ID B9M8I3_GEODF Unreviewed; 603 AA.
AC B9M8I3;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=bamV {ECO:0000313|EMBL:ACM18518.1};
GN OrderedLocusNames=Geob_0144 {ECO:0000313|EMBL:ACM18518.1};
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:ACM18518.1, ECO:0000313|Proteomes:UP000007721};
RN [1] {ECO:0000313|EMBL:ACM18518.1, 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};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP001390; ACM18518.1; -; Genomic_DNA.
DR RefSeq; WP_012645247.1; NC_011979.1.
DR AlphaFoldDB; B9M8I3; -.
DR STRING; 316067.Geob_0144; -.
DR KEGG; geo:Geob_0144; -.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_453271_0_0_7; -.
DR OrthoDB; 9805591at2; -.
DR Proteomes; UP000007721; Chromosome.
DR GO; GO:0005886; C:plasma 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; IPR033479; dCache_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; 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; PF02743; dCache_1; 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 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 PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000313|EMBL:ACM18518.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000007721};
KW Transferase {ECO:0000313|EMBL:ACM18518.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 318..339
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 385..594
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 603 AA; 67433 MW; 07903522059AE89C CRC64;
MTCIIRRHKL PVALFLISIG AVAALLLIQH ANRDVRAEAR ARFIEQYNRQ QSLMAELASH
TLEELFATYH RNLDLVVNLF EGKAVTRHRV EEVKGSLKKI YSSLANTPVI EMVIFDSKGT
AITIEPYDTY TIGRSYAWRD YYHWAREMGR PGQMYLSPYA RLQGGMQRGN KALIVAEGIY
GPGEKFLGVV ICAIDFEVLA KKHILPIHIG KEGHAWLADI SNRTMLVGPS GRLVGLSFEE
AFLPRWPRLY QLLLSMENGK PGSDWYDYLD PGTYQHQVRK IGSYHPIRIE NRLWALGIST
PEHEVEELLS TFLHRQELFA NTLLVTVLGV ATLLLGFLIN WNRVLSAQVQ NHTRALSEAH
TRLESTFDEL LVAKKVAAVG QLALGLSHEI RNPLSAIQMN MQMIRKKIDL AGTLRENFAI
VDGEIQRLNR LLKDVMDFAR PRSLNLQNTE LKEIISRLMQ LLSQRLEEQL IRTTVRTESP
IQLVCDPEQI HQVLLNLILN AMEAMNETPG ERHLTIFARS ADGMALVTVS DTGGGIPQGK
LEQLFDPFYT TRASGGGLGL SIVQTIVLRH GGSVAVESQP GQGATFTVAL PLKGPAGTGD
MSQ
//
