ID E8WSN3_GEOS8 Unreviewed; 732 AA.
AC E8WSN3;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=GM18_0710 {ECO:0000313|EMBL:ADW12191.1};
OS Geobacter sp. (strain M18).
OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC Geobacteraceae; Geobacter.
OX NCBI_TaxID=443143 {ECO:0000313|EMBL:ADW12191.1, ECO:0000313|Proteomes:UP000001442};
RN [1] {ECO:0000313|EMBL:ADW12191.1, ECO:0000313|Proteomes:UP000001442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M18 {ECO:0000313|EMBL:ADW12191.1,
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};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP002479; ADW12191.1; -; Genomic_DNA.
DR AlphaFoldDB; E8WSN3; -.
DR STRING; 443143.GM18_0710; -.
DR KEGG; geb:GM18_0710; -.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_114_15_7; -.
DR OrthoDB; 9758705at2; -.
DR Proteomes; UP000001442; Chromosome.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR036641; HPT_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 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; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000313|EMBL:ADW12191.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:ADW12191.1}.
FT DOMAIN 221..442
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 466..585
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 629..729
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 516
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 668
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 732 AA; 80071 MW; 1DC445C046B94BB8 CRC64;
MPDDPRDIQI RKLQERVNFL EETNLNYLRT LDVLTACSDF QSDIYRLKES SFVIHAVFGQ
LRRLIPFSTL AMFGIDEDSS FDLTVCEPER ARGPIRREIE ARVQDGTFAW ALNQNHPVVV
PTTSGSDTLV LHVLATNSRI RGMFAGVMQG SHLSVEVSTL NALSGILINT AYAVENSELY
DMLQEHMQNL ELKVQQRTTE LEHALVQAEA ATAAKSVFLA NMSHEIRTPM NGVIGLARLL
METPLDKVQS NYLESLSDCA ESLLTIINEI LDISKVEAGM ITLEKIVFDL RRFLDRSLQP
FMLRGQEKGV QVLLEASPDL PQLLVGDPVR IGQVLGNLIG NALKFTQRGT ITVSCRLIEM
KEGDVLLRLA VADTGIGIAP QALDVIFEKF SQADSSTTRL YGGTGLGLSI SRSLVELMGG
ALGVESRLGE GSVFSFTLQA RLPLPGELPA AEEAEEHEVE ARRPLRILLV DDVPINQLIS
LKLIAKTGAH QVDCAENGQD ALDKWEVTCY DLIFMDVQMP AMDGLEATRI IRGREQDTGH
RVHICAMTAN AMKEDVATCR EAGMDSHISK PVREKDLNAV IRKISAEALD LSAPGSGAVA
GAGAVPAPPA PDAEPDFDQG DLLERLGGEE ELVGVFVKKF VDAVTEHLQL LGEALQRGDH
DTCYFKSHTI AGTAANMGAP RIRKIAAQME QMVKSRELDQ LPELYQQLEQ AFNAFVVVAS
GPNDAAAAKM EA
//
