ID A0A263BXD6_9BACI Unreviewed; 373 AA.
AC A0A263BXD6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 13-SEP-2023, entry version 17.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=CIB95_01275 {ECO:0000313|EMBL:OZM58232.1};
OS Lottiidibacillus patelloidae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lottiidibacillus.
OX NCBI_TaxID=2670334 {ECO:0000313|EMBL:OZM58232.1, 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:OZM58232.1, ECO:0000313|Proteomes:UP000217083}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA5d-4 {ECO:0000313|EMBL:OZM58232.1,
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 -!- 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:OZM58232.1}.
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DR EMBL; NPIA01000001; OZM58232.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A263BXD6; -.
DR Proteomes; UP000217083; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 1.10.490.70; Histidine kinase N-terminal domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
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; IPR018984; Histidine_kinase_N.
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; PF02518; HATPase_c; 1.
DR Pfam; PF09385; HisK_N; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
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 Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 165..373
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 373 AA; 42565 MW; 56A37CC7AF9D498A CRC64;
MDKSNYVDSI VSLLKKNEDE LVENWFNQAL ISESEPYLNE MVQNGHTTIN MIIKYLENPN
IINNIAALTE KIARERVDAN VNIGDFVFNI NIGRKLIFET INTSSLSESV KIDAIIKITN
MFDIFVKDAV TKYTKIKDEI INNKNQFITE MHSDRLTILG QIAASFAHEF RNPLTSIKGF
INLLENNFEK SDETSNYFKI INNEMESLQE KVNQFLYLSK LKILDDNIEG IDISNVVKEM
IVFLTPRFNE ENITIVQNID ENLKIFAVRD QIKQVILNIL HNAVEELHNN NFDRIIDVNV
SKSDGNIIVA IANNGPQIPS HLLENIFEPF ISTKELGTGL GLSVCKQIIE KHNGTISVIT
NPERTTFLLT FPE
//
