ID D6XY21_BACIE Unreviewed; 693 AA.
AC D6XY21;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Bsel_0558 {ECO:0000313|EMBL:ADH98094.1};
OS Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC Salisediminibacterium.
OX NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH98094.1, ECO:0000313|Proteomes:UP000000271};
RN [1] {ECO:0000313|EMBL:ADH98094.1, ECO:0000313|Proteomes:UP000000271}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC {ECO:0000313|Proteomes:UP000000271};
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., Sims D., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Stolz J.;
RT "Complete sequence of Bacillus selenitireducens MLS10.";
RL Submitted (OCT-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; CP001791; ADH98094.1; -; Genomic_DNA.
DR RefSeq; WP_013171523.1; NC_014219.1.
DR AlphaFoldDB; D6XY21; -.
DR STRING; 439292.Bsel_0558; -.
DR KEGG; bse:Bsel_0558; -.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_023166_0_0_9; -.
DR OrthoDB; 9815750at2; -.
DR Proteomes; UP000000271; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; 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; 1.10.8.500; HAMP domain in histidine kinase; 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; IPR035965; PAS-like_dom_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; 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 SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ADH98094.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 256..278
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 275..327
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 465..683
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 308..342
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 693 AA; 78588 MW; 5819A23BD44C52F2 CRC64;
MRKKMQSIRN KVLFFGLLMT IIPLALISVY YIQNMADYVG ETGEEMQKMR LEHLATDIRS
EIRQVMDQLD VLASLERPAE MKGPFYEVLS SQDAIDTLVV IDRDGVLLSQ VARHTLNHAD
TGDTWPVQAD SGVTPDAGEP VISDVLVNEY GQPYMQMIAE TGTDGLRIGA TVQLQKLIGN
VSSYQLDDEA VIYLEDPSNQ VIAHQDYSKL WQPSTEETAQ GIEIRTEIDE VQWELVMEQP
RREALSPVFD MMRRGGFTAT VMILFGSVIS VFAGLYFVKP IETLQQGMRR MKTGYWPEAM
PVERQDEFGE LTRAFNEMNE TIQEKEQRLR QEKERLDIVV NSMDAGLAVV RKDYSIAWMN
PKLEGWIGER REVPCFQLFH DQDDACYACP LRDEVTYDKM DEIMTRKDRS GAERIYRHRV
FPLNYTLEQD EEALIVMEDI TEEKQMEEKI IQTDKLSALG LMASSFAHEV NNPLASVQIY
AEDLSDRLTE DEAELLESGD MAHYLQVIRK NIDRCKTITG NLLNFSRKEN WEERDIRVRQ
VVEESLVLMN HSLNKQGVDV TVTEEEGLPA IRGDALKLSQ VFVNFIQNAI DAMAGKTAPA
LSIRLYQEGQ DLLVDVADNG SGIRPEDLDK LFDPFFTSKP TGKGTGLGLS VCYGIIKQMN
GVLEVESEPG EGAVFRVRLP VPQKETNPEH GEV
//
