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Database: UniProt
Entry: F9P1F3_STRMT
LinkDB: F9P1F3_STRMT
Original site: F9P1F3_STRMT 
ID   F9P1F3_STRMT            Unreviewed;       344 AA.
AC   F9P1F3;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=HMPREF9178_1182 {ECO:0000313|EMBL:EGR93907.1};
OS   Streptococcus mitis bv. 2 str. F0392.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=768726 {ECO:0000313|EMBL:EGR93907.1, ECO:0000313|Proteomes:UP000003771};
RN   [1] {ECO:0000313|EMBL:EGR93907.1, ECO:0000313|Proteomes:UP000003771}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0392 {ECO:0000313|EMBL:EGR93907.1,
RC   ECO:0000313|Proteomes:UP000003771};
RA   Durkin A.S., Kim M., Radune D., Hostetler J., Torralba M., Gillis M.,
RA   Methe B., Sutton G., 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:EGR93907.1}.
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DR   EMBL; AFUO01000001; EGR93907.1; -; Genomic_DNA.
DR   RefSeq; WP_000769397.1; NZ_AFUO01000001.1.
DR   AlphaFoldDB; F9P1F3; -.
DR   PATRIC; fig|768726.4.peg.1114; -.
DR   eggNOG; COG3850; Bacteria.
DR   eggNOG; COG5002; Bacteria.
DR   OrthoDB; 335833at2; -.
DR   Proteomes; UP000003771; 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; 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; PTHR45453; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR   PANTHER; PTHR45453:SF1; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 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:EGR93907.1};
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|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        38..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          59..111
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          126..344
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   344 AA;  38928 MW;  E21DEF6B1073A533 CRC64;
     MKLKNYILVG YLVSTLLTIL VVFWAVQRML IEKSEVYFLV GMTLIASFIG AAVSIFLLSP
     VFSSLKHLKK QAQDIASKDF STEIETKGPL EFQELGQAFN DMSHNLQATF QSLDESEQEK
     RMMIAQLSHD IKTPITSIQV TVEGILDGVI KEEERLHYLT TIGRQTERLN KLVEELDVLT
     LNTQPQDTAT EEVEEVFLDQ LLIESMSEFQ LQIEQEERDV YIQVSPESAK IKSHSDKLSR
     ILVNLLNNAF KYSEPGTRIE VLAQLTEQEL RISVKDEGQG ILPEDLEKIF KRLYRVETSR
     NMKTGGHGLG LAIARELAHQ LGGEITAESQ YGLGSKFTFS LNLK
//
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