ID U2D6D1_9FIRM Unreviewed; 469 AA.
AC U2D6D1;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=HMPREF1982_02926 {ECO:0000313|EMBL:ERI91883.1};
OS Clostridiales bacterium oral taxon 876 str. F0540.
OC Bacteria; Bacillota; Clostridia; Eubacteriales.
OX NCBI_TaxID=1321778 {ECO:0000313|EMBL:ERI91883.1, ECO:0000313|Proteomes:UP000016490};
RN [1] {ECO:0000313|EMBL:ERI91883.1, ECO:0000313|Proteomes:UP000016490}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0540 {ECO:0000313|EMBL:ERI91883.1,
RC ECO:0000313|Proteomes:UP000016490};
RA Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL Submitted (AUG-2013) 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:ERI91883.1}.
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DR EMBL; AWSZ01000058; ERI91883.1; -; Genomic_DNA.
DR AlphaFoldDB; U2D6D1; -.
DR STRING; 1321778.HMPREF1982_02926; -.
DR PATRIC; fig|1321778.3.peg.2890; -.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG3850; Bacteria.
DR HOGENOM; CLU_000445_89_6_9; -.
DR OrthoDB; 9786919at2; -.
DR Proteomes; UP000016490; 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:ERI91883.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000016490};
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 20..45
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 170..193
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 195..248
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 256..469
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 469 AA; 53657 MW; 0F04D8F8BB04FBC1 CRC64;
MSLKKIKDLL KSIKSTRISI KLTVIYAFMF SLVLLLLNAS ILFGVKYYLY NQANRQIDDM
QTIMSNKLSD QNGQVDLESK ELFSDVPPRE SISIRIVDRD GKILNSTFGF DNRFKLPNVN
GKKLKNNARH QEDKERHLVY KNVQVQNKNY GTVFMQIVKD MHNEYDFLKI LFAVMAVADF
LGVIAAIILG YMVSKRMLKP IDYITKTAEN ISINNLKERI EVKGPDDELK RLANTFNKMI
DRLQDAFNRQ TQFVSDASHE LRTPIAVIQG YANLLDRWGK DDRAALEKSI YGIKLEAGNM
ANLIEKLLFL AKGESGQKVV EKKEFYLNEL IDEVVKESRL IEESHNITNS SNVKVKILAD
YKMIKQLLRI FIENSLKFTS KEGTIDINSE ADDKEVRITV SDNGIGIPKD EIEKIFDRFY
TVDKSRSKEL GGTGLGLSIA KWIVNMHQGT IDVESEEGKW TKITVAFKL
//
