ID E8WT79_GEOS8 Unreviewed; 1039 AA.
AC E8WT79;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=GM18_2834 {ECO:0000313|EMBL:ADW14279.1};
OS Geobacter sp. (strain M18).
OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC Geobacteraceae; Geobacter.
OX NCBI_TaxID=443143 {ECO:0000313|EMBL:ADW14279.1, ECO:0000313|Proteomes:UP000001442};
RN [1] {ECO:0000313|EMBL:ADW14279.1, ECO:0000313|Proteomes:UP000001442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M18 {ECO:0000313|EMBL:ADW14279.1,
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; ADW14279.1; -; Genomic_DNA.
DR AlphaFoldDB; E8WT79; -.
DR STRING; 443143.GM18_2834; -.
DR KEGG; geb:GM18_2834; -.
DR eggNOG; COG0715; Bacteria.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG3852; Bacteria.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_000445_86_3_7; -.
DR OrthoDB; 9813024at2; -.
DR Proteomes; UP000001442; 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 CDD; cd00130; PAS; 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; 3.30.450.20; PAS domain; 2.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
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; 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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR015168; SsuA/THI5.
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; PF09084; NMT1; 1.
DR Pfam; PF08448; PAS_4; 2.
DR Pfam; PF00072; Response_reg; 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; 2.
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; SSF53850; Periplasmic binding protein-like II; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
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 Kinase {ECO:0000313|EMBL:ADW14279.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:ADW14279.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 352..376
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 402..472
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 476..528
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 672..888
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 909..1029
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 963
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1039 AA; 113381 MW; DD70532D1E40F2AC CRC64;
MTVLWKLFSS RVPIFDSGAA GILSPLISNR FPSTRRPGRL AAALFLLSLL LLEAAPALAL
EKASVQLKWL HHFQFAGYYA AQEKGFYRDA GLDVTIREGG PDTEVEKEVT TGRADFGVGT
SALLLNRARG EDLVVLGQIF QHSPAILLTP RRTGIRSVAQ MKGRRFMYSN QHGDMLTLLR
KNGIGENDIG KVEHRGDARD LLSGKADVMM AYSFNEPFIL EQVGEPYLAF SPLTYGIDFY
GDNFFTDRAT INSRPEVVRA FREATLRGWR YALSNKEEIA DLILAKYSRE RSREWLLFEA
NQMESLIQPT LVEMGYQSPT RWQHISATFS GMGMLPEGFD PSDIIYDPRP GAIYRLLTGA
LLFCAAAIAV LFAIVMKFRQ LNANLKAEMG ERNAAESALK ESEEQLRVIF ETSRAGIIMV
DPQGAIRFAN NRMAEMFGCS MEELIGSGYT SHLHPDQLEA GNALMIRLMT GEVSYASTER
HYLCGESGSF WGYLSGRRLE TPDGKLRALV GIISDVTDRI QAEDARGKAL MLVETLLAQS
PMGIVVYDGA SGNCVRANRA AAEISGGSVE ALLQQNFRQM SSWREVGLIE MAEQVLADGV
PRPLEKEVQS SSGKDLALRC YLTRFEVEGN PHLLVLVQDI TEEKRLDREN KRIEAQMLNM
QKLESLGVLA GGIAHDFNNI LTGIVGNISF TQMMLEPDHK AKGPLGKAEK ACQRAAELAG
QLLTFARGGQ PIKKLFSVKH LAGESLSLVL RGTNVKGRLE IAESLDIVEA DEGQINQAFN
NIIINAVHAM PGGGNFTITG SNETMAPDNR LGLAPGSYVR LAFSDEGCGI SDADLKKIFD
PYFTTKASGT GLGLASTHSI ITRHGGVILV DSVLGRGTDF TIYLPSTGKN AREVKSERTE
QRTPAGGGRV VVMDDEEMIR ELASAMLAQL GYSVATCCDG AEAIELYKAA QQQGEGFDAV
IMDLTIPGGM GGKEAARRIL ELDPRACLIV SSGYSNDPVL AEYRGHGFRA TLGKPYNVKE
IARALSLARA GAAPTGDRA
//
