; 2.
DR   InterPro; IPR033479; dCache_1.
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; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013656; PAS_4.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR   PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF02743; dCache_1; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08448; PAS_4; 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   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
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:UP000282076};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   TRANSMEM        18..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        310..334
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        346..366
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          438..508
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          511..562
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          580..798
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   798 AA;  90611 MW;  2EDD5E00E694B353 CRC64;
     MKRTSLFQWV WKSLFKTIWI PLLVMGLFFI FLFFIANEWT RQENTRLDQE EANYSLLGQA
     LNEADIIDKQ LLSTAQVTEV YRKQTEKRLQ QPDHNDKEQR ERLKLSLEGD YHVYTDIAEG
     GAAIYIPANK PITTESIEKV LRLLPLEGLM EDIKFAYPLI EDMYFTNNES ISMIYPDDDG
     LDTSDLLDNM NALNAPGKQQ VKWTSPHMDS MGNGRLISSV APVYEGNSLE GIVGINITIE
     TFVNRIINLA VPWKGFGVLI DNTGKILSLP PHAEKLVGLN QFIEQDHFKS EIGTSDQGVQ
     KVSFAGRDHV VAWSTLADTG WKLILFTPIS AITANANEIS DKVSNAGYWI MGILILFYCI
     LFVIFYRRLK TLTRKIVTPL IQMKQTTINI GQGEYIQRQP SYPIQELHET AAQIVEMGKK
     MHRTMEQMEI VRLETEAAKN NLTSIVQSLD DVVFILNKQG VIVNIWSNDR NNLAAPMQQM
     IGKCFTEYVD EDLSKEYMNS LQKVFQSGQT GQVEYRVKTL RGWRWRLARL SPVIDSDGVQ
     RSVSVFSTDI TESKEMESSL RKAKEEAELA SKAKSEFLSS MSHELRTPMN AILGFAQLME
     YDEDYELSAE QKENVAEILK AGHHLLELIN DVLDLARIES GVISMELELI SVLSLVEDCL
     GMIEPMIKEK GITLTHHVTE DMASFEISAD RTRLKEILLN LLSNAVKYNK YKGSISIHYE
     RFDGYFKIHI SDTGYGIAPD KLDKIFDSFY RIKDNHVNVE GTGIGLPIAK QLIELMGGSI
     EVQSKLDEGS RFSIVIPF
//
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