ID R4KGJ0_9FIRM Unreviewed; 757 AA.
AC R4KGJ0;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=Desgi_2939 {ECO:0000313|EMBL:AGL02328.1};
OS Desulfoscipio gibsoniae DSM 7213.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfallaceae;
OC Desulfoscipio.
OX NCBI_TaxID=767817 {ECO:0000313|EMBL:AGL02328.1, ECO:0000313|Proteomes:UP000013520};
RN [1] {ECO:0000313|EMBL:AGL02328.1, ECO:0000313|Proteomes:UP000013520}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7213 {ECO:0000313|EMBL:AGL02328.1,
RC ECO:0000313|Proteomes:UP000013520};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Parshina S.,
RA Plugge C., Muyzer G., Kuever J., Ivanova A., Nazina T., Klenk H.-P.,
RA Brambilla E., Spring S., Stams A.F., Woyke T.;
RT "Complete sequence of Desulfotomaculum gibsoniae DSM 7213.";
RL Submitted (JAN-2012) 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; CP003273; AGL02328.1; -; Genomic_DNA.
DR RefSeq; WP_006520812.1; NC_021184.1.
DR AlphaFoldDB; R4KGJ0; -.
DR STRING; 767817.Desgi_2939; -.
DR KEGG; dgi:Desgi_2939; -.
DR eggNOG; COG3850; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_023032_0_0_9; -.
DR OrthoDB; 112712at2; -.
DR Proteomes; UP000013520; 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 Gene3D; 3.30.450.20; PAS 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; PTHR45528; SENSOR HISTIDINE KINASE CPXA; 1.
DR PANTHER; PTHR45528:SF9; SENSOR HISTIDINE KINASE YRKQ; 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:AGL02328.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000013520};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 31..52
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 424..476
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 537..754
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 478..537
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 757 AA; 84418 MW; CC8E01DFB796D987 CRC64;
MRKNHQHPRC KNYGTISKLI HLFESSLHYK LLLVMVLITI PPLVLLGAYS LYQTTVEISR
AVESTKQNLI QNTLNLQQEN LKSQAALIDA GLENVVNNIK ILQSISENIF NNPEEYNRPG
TITNILTDSQ YGYYYSPPDH LPDTEISNVF ISNKTKVTPK LLAELERLKH MEPVMQSFVS
SNENVVAVYF NFKESAARIY PKLDFKKLVE LQLFPPDLEV GNYEFFYSAD EKHNPEKEIT
WTKIYRDITD RGLMITCNAP VYLAGGELRG VLGVDITMAN IINNILNIEF EQPGAYAALI
TASGEVIANP EKLSPDTNPN PIASLLGRTD NPVFKEIGQK IREGESGCRE VVLSGESKYL
LYGPMGNSGW ALIYVIPAHQ ITEPIEKEAR SLIIEKNSAI LSKISFGTLS ILLIVTVFSI
LLSGNITKPV KDLTSGATAL GEGNFGHVVP VNSKDEIGTL SVAFNTMSKQ LQEMVLALQQ
KAMEQQILNT ELADLNQDLE SKVLERTSRL EEANANLQEA LDSISAVEKS RRELLANVSH
ELRTPLMKIQ GYVEAVRDGL YKDNKEFLRY LETIYLHTTG INRLINDLFD LSQLDARQSM
HFTVTDLTPV FEQYFEEVSL FLEQKEINFS YSLDNTLPPV KVDPDRIIQV LENLVYNAAK
YSQPGGQIQI FVKALADGVL VEVTDSGRGI PAKDLPYIFT RFFKGRGVNN PKSNGAGLGL
AIAKAIVEAH QGTIGVESQP GKGSRFFFNI PVVPKGK
//
