ID C6E6L1_GEOSM Unreviewed; 1023 AA.
AC C6E6L1;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=GM21_1798 {ECO:0000313|EMBL:ACT17852.1};
OS Geobacter sp. (strain M21).
OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC Geobacteraceae; Geobacter.
OX NCBI_TaxID=443144 {ECO:0000313|EMBL:ACT17852.1};
RN [1] {ECO:0000313|EMBL:ACT17852.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M21 {ECO:0000313|EMBL:ACT17852.1};
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 Lovley D.;
RT "Complete sequence of Geobacter sp. M21.";
RL Submitted (JUL-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; CP001661; ACT17852.1; -; Genomic_DNA.
DR AlphaFoldDB; C6E6L1; -.
DR STRING; 443144.GM21_1798; -.
DR KEGG; gem:GM21_1798; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG3829; Bacteria.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_000445_114_21_7; -.
DR OrthoDB; 5389366at2; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd12914; PDC1_DGC_like; 1.
DR CDD; cd12915; PDC2_DGC_like; 1.
DR CDD; cd00156; REC; 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; 4.
DR InterPro; IPR011006; CheY-like_superfamily.
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; 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 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; PF02743; dCache_1; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13426; PAS_9; 1.
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; 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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:ACT17852.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:ACT17852.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 17..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 448..504
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 648..873
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 893..1009
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 324..374
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 944
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1023 AA; 112852 MW; 31592785A03B1DF0 CRC64;
MNAATSQRNI RQSGRNLMVW TASVVLLVNL FLALTGFFSL WQSRETYLNN AQVQSDNLLQ
ALSYSIAGAL ESADIALLSM VDEVQQELQQ GPVEEGRLNR LLAGQHSRLP LLDSMRMADA
QGDIRYGTGL QAGALKNVSQ RSYFKKLAAD PKAGLVISEP ILGLISGKRV IILARRVERR
GGAFAGVVYC AIDLERVRGM LQPMQVGSHG KITLTDATLA TIVRHPQGTD AGDAPGEKGA
SGEIWDQIAR GRESGSYFGE SDAWGSSRLA SFRKIGRFPL YLSLELAPED FLARWRGELL
QISTMVCVFI LVTLILSRLI YLRCRRQAAA EDELTQAKEE LELRVAERTA ELHLANLKLT
TELAERERAE KREREGRNML AQIIDTIPQY VFWKDRQSIY EGCNAVFAKG AGMAHSDEIR
GKSDFDLPWL REESEAYRSD DCVVMEQKRA KFHIIEQQLQ AGGKRLWVDT TKVPLLNEQG
EVTGILGVYE DISERKAVEE SRDKALALVE SLLAASPTGI LVYEGASGCC VMANQAMAAM
VGVTRQQMPA LNFREIGLWR ETGILQLAEQ VLVDGRTRSI EVCAQTSFEK SLQAEFLLSR
FEVEGRPHLM FIAVDIAARK GLEEEKRQIQ AQMLHVQKLE SLGVLAGGIA HDFNNILMVV
LGNADLALMR LPEGTPAREN LQQIEQAASR AADLAQQMLA YSGRGNFVIE KLDLAQTVKE
MAQMLEISIS KKTRLHYDFA PDLPAISGDA TQLRQVILNL VLNASEAIGD NIGVIGIRTG
YLECDRAYLS ETWIDDRLPE GPYLMLEISD NGCGIKKEII PKIFDPFFTT KFTGRGLGMA
AVLGIVRSHN GAIKIYSEEG KGSTFRLLLP CMSAQGEALQ PTAEEDLWRG SGTVLLADDE
ESIRALGQEM LETLGFRVLT ACDGCAAVEL FREKREEIAC VVLDLTMPEL DGEQAFNVLR
ELDPGARVIL SSGYNEREVS RKFAGAGVSG FMQKPYKLAE MSRKLRQILE PGGGSQQAAE
LGG
//
