ID Q74AD2_GEOSL Unreviewed; 610 AA.
AC Q74AD2;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 113.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=GSU2444 {ECO:0000313|EMBL:AAR35817.1};
OS Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA).
OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC Geobacteraceae; Geobacter.
OX NCBI_TaxID=243231 {ECO:0000313|EMBL:AAR35817.1, ECO:0000313|Proteomes:UP000000577};
RN [1] {ECO:0000313|EMBL:AAR35817.1, ECO:0000313|Proteomes:UP000000577}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51573 / DSM 12127 / PCA
RC {ECO:0000313|Proteomes:UP000000577};
RX PubMed=14671304; DOI=10.1126/science.1088727;
RA Methe B.A., Nelson K.E., Eisen J.A., Paulsen I.T., Nelson W.,
RA Heidelberg J.F., Wu D., Wu M., Ward N., Beanan M.J., Dodson R.J.,
RA Madupu R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., Gwinn M.,
RA Kolonay J.F., Sullivan S.A., Haft D.H., Selengut J., Davidsen T.M.,
RA Zafar N., White O., Tran B., Romero C., Forberger H.A., Weidman J.,
RA Khouri H., Feldblyum T.V., Utterback T.R., Van Aken S.E., Lovley D.R.,
RA Fraser C.M.;
RT "Genome of Geobacter sulfurreducens: metal reduction in subsurface
RT environments.";
RL Science 302:1967-1969(2003).
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; AE017180; AAR35817.1; -; Genomic_DNA.
DR RefSeq; NP_953490.1; NC_002939.5.
DR RefSeq; WP_010943083.1; NC_002939.5.
DR AlphaFoldDB; Q74AD2; -.
DR SMR; Q74AD2; -.
DR STRING; 243231.GSU2444; -.
DR EnsemblBacteria; AAR35817; AAR35817; GSU2444.
DR KEGG; gsu:GSU2444; -.
DR PATRIC; fig|243231.5.peg.2471; -.
DR eggNOG; COG0834; Bacteria.
DR eggNOG; COG4251; Bacteria.
DR HOGENOM; CLU_000445_114_69_7; -.
DR InParanoid; Q74AD2; -.
DR OrthoDB; 5287570at2; -.
DR Proteomes; UP000000577; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000156; F:phosphorelay response regulator activity; IBA:GO_Central.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0030295; F:protein kinase activator activity; IBA:GO_Central.
DR GO; GO:0007234; P:osmosensory signaling via phosphorelay pathway; IBA:GO_Central.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd01007; PBP2_BvgS_HisK_like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
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 InterPro; IPR001638; Solute-binding_3/MltF_N.
DR PANTHER; PTHR42878:SF7; BACTERIOPHYTOCHROME; 1.
DR PANTHER; PTHR42878; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00497; SBP_bac_3; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00062; PBPb; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:AAR35817.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000000577};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000313|EMBL:AAR35817.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 283..307
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 395..609
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 311..356
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 610 AA; 68014 MW; 415CF20EF64CFBFF CRC64;
MAGRGYASRL SILSASALIL ALVVILAATG GSRAESGAVS LTPEERAWLN AHPVIKLAPD
PDFKPIEYFD ENGVYRGAAA DHIHALEKKL GITITIVHLR NWDEVMDAFK RHEVDLLGAV
AATPDRERYM LFSDPLVVVP GGIFSAREFG KPLAIKDLQG LKVAVVSNYM AHDYLRNTYP
QISLDIVPDV STGLAKASLG MVDVYVENMA NATFYLQEAG ITNLRLVGNT DFMYRWGIGI
RKDWPMMRQI LNKGLAALSE DEKSALIGRW IYVKAPPWRP SRAFVAGMVA SVAGVLLVAA
VSINLTLKRK VNARTAELQG ELAERRRLEQ ELTRLNEQLE ERVRERTAEL ERQVADRRRA
EEALQQLTVG LEQRVKARTA ELEASNRELE SFTFAVSHDL RAPVRHINGY VEILTEELAA
KECLCAGDYL ARIMVSCRRM QEMIDSLLDL SRISRKELQC EQVDLSEIAR QIMAEMREAE
PHRRVEATIA DGIRAKGDPV LLRSVIENLL HNAWKYTGRK DVAHIEFGVD TGGGETVYYV
RDDGAGFDAA YAGKLFTPFQ RLHTDAEFTG TGVGLATVQR IIHRHRGRVW AFSEPGRGAC
FFFTLNTETA
//
