ID D4KK11_9FIRM Unreviewed; 465 AA.
AC D4KK11;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ROI_39450 {ECO:0000313|EMBL:CBL10691.1};
OS Roseburia intestinalis M50/1.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Roseburia.
OX NCBI_TaxID=657315 {ECO:0000313|EMBL:CBL10691.1, ECO:0000313|Proteomes:UP000008807};
RN [1] {ECO:0000313|EMBL:CBL10691.1, ECO:0000313|Proteomes:UP000008807}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M50/1 {ECO:0000313|EMBL:CBL10691.1,
RC ECO:0000313|Proteomes:UP000008807};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT "The genome sequence of Roseburia intestinalis M50/1.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBL10691.1, ECO:0000313|Proteomes:UP000008807}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M50/1 {ECO:0000313|EMBL:CBL10691.1,
RC ECO:0000313|Proteomes:UP000008807};
RA Pajon A.;
RL Submitted (MAR-2010) 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; FP929049; CBL10691.1; -; Genomic_DNA.
DR AlphaFoldDB; D4KK11; -.
DR KEGG; rim:ROI_39450; -.
DR PATRIC; fig|657315.3.peg.1169; -.
DR HOGENOM; CLU_000445_89_26_9; -.
DR Proteomes; UP000008807; Chromosome.
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; 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 PANTHER; PTHR45453; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR PANTHER; PTHR45453:SF1; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:CBL10691.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Transferase {ECO:0000313|EMBL:CBL10691.1};
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..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 162..181
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 247..465
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 465 AA; 51944 MW; 339D4938BD90A55D CRC64;
MKSVPKLIRR FVGILLLSSI LIVLINFIVF VVLMASYVPD KDASPYNIAR ETGKALQLST
GGNYVLSENM SAKLTDCGAW AILVDNNTLN VTWKTENVPS TIPNDYTLSD IANLSVGYLD
GYPTYTGENE YGVVVLGFPK DSFWKHTQPS WDYSLLSNFP QIVLNVLFIN IMLILAIYLI
ANMKLLKSVK PITKGIQGLS IGENVHIPET GVLSEISVNI NHTSDILQEQ KKQLIKKETA
RANWIAGVSH DIRTPLSMVM GYAGQLENSP SLSETERKKA TVIVKQSERM KNLINDLNLA
SKLEYNMQPI MKKEENAVAV VRQVVVDFMN MDIDDRFPIK WKTDDKLTVC NINADKDLLK
RAISNLIQNS ITHNENGCAI YVSVSTYNNK CIICVEDNGI GVSDEQIEKL NHTPHYMVCD
TNTTEQRHGL GLLIVKQIMD GHSGTVIIDH SEYYGGFKTE LTIPL
//