ID A0A4Y9ACV5_9BACI Unreviewed; 533 AA.
AC A0A4Y9ACV5;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 18-JUN-2025, entry version 25.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=E4U82_08000 {ECO:0000313|EMBL:TFJ93265.1};
OS Lentibacillus salicampi.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC Lentibacillus.
OX NCBI_TaxID=175306 {ECO:0000313|EMBL:TFJ93265.1, ECO:0000313|Proteomes:UP000298484};
RN [1] {ECO:0000313|EMBL:TFJ93265.1, ECO:0000313|Proteomes:UP000298484}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-719 {ECO:0000313|EMBL:TFJ93265.1,
RC ECO:0000313|Proteomes:UP000298484};
RA Maclea K.S., Simoes Junior M.;
RT "Genome sequence of Lentibacillus salicampi ATCC BAA-719.";
RL Submitted (MAR-2019) 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:TFJ93265.1}.
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DR EMBL; SRHY01000008; TFJ93265.1; -; Genomic_DNA.
DR RefSeq; WP_135109675.1; NZ_SRHY01000008.1.
DR AlphaFoldDB; A0A4Y9ACV5; -.
DR OrthoDB; 9792686at2; -.
DR Proteomes; UP000298484; 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: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 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; 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:SF3; SENSOR PROTEIN CITS; 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:TFJ93265.1};
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:UP000298484};
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 13..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 335..526
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 533 AA; 59478 MW; 8FB9404C2D940DAF CRC64;
MVKLKNVSLQ TKILTLIISL ILVVIILLSG IYIVLEKQQT EENMGDRALQ VSKTVSFMPS
VREAFHDANP SDSLQSIAEN VRLQVGADYV VIANADGERY AHPNASLLGK PMAGDDNYRA
LIFGQYYISQ SASSLGPALN GKSPVFDDDG NIMGIVSTGY LLEEIYAEIY QKIWDISKIS
LVVLILGTIG GIVLTNNIRK DTLGLEPYEI ANLYRERSAI LHSIKEGVIA IDEKGLITMM
NQAASDMLEL HSNYLYKPIE DILPNTLMYR VLESGENEQN QEMYLNDRWV IVSREVIKES
DKIVGVVASF RDKTEIQEMI ETISEVRQYS EDLRAQTHEY TNRLYVLSGL IQLGEYDEAV
DMIQSELKTT DTQNHILFDQ IQDSKVQAIL LGKIGKASEK KVNFSLDDNS SLNALPDHID
ISSLIGIIGN IIDNAFESVE STEEKDVTFF ATDVGNDIIF EVADSGKGID ENKDLFKKGF
STKIGGDRGY GLTILQDTVK RLGGWIEMKN QKYGGTIVTV FLPEQLKQRG TFR
//