ID A0A263BTX0_9BACI Unreviewed; 586 AA.
AC A0A263BTX0;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 18-JUN-2025, entry version 31.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=CIB95_06735 {ECO:0000313|EMBL:OZM57160.1};
OS Lottiidibacillus patelloidae.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC Lottiidibacillus.
OX NCBI_TaxID=2670334 {ECO:0000313|EMBL:OZM57160.1, ECO:0000313|Proteomes:UP000217083};
RN [1] {ECO:0000313|Proteomes:UP000217083}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA5d-4 {ECO:0000313|Proteomes:UP000217083};
RA Huang Z.;
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OZM57160.1, ECO:0000313|Proteomes:UP000217083}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA5d-4 {ECO:0000313|EMBL:OZM57160.1,
RC ECO:0000313|Proteomes:UP000217083};
RA Liu R., Dong C., Shao Z.;
RT "Bacillus patelloidae sp. nov., isolated from the intestinal tract of a
RT marine limpet.";
RL Submitted (SEP-2017) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OZM57160.1}.
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DR EMBL; NPIA01000003; OZM57160.1; -; Genomic_DNA.
DR RefSeq; WP_094923576.1; NZ_NPIA01000003.1.
DR AlphaFoldDB; A0A263BTX0; -.
DR Proteomes; UP000217083; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000156; F:phosphorelay response regulator activity; IEA:TreeGrafter.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0030295; F:protein kinase activator activity; IEA:TreeGrafter.
DR GO; GO:0007234; P:osmosensory signaling via phosphorelay pathway; IEA:TreeGrafter.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR FunFam; 3.30.450.20:FF:000098; Sensor histidine kinase ResE; 1.
DR FunFam; 3.30.565.10:FF:000006; Sensor histidine kinase WalK; 1.
DR FunFam; 1.10.287.130:FF:000001; Two-component sensor histidine kinase; 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; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P_dom.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR041328; HisK_sensor.
DR InterPro; IPR052545; Light-responsive_reg.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR42878:SF3; HISTIDINE PROTEIN KINASE SAES; 1.
DR PANTHER; PTHR42878; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF18698; HisK_sensor; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 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 Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:OZM57160.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000217083};
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 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 172..193
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 193..245
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 369..586
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 586 AA; 65777 MW; B904FF2CEFA0F81C CRC64;
MSFLRSVVGK LWGTIIILVA LVLFILTLLL LQYFENFHVN EAEKTLTQVA TKISHMLEDY
ELEEEALTIA SEILDSHLAN GVIIKDSSMM WLAEGMEDAK QNEAAFFNLI EANKVLSGSQ
VIKQEKRQSE ETIGDLFIVG VPYTIKSGNI GAVYVFQSIE DVEETTAHTK TAIFISATIA
IILTTIFAFF LSSRITAPLR KMREAATKVA KGQFDTKVPM VTNDEIGELA MAFNRMGRQL
SNNIMALNQE KEQLSSILSS MADGVITINK RGGIVITNPP AEQFLRVWSY QQGLNEEEKE
LPADVRELFT RVVSIEKEQF ADIHIQGRSW VVVMTPLYNN NTIRGAVAVI RDMTEERRLD
KLREDFIANV SHELRTPIAM LQGYSEAIID DIAQSPDDKK QIAKIIYDES LRMGRLVNEL
LDLARMESED VTLQLEEVEL NSFIERVTRK FNGMVNEKNI ALAFNKISSE KLTIDQDRIE
QVLTNLIDNA IRHTPENGKV EVKVKSVSSG VQFSVSDNGI GIKGEELPYI FERFYKTDKA
RTRGRSGIGL GLAIAKKIVE AHKGQISVES KIGHGTTFSF YIPRIS
//
