ID T0V5P1_9STRE Unreviewed; 450 AA.
AC T0V5P1;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=HSISM1_1764 {ECO:0000313|EMBL:EQC77084.1};
OS Streptococcus sp. HSISM1.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1316408 {ECO:0000313|EMBL:EQC77084.1};
RN [1] {ECO:0000313|EMBL:EQC77084.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HSISM1 {ECO:0000313|EMBL:EQC77084.1};
RA Van den Bogert B., Boekhorst J., Herrmann R., Smid E.J., Zoetendal E.G.,
RA Kleerebezem M.;
RT "Comparative Genomics Analysis of Streptococcus Isolates from the Human
RT Small Intestine Reveals their Adaptation to a Highly Dynamic Ecosystem.";
RL PLoS ONE 8:E83418-E83418(2013).
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:EQC77084.1}.
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DR EMBL; ASKI01000058; EQC77084.1; -; Genomic_DNA.
DR AlphaFoldDB; T0V5P1; -.
DR PATRIC; fig|1316408.3.peg.1317; -.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000445_89_2_9; -.
DR Proteomes; UP000015933; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 1.10.8.500; HAMP domain in histidine kinase; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS 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; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; NF033093; HK_VicK; 1.
DR NCBIfam; TIGR00229; sensory_box; 1.
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 Pfam; PF00989; PAS; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 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 SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EQC77084.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
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..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 41..87
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 92..162
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 157..211
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 215..437
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 450 AA; 51084 MW; 060F3994394A55D0 CRC64;
MIDLIKQFVM SSNFVFVLIT VGFIIVVALL LLENRRDNIK LRQLNAKIKD LIAGDYSEVV
DMQGSPELTD MTNSINDLSE VIRLTHENLE QETKRLTSIL AYMTDGVLAT NRRGQIIMVN
EMAAKQLNVN PDEVLNTSIL DLLSIGDDYD LRSLITEVPE LTIDSQDENG EYLSLRVRFA
LIRRESGFIS GLVAVLHDTT EQDKEERERR LFVSNVSHEL RTPLTSVKSY LEALDDGALS
EPVAPDFVKV SLNETNRMMR MVTDLLSLSR IDNETSQLDI ELTNFTAFIT FILNRFDKIK
SQSQEDTKKY ELIREYPITP IWVEIDTDKM TQVIDNILNN AIKYSPDGGK IKVGMKTTDA
QLIISISDEG LGIPKKDLPR IFDRFYRVDK ARSRAQGGTG LGLAIAKEII KQHKGFIWAK
SEYGKGSTFT IVLPYDKDAI KDDWDTEEEE
//
