ID A5GDW3_GEOUR Unreviewed; 726 AA.
AC A5GDW3;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Gura_0011 {ECO:0000313|EMBL:ABQ24229.1};
OS Geotalea uraniireducens (strain Rf4) (Geobacter uraniireducens).
OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC Geobacteraceae; Geotalea.
OX NCBI_TaxID=351605 {ECO:0000313|EMBL:ABQ24229.1, ECO:0000313|Proteomes:UP000006695};
RN [1] {ECO:0000313|EMBL:ABQ24229.1, ECO:0000313|Proteomes:UP000006695}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rf4 {ECO:0000313|EMBL:ABQ24229.1,
RC ECO:0000313|Proteomes:UP000006695};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Shelobolina E., Aklujkar M.,
RA Lovley D., Richardson P.;
RT "Complete sequence of Geobacter uraniireducens Rf4.";
RL Submitted (MAY-2007) 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; CP000698; ABQ24229.1; -; Genomic_DNA.
DR RefSeq; WP_011936958.1; NC_009483.1.
DR AlphaFoldDB; A5GDW3; -.
DR STRING; 351605.Gura_0011; -.
DR KEGG; gur:Gura_0011; -.
DR HOGENOM; CLU_000445_114_51_7; -.
DR OrthoDB; 5522808at2; -.
DR Proteomes; UP000006695; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd00156; REC; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 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; IPR011006; CheY-like_superfamily.
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; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43711:SF31; SENSOR HISTIDINE KINASE GRAS; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF13492; GAF_3; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF55781; GAF 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; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ABQ24229.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000006695};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABQ24229.1}.
FT DOMAIN 6..122
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 466..718
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 422..459
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 57
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 726 AA; 81646 MW; 6ABA1C6716E3EC33 CRC64;
MKRQLRVLLV EDSQDDMLLL LRELKNGGFE PIHELVETAA AMKCALVEKT WDMVISDYRM
PQFDAPGALK VLHESGLDLP FIIVSGKIGE DLAVAAMKSG AHDYLMKGNL SRLVPAVDRE
LREAAERRKH RLAEEAIRQG KMQWEAAFDS VSDLIILTDF NGKIVRCNKR VTTYFHCQYA
SMIGKNIGEL FYGGEEIASR VFQFPHKFHA EAEEDIVFPM LTGWYNVSSY PMHAEEEESQ
GVVFIIKDIT KRKRVEEEKR IIDRELLTLY AIAFRLNSKQ SLEKIMSDLL FQLHNMLRID
FSCIHLLEKG VLKLKASLGL DLELETSLKT LSTTFPWVSN MLKGKLVKTK TPTGHLPADV
AQAALKVGVQ AWCTIPLKIG PDVIGVTMVA SQSNKGFTDR EVFLLTSIAN QLAVLIENYT
LYDQMKEKAE ELQRSKKALK ENLLEVKRAN IELDRLNVAK NNFIGMASHE LKTPITSIMG
GVQFLHKYSG LQMTPEQESI LNSVYEGTVQ LRKLVEDLLS ISRIEAQGII PQKKPFKLVT
LCREVYETFT LPLSRRQISV EISGDELLVP VDESLSSLAM RNLIENAIKF TPDGGSITIS
GRLVEKWEVL NYAKIVRPFY PAFPKNLPAG NNSFYLLDFI DSGIGIPLEE RVRIFEKFYG
VGDIAYHSSG TFDFMSKGSG LGLSIVRGVM DAHRGMVWTT PGSDGTGSVF TLLFPMDKSS
EMKVSR
//
