ID A0A1B3XSU9_9BACI Unreviewed; 528 AA.
AC A0A1B3XSU9;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 18-JUN-2025, entry version 37.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ABE28_018110 {ECO:0000313|EMBL:AOH56283.1};
OS Peribacillus muralis.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC Peribacillus.
OX NCBI_TaxID=264697 {ECO:0000313|EMBL:AOH56283.1, ECO:0000313|Proteomes:UP000077926};
RN [1] {ECO:0000313|EMBL:AOH56283.1, ECO:0000313|Proteomes:UP000077926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G25-68 {ECO:0000313|EMBL:AOH56283.1,
RC ECO:0000313|Proteomes:UP000077926};
RA Zheng Z.;
RT "Complete genome sequence of Bacillus muralis G25-68, a strain with
RT toxicity to nematodes.";
RL Submitted (AUG-2016) 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: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
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DR EMBL; CP017080; AOH56283.1; -; Genomic_DNA.
DR RefSeq; WP_064465706.1; NZ_CP017080.1.
DR AlphaFoldDB; A0A1B3XSU9; -.
DR STRING; 264697.ABE28_018110; -.
DR KEGG; bmur:ABE28_018110; -.
DR Proteomes; UP000077926; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR FunFam; 3.30.450.20:FF:000018; Sensor histidine kinase DcuS; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR033463; sCache_3.
DR InterPro; IPR029151; Sensor-like_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR016120; Sig_transdc_His_kin_SpoOB.
DR InterPro; IPR039506; SPOB_a.
DR PANTHER; PTHR43547:SF3; SENSOR PROTEIN CITS; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF17203; sCache_3_2; 1.
DR Pfam; PF14689; SPOB_a; 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; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR SUPFAM; SSF103190; Sensory domain-like; 1.
DR SUPFAM; SSF55890; Sporulation response regulatory protein Spo0B; 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 Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000077926};
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 174..192
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 332..525
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 528 AA; 58616 MW; 86D3EAA4EF6CAF25 CRC64;
MRKVSLETKI LGLVLSLSLF LILLLAISFS YMEGRQIAKD KGQLALELSK TISFMPTVTE
AFETDEPASI IQPVVERIRR ETGAEFIVVG NDKEMRYSHP LISEIGKRMK GGDNSRAIRD
GEYYVSEAAG SLGLSIRGKS PIFNKEGKII GIVSVGFLVE DVRAQIFKDL SKEMLISLLA
IMISIIGSYM LARSIRRDTL GLEPFEIANL YKEKNAVLQS VKEGILAIDQ NGLITSMNQP
AKKLLDIKES VRHLNVDGLF PSKYLFEVLR SGEPQADKEI SWKDKSIIVN CTPIFDSEGV
SGVVASFRDR TEIEEMVNTL SEVKMHSEDL RAQTHEFTNK LYVLSGLLQL GEYDEAIDMI
QSETSELHSL NRVVFEQIKD TKVQALLLGK IGKASEKKIS FEIDSQSYLE KLPDHIKLSQ
LTLIVGNIID NALEAVSGMD EPLVKFFATD IGNDLVFEVS DNGKGIPEQD ISFIFDRGFT
SKNNGSPSGY GLANADQVVK ELEGIIEVQS EDGNTIFTVY LPKQRRGG
//
