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Database: UniProt
Entry: F9VCM4_LACGL
LinkDB: F9VCM4_LACGL
Original site: F9VCM4_LACGL 
ID   F9VCM4_LACGL            Unreviewed;       461 AA.
AC   F9VCM4;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=LCGL_0615 {ECO:0000313|EMBL:BAK60075.1};
OS   Lactococcus garvieae (strain Lg2) (Enterococcus seriolicida).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=420890 {ECO:0000313|EMBL:BAK60075.1, ECO:0000313|Proteomes:UP000008520};
RN   [1] {ECO:0000313|EMBL:BAK60075.1, ECO:0000313|Proteomes:UP000008520}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lg2 {ECO:0000313|EMBL:BAK60075.1,
RC   ECO:0000313|Proteomes:UP000008520};
RX   PubMed=21829716; DOI=10.1371/journal.pone.0023184;
RA   Morita H., Toh H., Oshima K., Yoshizaki M., Kawanishi M., Nakaya K.,
RA   Suzuki T., Miyauchi E., Ishii Y., Tanabe S., Murakami M., Hattori M.;
RT   "Complete genome sequence and comparative analysis of the fish pathogen
RT   Lactococcus garvieae.";
RL   PLoS ONE 6:E23184-E23184(2011).
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; AP009333; BAK60075.1; -; Genomic_DNA.
DR   RefSeq; WP_014024478.1; NC_017490.1.
DR   AlphaFoldDB; F9VCM4; -.
DR   STRING; 420890.LCGL_0615; -.
DR   KEGG; lgv:LCGL_0615; -.
DR   PATRIC; fig|420890.5.peg.613; -.
DR   eggNOG; COG2205; Bacteria.
DR   HOGENOM; CLU_000445_89_6_9; -.
DR   Proteomes; UP000008520; Chromosome.
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; PTHR45528; SENSOR HISTIDINE KINASE CPXA; 1.
DR   PANTHER; PTHR45528:SF9; SENSOR HISTIDINE KINASE YRKQ; 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; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:BAK60075.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008520};
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        12..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        166..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          188..240
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          248..453
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   461 AA;  51793 MW;  2E116957B43BB5D6 CRC64;
     MIRRKPLSIK TRLLLTNIGF VFFAFLWIIL IFNILINSYI SNSASRQLSQ VRIYQAQVTP
     PSGSTSADLE DAPRGSFNTH PVAFNINDNY EVQDLEKVGN FERDTANNIA QALKNQKVPL
     SKVKNYRLDT SGSTFYIETI RQSSGLYQVL YVDITGIINF TNSVNLFLVS VALAVIVILS
     LAVTFVTQRL IKPLSILAKF ATRIGQGDFT EYQGSFQDRE LATLAHNMNV AARQLDHNDK
     NQKLFFQNAS HELRTPLMAI KSYAEGISYE VMDPKKASET ILYETDRMSE LVEDLLTLSR
     LDSLSVHQEL VYQDVRLIMK DIAKEQEIFA EQKGIKLTTV FDKKAVMLTC DYKALRRAIS
     NLVSNAMRYV ETEIVLTCTK KDGAVMISVA NDGSGIDPET LPHIFERFYK GAGGVHGIGL
     AIVQTIVEQH QGQVSVESDE HQTMFTMTFA KMSKKALEKK A
//
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