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Database: UniProt
Entry: A0A2A9EPT4_9MICO
LinkDB: A0A2A9EPT4_9MICO
Original site: A0A2A9EPT4_9MICO 
ID   A0A2A9EPT4_9MICO        Unreviewed;       463 AA.
AC   A0A2A9EPT4;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=ATJ97_2774 {ECO:0000313|EMBL:PFG40250.1};
OS   Georgenia soli.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Bogoriellaceae;
OC   Georgenia.
OX   NCBI_TaxID=638953 {ECO:0000313|EMBL:PFG40250.1, ECO:0000313|Proteomes:UP000222106};
RN   [1] {ECO:0000313|EMBL:PFG40250.1, ECO:0000313|Proteomes:UP000222106}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21838 {ECO:0000313|EMBL:PFG40250.1,
RC   ECO:0000313|Proteomes:UP000222106};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (OCT-2017) 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   -!- 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:PFG40250.1}.
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DR   EMBL; PDJI01000004; PFG40250.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A9EPT4; -.
DR   OrthoDB; 9786919at2; -.
DR   Proteomes; UP000222106; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd06225; HAMP; 1.
DR   CDD; cd00075; HATPase; 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; 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   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:PFG40250.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000222106};
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..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        155..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          176..229
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          237..447
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   463 AA;  49694 MW;  B99EAEC685321952 CRC64;
     MTGGRLSVRA TTTLAATAVV AVILAGAGAA LVLLVRQELV AGVDAMAQDR ALDIAVLQDG
     LVTTPGVRPV PYSGSLVQVL DDQGHVIAAS EGLKIGPMSR PVDEPHVRTR TLPVTPGRQY
     RVLAMPAGTS NHPRTVVVAQ SLRAANRAVS DTARMVAAVF PAVLVLTGLV TWLSVGRALA
     PVEEIRRKAA TIGAGDLSQR VPLPPARDEL YRLADTMNSM LARIQAATER RRHFVSDASH
     ELRTPLANMQ AMLEVAVARD EPDLWQETAA ALHTEQSRMA RLVDDLLLLA RLDGRAPRTE
     REVDLDDVVH DEAQWLRRTT DLQVEVEPLP ALRVLGDPSQ LARVLRNLTD NARRHARTTI
     SLSLRRHGGS AVVTVRDDGG GIAPEDRERV FDRFARLDEA RGRDQGGSGL GLAISREIAR
     AHGGELLVAD ATGPGGAVLE LRLPLLTEES EAASDDEHQA SLS
//
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