ID E8WRT7_GEOS8 Unreviewed; 743 AA.
AC E8WRT7;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, 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=GM18_3880 {ECO:0000313|EMBL:ADW15302.1};
OS Geobacter sp. (strain M18).
OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC Geobacteraceae; Geobacter.
OX NCBI_TaxID=443143 {ECO:0000313|EMBL:ADW15302.1, ECO:0000313|Proteomes:UP000001442};
RN [1] {ECO:0000313|EMBL:ADW15302.1, ECO:0000313|Proteomes:UP000001442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M18 {ECO:0000313|EMBL:ADW15302.1,
RC ECO:0000313|Proteomes:UP000001442};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Chertkov O., Munk C., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Holmes D.,
RA Aklujkar M., Lovley D., Woyke T.;
RT "Complete sequence of Geobacter sp. M18.";
RL Submitted (JAN-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};
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DR EMBL; CP002479; ADW15302.1; -; Genomic_DNA.
DR AlphaFoldDB; E8WRT7; -.
DR STRING; 443143.GM18_3880; -.
DR KEGG; geb:GM18_3880; -.
DR eggNOG; COG2203; Bacteria.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_396795_0_0_7; -.
DR OrthoDB; 9769359at2; -.
DR Proteomes; UP000001442; Chromosome.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 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; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ADW15302.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000313|EMBL:ADW15302.1}.
FT DOMAIN 484..707
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 720..743
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 743 AA; 81358 MW; 7A47806BB0D269A9 CRC64;
MASPKPGGHL RRAPQPEFSV TSDEQPLYNS KIINTFVNLL KKKYPQVDVR ELLQYAEITP
YELSDEGHWL TQSQVDRFHA RMAQLVGGDI SREGGRYAAA QASLGVMAKY TLGLIGPANT
LLAIGKCAPN FSRSASYSAK KIADNRVEIT VTPHAGVEEK PYQCDNRVGF FEAIVMMFNY
QTPEIEHLDC IFKGGECCRY LVSWKKTLYA TVRGVRNRAI PLVLAIYALL QHYYQVGHLV
EVLTALTFFA LGSSYLAQRL ETQEILSTLS SVRESTEQMI ERIGVNYNNA RMVNEVGQAV
SKQSSINEVL GNVIKVIEKR LGYDRGAILL ADAKKSRLTF STGFGYTEKQ LEALLKTSFD
LADPMAQGVF VACFRERQSR FVSDFAEVAH LHTPQSIAFS QELEAQSFIC CPIVCDGEAL
GILAVDNKKS QRPLTQSDLS LLTGIAPVIG MSLRNAIYLE RERRMSEQIR QSQKMESVGV
LAGGIAHDFN NLLTGMMGFV ELAQMKLNKD DQAQVFLEQV LSAAERAASL TRGLLAFSRK
QINHPQPVNL NQIVDNLRKL LSPLVIPQVG LIIDLYREKL PVVADSSQLD QLITNLVTNA
RDAMPEGGEL TIRTGLMEMT EEWVDAHGYG AVGGYAKMSV TDTGAGMDEA TKAHILEPFF
TTKEVGKGSG LGLAIVYGIV KQHEGYLEID SKPGVGTTFN VYLPLLVGTA AAGVPALQSS
AAHAPSGTGP GAFSHPESRP TSP
//
