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Database: UniProt
Entry: A0A1T5A9Z9_9BACI
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ID   A0A1T5A9Z9_9BACI        Unreviewed;       533 AA.
AC   A0A1T5A9Z9;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=SAMN06295926_101450 {ECO:0000313|EMBL:SKB31822.1};
OS   Lysinibacillus sp. AC-3.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX   NCBI_TaxID=1680467 {ECO:0000313|EMBL:SKB31822.1, ECO:0000313|Proteomes:UP000190941};
RN   [1] {ECO:0000313|EMBL:SKB31822.1, ECO:0000313|Proteomes:UP000190941}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AC-3 {ECO:0000313|EMBL:SKB31822.1,
RC   ECO:0000313|Proteomes:UP000190941};
RA   Peterson S.W.;
RL   Submitted (FEB-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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; FUYW01000001; SKB31822.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T5A9Z9; -.
DR   STRING; 1680467.SAMN06295926_101450; -.
DR   Proteomes; UP000190941; 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   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd00130; PAS; 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; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013767; PAS_fold.
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:SF10; SENSOR HISTIDINE KINASE DCUS; 1.
DR   PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00989; PAS; 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   SMART; SM00091; PAS; 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, ECO:0000313|EMBL:SKB31822.1};
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|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        175..194
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          337..532
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   533 AA;  59730 MW;  386A08CCD20478CA CRC64;
     MMKMPVNGKI LLVTFLIIAF SFLLGGIFVL GNLLTEQEKE FGQRAMLVAR TVSNVPEIST
     HLKNDNMKEA AKHVNKIVDG IRVVNKAEYI VVMNKDRIKL SHPVSKEIGK RSESQDLNAA
     FSEHYYVSKA QGEAGVMIRA FVPIIDEKKE QVGIVIVGYS LPTFIEMLQN YEHEIFITIL
     ISLVFSIWGA YTLGRHIKKQ MFGLEPHEIA KMYVERTETF NAMHEGIIAV DKEMNITIFN
     EKAADILGVT RKIEDCIGEN IYDVLPDTRL PEIVETANPV YNQELYINHH SILSNRVPII
     VNGELVGAVA MFKDLTAVKK LAEEVTGVKA FVQALRVQTH EHKNKLHTIA GLLQLGHTKQ
     ALEYVTATTE NEASLTKFLN ERFHNENISG LLLSKVSYGK ELGIQVEIDR KSHFKRFPPL
     LDHHDFVVLL GNLIENAFEA LNVLSKDDKY VAISVDEHDG VLAIAVSDNG IGMSEEVQAR
     MFENGFSTKA SENRGIGLHL IHEIVKKGNG DIEVVSEFMK GTSFLILLEL GEE
//
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