ID A0A099SB74_9CLOT Unreviewed; 614 AA.
AC A0A099SB74;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=DP68_01310 {ECO:0000313|EMBL:KGK90092.1};
OS Clostridium sp. HMP27.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1487921 {ECO:0000313|EMBL:KGK90092.1, ECO:0000313|Proteomes:UP000030009};
RN [1] {ECO:0000313|EMBL:KGK90092.1, ECO:0000313|Proteomes:UP000030009}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMP27 {ECO:0000313|EMBL:KGK90092.1,
RC ECO:0000313|Proteomes:UP000030009};
RA Tan B.F., Foght J., Budwill K.;
RT "Draft genome sequence of Clostridium sp. HMP27 isolated from a coal
RT degrading methanogenic culture.";
RL Submitted (APR-2014) 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:KGK90092.1}.
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DR EMBL; JMFY01000002; KGK90092.1; -; Genomic_DNA.
DR RefSeq; WP_035305011.1; NZ_JMFY01000002.1.
DR AlphaFoldDB; A0A099SB74; -.
DR STRING; 1487921.DP68_01310; -.
DR eggNOG; COG5002; Bacteria.
DR Proteomes; UP000030009; 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 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; IPR024478; HlyB_4HB_MCP.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43711:SF32; DRUG SENSORY PROTEIN A; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF12729; 4HB_MCP_1; 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 SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000030009};
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 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 185..204
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 205..257
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 393..611
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 614 AA; 69524 MW; 27FCEC60EFA340DB CRC64;
MFKTLKFKMA MVYLILVSTT AIVGGISFLN IYTLNKSING LMVNNYKSIS ATANMLEVLN
EQNSQIYNYI YVNSTSSIDN IHKNINIFYL WYNLESNNIT EDSEKELVAR INNNYSTYLR
LFSQIQETKN LQGIEAASKY YNDNLLPIFN SLKKDLKQLS FINEKAMFKN KEVVTKDAHK
SLDTIIFLSV VSVLGGFILS RYSIKRTLKP IYSLRETMKA IKEGNLSQQA PIISEDEIGE
LTIEFNNMTD RIHKLEESNI GKLLTEKTKS DAIIKSISDP LIVLDSNYKI IRINMACEKF
FNIEEASSIN KYFLEVIRSG ELFDFIYNSS KLDSMNPSQK IIYFNIDEED YYFNIIVSIV
RDSEAKITGI IILLQNVTNL KQLEQIKSDF ISTISHEFKT PLTSIMIGAS LILDESIGSL
NESQHQIINT IQEDGEKLNT LVNNLLQLSK LECSESIFNI MPCSVTSLVN NAISDFCEQA
CSTKINLYYE SKENLPYINA DPEKISWVLN NLISNALKYT QAGGNIIITT FTKQNSMYVS
VSDTGSGIPE EYHEEIFNRF VQVRGENSDV KGTGLGLAIA KEIVKAHGGE IWCESKLGYG
SVFTFTLPLA VEKI
//
