ID B9M5H4_GEODF Unreviewed; 427 AA.
AC B9M5H4;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Geob_3390 {ECO:0000313|EMBL:ACM21733.1};
OS Geotalea daltonii (strain DSM 22248 / JCM 15807 / FRC-32) (Geobacter
OS daltonii).
OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC Geobacteraceae; Geotalea.
OX NCBI_TaxID=316067 {ECO:0000313|EMBL:ACM21733.1, ECO:0000313|Proteomes:UP000007721};
RN [1] {ECO:0000313|EMBL:ACM21733.1, ECO:0000313|Proteomes:UP000007721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22248 / JCM 15807 / FRC-32
RC {ECO:0000313|Proteomes:UP000007721};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA Kostka J., Richardson P.;
RT "Complete sequence of Geobacter sp. FRC-32.";
RL Submitted (JAN-2009) 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; CP001390; ACM21733.1; -; Genomic_DNA.
DR AlphaFoldDB; B9M5H4; -.
DR STRING; 316067.Geob_3390; -.
DR KEGG; geo:Geob_3390; -.
DR eggNOG; COG3852; Bacteria.
DR HOGENOM; CLU_000445_114_39_7; -.
DR Proteomes; UP000007721; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
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 PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 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; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ACM21733.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000007721};
KW Transferase {ECO:0000313|EMBL:ACM21733.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 47..66
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 93..151
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 219..425
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 427 AA; 47794 MW; D97CB023F4C5319D CRC64;
MRNSANALLR VWFFLFKIMA AVFIVETLVM LLMQYPLSSL PDNKKTFLDG AFLLLFLSPI
LYFLVVRPLV QKNAEHAEFQ ADLEEAFFEL NERKTFIESV LKNIQSGIIV TDPELRINLA
NEYALDFFAR KGSELVGEKL DTVCPMIYDL IRTGTYAAEV SESGRQQRTV GYKRFDLKQA
DGLPAGHIIT FIDISEVEKV RKEMRQKDRL ATMGEVVARV AHEMRNPLFG ITASSQILAM
ELPLTAEQKE LMNSILVEGR RMNRLVDELL DCSKEMKLKK VPFDMVKAVR DSISFNEPLI
MEKRLFLHKS FAEGEVTVTA DQERIRQVLV NLLKNAVDAV SEGGSITIEM EGKDGKVLIR
ILDSGPGIPE KNLEKIFDIF YTTKKSGTGL GLAVSRKIIE AHDGTLVAGN GPGGAVFTIT
LPRGLSA
//
