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Database: UniProt
Entry: A0A239QV75_9MICO
LinkDB: A0A239QV75_9MICO
Original site: A0A239QV75_9MICO 
ID   A0A239QV75_9MICO        Unreviewed;       376 AA.
AC   A0A239QV75;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=SAMN06298212_11712 {ECO:0000313|EMBL:SNU01780.1};
OS   Ruaniaceae bacterium KH17.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Ruaniaceae.
OX   NCBI_TaxID=1945888 {ECO:0000313|EMBL:SNU01780.1, ECO:0000313|Proteomes:UP000214750};
RN   [1] {ECO:0000313|EMBL:SNU01780.1, ECO:0000313|Proteomes:UP000214750}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KH17 {ECO:0000313|EMBL:SNU01780.1,
RC   ECO:0000313|Proteomes:UP000214750};
RA   Sun Z.S., Albrecht U., Echele G., Lee C.C.;
RL   Submitted (JUL-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};
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DR   EMBL; FZQV01000017; SNU01780.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A239QV75; -.
DR   OrthoDB; 9806130at2; -.
DR   Proteomes; UP000214750; 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; cd00075; HATPase; 1.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 1.20.120.620; Backbone structure of the membrane domain of e. Coli histidine kinase receptor kdpd; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 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; IPR038318; KdpD_sf.
DR   InterPro; IPR025201; KdpD_TM.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR45569; SENSOR PROTEIN KDPD; 1.
DR   PANTHER; PTHR45569:SF1; SENSOR PROTEIN KDPD; 1.
DR   Pfam; PF13493; DUF4118; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 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   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000313|EMBL:SNU01780.1};
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:UP000214750};
KW   Transferase {ECO:0000313|EMBL:SNU01780.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        27..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        57..90
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        102..121
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          157..370
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   376 AA;  39856 MW;  00685DFF07E2CDBE CRC64;
     MAKDGAVAAV ALPRFQGALT ARRRWAGVGL VLVGAPLLAW LLSRVHDSST ITIEVLAFQL
     LIVVVALVGG IWPALLAAVL SALILDLFFI EPHLTVAVAD PVHVITLVFH IVIAVLVSYV
     VDRAAHETIE HLRLEETVSE IEPLAASDRA RASLLSALSH DIRRPLASAT AAVSGIRSAE
     DTLSLADRRE LLATAEESLA ALTHLVTDLL DVSRLEAGVM TISTMPCDPI DVIIPALDEL
     DVDPGAVELD LEHGSATMLA DPVLLQRAVV NLLANALRFS PVGSPVTVVT VVAGDRLEIR
     VIDHGPGIAL ERRDEVFVPF QRRGDVDNGS GLGLGLALSR GFVEVMHGSI EPRETPGGGL
     TMVVALPVGA RRGERR
//
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