ID E8WTW7_GEOS8 Unreviewed; 947 AA.
AC E8WTW7;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=GM18_2858 {ECO:0000313|EMBL:ADW14302.1};
OS Geobacter sp. (strain M18).
OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC Geobacteraceae; Geobacter.
OX NCBI_TaxID=443143 {ECO:0000313|EMBL:ADW14302.1, ECO:0000313|Proteomes:UP000001442};
RN [1] {ECO:0000313|EMBL:ADW14302.1, ECO:0000313|Proteomes:UP000001442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M18 {ECO:0000313|EMBL:ADW14302.1,
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};
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DR EMBL; CP002479; ADW14302.1; -; Genomic_DNA.
DR AlphaFoldDB; E8WTW7; -.
DR STRING; 443143.GM18_2858; -.
DR KEGG; geb:GM18_2858; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2202; Bacteria.
DR eggNOG; COG4191; Bacteria.
DR eggNOG; COG4319; Bacteria.
DR HOGENOM; CLU_310527_0_0_7; -.
DR OrthoDB; 9813024at2; -.
DR Proteomes; UP000001442; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.10.450.50; -; 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; 3.
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; IPR032710; NTF2-like_dom_sf.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR037401; SnoaL-like.
DR NCBIfam; TIGR00229; sensory_box; 2.
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; PF00989; PAS; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF12860; PAS_7; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF13474; SnoaL_3; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 3.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF54427; NTF2-like; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:ADW14302.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:ADW14302.1}.
FT DOMAIN 266..317
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 318..376
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 394..445
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 585..801
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 824..944
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 141..182
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 301..328
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 878
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 947 AA; 104514 MW; E7698831A9700C11 CRC64;
MDTSDYQEIR ELFDHYIRMY SNRDDLLTTY FSEDFSGITG SGDYLVKDRE TWIAVTRQDF
AQVKDPINIE LKDLAIQMLA DTIAVTSSTF IIRLPIEEQI LSKKIARLVL IFRKEGAGWK
ISHSSISVSF GVADEGEIYP LKDLEDRNRH LEELVAERTG QLSEANCKLK QANENLAKEI
EGHKKSEIAN ARLLLRQRAI LDNLPMMAWL KDTESRLEMI NEPYARACGR TIEECIGKTD
LELFPREMAE EFLADDRAVC VSGRKRHFEE QIATQDGIRW HSTSKTPLFD ELGRVVGTTG
IARDITERKQ AEKALVESEE RFRSLMENIP NVAVQGYALD GTVLFWNRAS EILYGYSAQE
ALGANLLELI IPDEMQDGVK EAIGWMQESG TPIPAGELLL MRKDGSRVPV FSSHALLSPV
GRPPEFFCVD VDLTKRKKAE DLLSYAISLT NASLESTADG ILVVNRNGKI AQWNRKFIEL
WHVPEELLVT DVKDPVLAYL TSQMAHPDEF LAKVTELYEH PEASSQDLLT LADGRLFDRY
SQPLEIGKEI VGRFWSFRDV TGHKRHQQEQ LKIEKLESLG LLAGGIAHDF NNILTGVMGN
ISFAQMLLDP SHKSFKPLAE AEKASLRATE LARQLLTFAR GGEPVRKIIS LQDVVNESVE
LVLSGSNVKG IIDIPDATHA IDADEGQLSQ VLHNIVINAA QAMPGGGTLT VTARNETLTE
TNDMSLNPGS YVRLTIADRG CGMPEAVMTK IFDPYFTTKS AGNGLGLASA YSIVTRHGGH
IGVDSVLDRG TVFTIHLPSI GETYSAYTTE SAAESAGEQH GGGSILVMDD EAMIRDFTSA
MLQELGYQVT TCTGGAEAIT LYQRALRSGS PFAAVIMDLT IPGGIGGKEA AQQVLAMDAK
AKLIVSSGYS NDPIVSDYSA YGFSAAVAKP YRIHDLGQIL ISLLSRQ
//
