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Database: UniProt
Entry: F9PJG9_9ACTO
LinkDB: F9PJG9_9ACTO
Original site: F9PJG9_9ACTO 
ID   F9PJG9_9ACTO            Unreviewed;       509 AA.
AC   F9PJG9;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=HMPREF9058_2085 {ECO:0000313|EMBL:EGV14006.1};
OS   Actinomyces sp. oral taxon 175 str. F0384.
OC   Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC   Actinomyces.
OX   NCBI_TaxID=944560 {ECO:0000313|EMBL:EGV14006.1, ECO:0000313|Proteomes:UP000004281};
RN   [1] {ECO:0000313|EMBL:EGV14006.1, ECO:0000313|Proteomes:UP000004281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0384 {ECO:0000313|EMBL:EGV14006.1,
RC   ECO:0000313|Proteomes:UP000004281};
RA   Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA   Nelson K.E.;
RL   Submitted (JUL-2011) 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:EGV14006.1}.
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DR   EMBL; AFUR01000001; EGV14006.1; -; Genomic_DNA.
DR   RefSeq; WP_009406108.1; NZ_AFUR01000001.1.
DR   AlphaFoldDB; F9PJG9; -.
DR   eggNOG; COG5002; Bacteria.
DR   Proteomes; UP000004281; 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:EGV14006.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
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        16..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        184..206
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          207..259
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          267..476
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   REGION          482..509
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   509 AA;  55114 MW;  28D2B7D02C78E872 CRC64;
     MTSLLPTRTV TIRTRVMWAI VLVAGIALVM CGTIVWTLGL SSVSADATNR LEHSRDRIRQ
     LAADRQDPSS GQPLEDVSAV LRTHIQRTAE GRGEAELGFV GTDASTKLTW VSADSVSFRP
     EQDKELLTRV SSQAAASESV IETVRTPTSS YRVLVVPLQG GAQRGALVHV IDLKVAESQL
     RRTMAFYAAA AVFTVALVTG LAWFAVERLL RPIEQLRRAT ESIGEEDLTT RVPVKGRDDL
     TALAAAVNRM LDRVQTSVEA QRNLLDDVGH ELRTPIAVVR GHLELTDPAD PEDVRQTQLL
     ALDELDRMGM LVGDLILLAK SVQSDFVTPV DTDVAELTEL VFDKSLALGE RRWKMESAAF
     TRAMVDPTRI TQAWLQLVAN AVRYSEHCST VSLGSAVRDG HLQMWVRDEG IGIAPEDIDL
     VRQRFKRTAG AQKLASGTGL GLSIVETIVA AHGGRLDILS EVGRGSVFTM VIPLRPPAAV
     ASSRGDALTP AGDSLPAQPP TASRRSHSP
//
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