ID I4C2I5_DESTA Unreviewed; 493 AA.
AC I4C2I5;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Desti_1060 {ECO:0000313|EMBL:AFM23776.1};
OS Desulfomonile tiedjei (strain ATCC 49306 / DSM 6799 / DCB-1).
OC Bacteria; Thermodesulfobacteriota; Desulfomonilia; Desulfomonilales;
OC Desulfomonilaceae; Desulfomonile.
OX NCBI_TaxID=706587 {ECO:0000313|EMBL:AFM23776.1, ECO:0000313|Proteomes:UP000006055};
RN [1] {ECO:0000313|Proteomes:UP000006055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49306 / DSM 6799 / DCB-1
RC {ECO:0000313|Proteomes:UP000006055};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Zeytun A.,
RA Lu M., Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Spring S., Schroeder M., Brambilla E.,
RA Klenk H.-P., Eisen J.A.;
RT "Complete sequence of chromosome of Desulfomonile tiedjei DSM 6799.";
RL Submitted (JUN-2012) 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};
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DR EMBL; CP003360; AFM23776.1; -; Genomic_DNA.
DR RefSeq; WP_014808929.1; NC_018025.1.
DR AlphaFoldDB; I4C2I5; -.
DR STRING; 706587.Desti_1060; -.
DR KEGG; dti:Desti_1060; -.
DR eggNOG; COG2770; Bacteria.
DR eggNOG; COG4251; Bacteria.
DR HOGENOM; CLU_000445_114_71_7; -.
DR OrthoDB; 5524356at2; -.
DR Proteomes; UP000006055; Chromosome.
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; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 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:AFM23776.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000006055};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 171..188
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 192..244
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 280..493
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 229..266
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 493 AA; 55819 MW; DE9C5B990B2670D3 CRC64;
MTIRRRLQVG SLLFAVFCLL IVGKVCLDAR YTEQALNELR LDAEIVRSAF DLQVLADQWL
SDPQEGSLLQ WNAKNATLAK LLRRISESGR TDSRSIDELH QDHSRIRTIF GDIVQIRQEN
EELSNPKMSR VEQDLKQMLN VKLQSMASKA SNTYRASESA VLITIRRSVD ALLVLLILML
LLIIGNWIQV HRAIIYPLGI LAHGAEIIGS GNLDHTVDIE SKDEVGKVAS SFNQMAANLK
KTISQVEQEI KERRQAQVAL QEQAAELARS NADLEQFAYA ASHDLQEPLR NISSCMQMLE
RWYRDSLGAE GKQLICYAVD SANRMKDLIN DLLVYSRVGA RVKEFRLTDT ARVFDSAAAN
LRLAIIESGA MITRDDLPRI LADDILLIQV FQNLLSNALK FRGRDDLQIH VSAKQRDSEW
VFSVQDNGIG IEPEFFERIF SIFQRLHTRA EYPGTGIGLA LTKRILDHHG GKIWVESEYG
KGSTFFFTIP DRR
//
