ID A0A177KXS2_9BACI Unreviewed; 592 AA.
AC A0A177KXS2;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=AWH49_05785 {ECO:0000313|EMBL:OAH58198.1};
OS Domibacillus aminovorans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Domibacillus.
OX NCBI_TaxID=29332 {ECO:0000313|EMBL:OAH58198.1, ECO:0000313|Proteomes:UP000076935};
RN [1] {ECO:0000313|EMBL:OAH58198.1, ECO:0000313|Proteomes:UP000076935}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1314 {ECO:0000313|EMBL:OAH58198.1,
RC ECO:0000313|Proteomes:UP000076935};
RA Verma A., Pal Y., Krishnamurthi S.;
RT "Investigation of taxonomic status of Bacillus aminovorans.";
RL Submitted (JAN-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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:OAH58198.1}.
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DR EMBL; LQWY01000073; OAH58198.1; -; Genomic_DNA.
DR RefSeq; WP_063966875.1; NZ_LQWY01000073.1.
DR AlphaFoldDB; A0A177KXS2; -.
DR STRING; 29332.AWH48_04405; -.
DR Proteomes; UP000076935; Unassembled WGS sequence.
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; cd00075; HATPase; 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; IPR041328; HisK_sensor.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR45453; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR PANTHER; PTHR45453:SF1; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF18698; HisK_sensor; 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 Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:OAH58198.1};
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..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 177..196
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 198..250
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 374..592
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 592 AA; 66280 MW; FFB8ED2CDD44EA09 CRC64;
MKIWRSVVGK LWATILLLVS FVLAFLTILL LEFFENYHIT QVEQQLENTA EKIATVIADH
ENKATGLEVA WELVDDPAHV MIAENENVYH YSPVETDEAK LSKETITGDP TLSAVFEGRQ
KVQAEVPIDE GSSLDSRYEN SFIVGVPFEM NNGENGAVFI YQSLQVMKET TEQTTKLILA
AAGIAIVLTT FFAFFLSTRV TAPLRKMREA ATELTQGNFD MKVPILTNDE IGALATSFNK
MGYQLKGNIH ALNQEKEQLS SILSSMADGV ITLDQNAKVL ITNPPAHQFL HNWQFENKAS
GNEAEVPTLL TALFEEAVKT ETEQEGELTM QGRSYVIIVS PLYNDESVRG AVTVVRDMTE
ERRLDKLRED FIANVSHELR TPISMMQGYS EAIVDDIAST EEEKREIAQI IHEESLRMGR
LVNELLDLAR MQAGHMTLNK EEADIEPFLI RVTNKFQGIA KEKNIHLSAE TSYSHAPVSI
DEDRIEQVLT NLIDNALRHT PENGNVKVVH ELKELYHVIR VEDSGSGIPE EDLPFVFERF
YKADKARTRG RSGTGLGLSI AKNIVHAHGG TIKVQSHLGQ GTVFFFTIPR HA
//