ID Q39VW1_GEOMG Unreviewed; 579 AA.
AC Q39VW1;
DT 22-NOV-2005, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2005, sequence version 1.
DT 27-MAR-2024, entry version 113.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Gmet_1379 {ECO:0000313|EMBL:ABB31613.1};
OS Geobacter metallireducens (strain ATCC 53774 / DSM 7210 / GS-15).
OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC Geobacteraceae; Geobacter.
OX NCBI_TaxID=269799 {ECO:0000313|EMBL:ABB31613.1, ECO:0000313|Proteomes:UP000007073};
RN [1] {ECO:0000313|EMBL:ABB31613.1, ECO:0000313|Proteomes:UP000007073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 53774 / DSM 7210 / GS-15
RC {ECO:0000313|Proteomes:UP000007073};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J.,
RA Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Geobacter metallireducens GS-15.";
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABB31613.1, ECO:0000313|Proteomes:UP000007073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 53774 / DSM 7210 / GS-15
RC {ECO:0000313|Proteomes:UP000007073};
RX PubMed=19473543; DOI=10.1186/1471-2180-9-109;
RA Aklujkar M., Krushkal J., DiBartolo G., Lapidus A., Land M.L., Lovley D.R.;
RT "The genome sequence of Geobacter metallireducens: features of metabolism,
RT physiology and regulation common and dissimilar to Geobacter
RT sulfurreducens.";
RL BMC Microbiol. 9:109-109(2009).
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; CP000148; ABB31613.1; -; Genomic_DNA.
DR AlphaFoldDB; Q39VW1; -.
DR STRING; 269799.Gmet_1379; -.
DR KEGG; gme:Gmet_1379; -.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_000445_133_4_7; -.
DR Proteomes; UP000007073; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR029150; dCache_3.
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; IPR029151; Sensor-like_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF14827; dCache_3; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF103190; Sensory domain-like; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000313|EMBL:ABB31613.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000007073};
KW Transferase {ECO:0000313|EMBL:ABB31613.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 299..321
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 350..573
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 579 AA; 66721 MW; 5525418272830D5E CRC64;
MLKFIEANKK RIVIVTYILL FCMFCFFSLM DLYKRTSDYA YFANKINSFI KHAHDSESEY
LCSRLVNYVS DIAKQKHFAE LLKAGDAEAL EKVANHAFYD FGKRYVPVIS VLIYDGDGKL
RYHMTPPSIT HDPEELRPNV SKEVFATKNY TYGYETNIVP LYFCIVLPVR DARSNVEGTI
EIGVDLSFFH YNLKWFLHDV KTAIFSNGKL LEFDTGDKTD SEEYVYDYYK KLKSNDAAFF
NQFKDRIDFR WAKNDIKIGD KYYLVSTSQV LRDNLGREVG KYLVAYDMTE LRNRHWGYFY
AWLLFFALTA CVMLCINMVG FRKYEHIITE QDKMLAQRSK QCALGEMLGH IGHQWRQPLY
NLSLIVQNIG LQNQYGKLDD ALLSKQITQA NQNIEYMSNI IDDWRSLLMS GSSRTVIELQ
SSVERAIAMV APVMEQSRVT IENRITTPVH TMGFVNDLVQ LTINVLLNAR DQLSLVQSDR
FILLSCNEES GGVVTVTFQD NGGGIPDHLL KRIFEPYVTT KDKADGTGLG LYLCHQIVEN
LDQGKVWAEN RSFELHGETH YGARICLQFA RTTEGGKQI
//
