ID K6U5I6_9CLOT Unreviewed; 505 AA.
AC K6U5I6;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=A370_02138 {ECO:0000313|EMBL:EKQ56247.1};
OS Clostridium sp. Maddingley MBC34-26.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1196322 {ECO:0000313|EMBL:EKQ56247.1, ECO:0000313|Proteomes:UP000001325};
RN [1] {ECO:0000313|EMBL:EKQ56247.1, ECO:0000313|Proteomes:UP000001325}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Maddingley MBC34-26 {ECO:0000313|Proteomes:UP000001325};
RX PubMed=23405323;
RA Rosewarne C.P., Greenfield P., Li D., Tran-Dinh N., Bradbury M.I.,
RA Midgley D.J., Hendry P.;
RT "Draft Genome Sequence of Clostridium sp. Maddingley, Isolated from Coal-
RT Seam Gas Formation Water.";
RL Genome Announc. 1:E00081-12(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:EKQ56247.1}.
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DR EMBL; ALXI01000075; EKQ56247.1; -; Genomic_DNA.
DR AlphaFoldDB; K6U5I6; -.
DR STRING; 1196322.A370_02138; -.
DR PATRIC; fig|1196322.3.peg.2075; -.
DR eggNOG; COG5002; Bacteria.
DR Proteomes; UP000001325; 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:SF3; HISTIDINE KINASE; 1.
DR PANTHER; PTHR45453; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EKQ56247.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001325};
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 178..197
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 199..251
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 280..497
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 239..270
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 505 AA; 57809 MW; 208325946FCDCAF4 CRC64;
MKRSLSKRLF GITLSLVIAL MLLTYFAQAF FFENFYSYKK TISLVKEVNK FNDLYSLHID
SDADLYKALQ KFENDNNAQI IIFQNGKIMY ASNTIYGNQE SYDSFTSSAS ELINDKDLIN
QAITYSQPRY KNFENESTGL RKIGVVSPMS LNNKNDSLIF CIASIQPIKE ASEVISEFFL
YLFFGLIIVS IILALIYSNL ISKPLVNLTL AANKISKMNF TEVCETDRED EIGSLAKSLN
FLSKNLQTAL LDLQQKNKKL ELDIEKERQL EDMRKDFISN VSHELKTPIG IIEGYAEGLK
DGIVSGEDAN MYLETIIDES KKMSVLVTNM LELSKLESGT IKPNFEAFNI NRLIKKILKK
HSIDFEENKF NVSFNSSTPY SYVYADPFQM EQVLTNIITN AIKYTPPNNN INISIEEGLD
KFKISVQNMG VTIPDEEISK LFDKFYRLDK SRERTQKNST GIGLSIVKNI LHLHNSEFNL
QNINGGVEFY FYLEKIVSPE EQEEF
//
