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Database: UniProt
Entry: Q39S19_GEOMG
LinkDB: Q39S19_GEOMG
Original site: Q39S19_GEOMG 
ID   Q39S19_GEOMG            Unreviewed;       523 AA.
AC   Q39S19;
DT   22-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 128.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=Gmet_2737 {ECO:0000313|EMBL:ABB32955.1};
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:ABB32955.1, ECO:0000313|Proteomes:UP000007073};
RN   [1] {ECO:0000313|EMBL:ABB32955.1, 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:ABB32955.1, 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; ABB32955.1; -; Genomic_DNA.
DR   RefSeq; WP_004511722.1; NC_007517.1.
DR   AlphaFoldDB; Q39S19; -.
DR   STRING; 269799.Gmet_2737; -.
DR   KEGG; gme:Gmet_2737; -.
DR   eggNOG; COG4251; Bacteria.
DR   eggNOG; COG5000; Bacteria.
DR   HOGENOM; CLU_000445_114_71_7; -.
DR   Proteomes; UP000007073; 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   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 6.10.340.10; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR42878:SF7; BACTERIOPHYTOCHROME; 1.
DR   PANTHER; PTHR42878; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF158472; HAMP domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ABB32955.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007073};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        29..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        184..207
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          208..260
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          300..514
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          248..293
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   523 AA;  57723 MW;  D731C0120D4C5666 CRC64;
     MDKNSPCDSS QPANPTPPRD VRGSFRAKLF SATAAGIVIL SAVSIVFFLT NQHAILHENL
     VTEGQLLTRL LAHNARLGLF AANRDQLADL ADGVIRTPDV LEVTIVDRDG RTLARAARQS
     VSDGGSSAAL TQEFSEPVFA LQGKGNDDDL YFSPAQQPPQ AGQRLGTVRV VMDEEKVHAH
     VRRLTATAVI GALAFLAVGM GLVYLIIRGI TRPLTHLSDE VRAIERGETN VLLPVESEDE
     IGELTASYNR MVNALRQRRE ERDEAERQLR ELNARLEDKV IDRTAQLEAV NRELESFSYS
     AAHDLRAPLL RLNGLCKALK EDCGERLDEE ARAYIRRIAT VGRQMERVIS TMSTLFNVQR
     RGMTCREMDL GAMVRAIVAT LRQADPLREV ALTVGPEVTA HGDTELIWTA LENMVGNAWK
     FTSRTPDARI EFGSIERDGE KVFLLKDNGV GFDMAYVGKL FKPFERLHGP DEFPGTGVGL
     AIVHRVMERH DGRVWLESTP GAGTTCYFTL PSCSTSTTKT TSF
//
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