ID B9M3C3_GEODF Unreviewed; 887 AA.
AC B9M3C3;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Geob_1173 {ECO:0000313|EMBL:ACM19533.1};
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:ACM19533.1, ECO:0000313|Proteomes:UP000007721};
RN [1] {ECO:0000313|EMBL:ACM19533.1, 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; ACM19533.1; -; Genomic_DNA.
DR RefSeq; WP_012646262.1; NC_011979.1.
DR AlphaFoldDB; B9M3C3; -.
DR STRING; 316067.Geob_1173; -.
DR KEGG; geo:Geob_1173; -.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_000445_114_21_7; -.
DR OrthoDB; 5389345at2; -.
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; cd06225; HAMP; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd12914; PDC1_DGC_like; 1.
DR CDD; cd00156; REC; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003660; HAMP_dom.
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; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 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; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ACM19533.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000007721};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 285..308
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 310..362
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 374..418
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 450..500
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 520..743
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 765..879
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 484..511
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 814
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 887 AA; 98005 MW; 9BD7F695F2B21D13 CRC64;
MAFFKWYSIR IKLLGIMLLS GLPLVLAVGS LLHGNFKGAY RESEHAAIVT AQAIAYRHNA
QVEGLRHLLV ALAQHPDIKA RNRGACARIL QEIMSQGSSS SNIGIADTKG NLIASGTRSL
APDFNILDRK YFRDALRNRR FSVGEFAISR TLGKASLHFA LPVLDASGEP QAVIFAIQDL
NQFDTFFNLQ GFPADCNLTL SDHRGMIIYT YPGVRGLKVG SPDRLEITGM LHGGGDEGTF
VKIGLDGVKK LFAFKKIRLE QDGEPYMYIR ITIPHEVAMA DANRFILTSV AVLFLATLLT
IALSSLLAGR YLTTPLEQLS SAAREVAHGN LSVRTALPSH DELGFLSRSF DAMTEALSAR
LQEKDAAEAQ LKVSEEKFRA IFDHLSDAIF IHEIGNGRII DVNYAMCDMY GYTATEAIKL
TIQEISQGEP PYSATEAMQF MQLAGDGEPQ LFEWHARHHD GSFFWVEVSM RRAAVGETDA
IVVLARDISE RKAAEAEKKT LLEQLNQSQK MESVGRLAGG IAHDFNNLLT PIIGFAELAA
QEIPENGTTK AKIDRIVQAA LRAKDLVHQL LSFSRKQILD MKIIDLNVVI SSFYQILRRT
ISERIEIRLQ LFPGLGGIRA DRTNVEQILM NLLVNAQDAI DGAGTVTIET GEVVLDDEYA
RFHAEAVPGR YALLAVTDTG NGIAKGDLPH IFEPFFTTKM TGKGSGLGLA TVYGIVKQHH
GNIWAYSEEG QGTVFKMYFP MTEAMPYLAD EKPIEQVDRG RTQGVILLVE DNELVRTMLK
ELLLGIGYDV LDAEHPRQAI LLAEGRQIDL LLTDVIMPDM DGPELHRRLL AAYPGLRVIF
MSGYTDNVVV QLVKEVQMAN FIQKPFTVHD IVERVAAMMA AAQRPVS
//
