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Database: UniProt
Entry: A0A3D9IA23_9BACL
LinkDB: A0A3D9IA23_9BACL
Original site: A0A3D9IA23_9BACL 
ID   A0A3D9IA23_9BACL        Unreviewed;       621 AA.
AC   A0A3D9IA23;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=DFP95_1088 {ECO:0000313|EMBL:RED58485.1};
OS   Cohnella lupini.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Cohnella.
OX   NCBI_TaxID=1294267 {ECO:0000313|EMBL:RED58485.1, ECO:0000313|Proteomes:UP000256869};
RN   [1] {ECO:0000313|EMBL:RED58485.1, ECO:0000313|Proteomes:UP000256869}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 8236 {ECO:0000313|EMBL:RED58485.1,
RC   ECO:0000313|Proteomes:UP000256869};
RA   Whitman W.;
RT   "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT   soil and plant-associated and newly described type strains.";
RL   Submitted (JUL-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:RED58485.1}.
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DR   EMBL; QRDY01000008; RED58485.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3D9IA23; -.
DR   Proteomes; UP000256869; 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; cd12912; PDC2_MCP_like; 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; IPR033479; dCache_1.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR029151; Sensor-like_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR010559; Sig_transdc_His_kin_internal.
DR   PANTHER; PTHR34220; SENSOR HISTIDINE KINASE YPDA; 1.
DR   PANTHER; PTHR34220:SF7; SENSOR HISTIDINE KINASE YPDA; 1.
DR   Pfam; PF02743; dCache_1; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF06580; His_kinase; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 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:RED58485.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000256869};
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        36..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        327..346
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          508..619
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   621 AA;  69800 MW;  B7F30C123B1AACF4 CRC64;
     MTPMRKAHED ASHRSDYGIG SVRRLLHRFS IPRPWLLAYL LLIVVPAAVF LYGYYERSAS
     ILKNEVMRTM QQALKQAGSN LSYRLEHIQD ISNAAFMNSN LHSYLSVGAD DQSIAIQLKV
     IEDLRYLVDT VQSNSDVYHV RLFVDKSKLY AQERINFFTL DSLQARPWYP AIIGGNGGIV
     WTGIYHESFL GEGDANIFSA ARMLRDPENY DKVSGVLMID VQESLVSDIL SALQFSPGTQ
     VYLVDESGTI VYHPDRSLIG TKVDRSIFDV LRQGDEGIRT LKQNSDANNV MYTTLNPTGW
     KLVAQGTESQ LSPQSVKLTQ RSEWTSLIEY VTLFLILPFV LLAIIVRGMN RRVNHVITVI
     RKEGTDSLND LPAASGDFHM LERSVDHLII RVRTLVEEKY KAELHEREAQ LQALQAQINP
     HFLYNTLDTI NWIAIGKGAT DISQMIDSLA KYFRLSLNKG QSIVSVEDEL RLAQVYLEIQ
     QSRFLDTFDF KLEIQEGLDA YRMPKLILQP IVENALLHGI RKAKDRRGLI VISAKEDKGD
     LFFAVSDNGI GMEESLASRL LTEAPTESAN RGSSDSGSSY GLFNVNERIK LYSGENYGVG
     IDSRLGVGTT VTVRLKAGFS E
//
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