ID   LYTS_STAHJ              Reviewed;         584 AA.
AC   Q4L8V3;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   25-MAY-2022, entry version 125.
DE   RecName: Full=Sensor protein LytS;
DE            EC=2.7.13.3;
DE   AltName: Full=Autolysin sensor kinase;
GN   Name=lytS; OrderedLocusNames=SH0613;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC1435;
RX   PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA   Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(2005).
CC   -!- FUNCTION: Member of the two-component regulatory system LytR/LytS that
CC       probably regulates genes involved in cell wall metabolism.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
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DR   EMBL; AP006716; BAE03922.1; -; Genomic_DNA.
DR   RefSeq; WP_011274938.1; NC_007168.1.
DR   AlphaFoldDB; Q4L8V3; -.
DR   SMR; Q4L8V3; -.
DR   STRING; 279808.SH0613; -.
DR   PRIDE; Q4L8V3; -.
DR   EnsemblBacteria; BAE03922; BAE03922; SH0613.
DR   KEGG; sha:SH0613; -.
DR   eggNOG; COG3275; Bacteria.
DR   HOGENOM; CLU_020473_3_3_9; -.
DR   OMA; SHFFRSN; -.
DR   OrthoDB; 1031920at2; -.
DR   Proteomes; UP000000543; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0071555; P:cell wall organization; IEA:InterPro.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR010559; Sig_transdc_His_kin_internal.
DR   InterPro; IPR011620; Sig_transdc_His_kinase_LytS_TM.
DR   Pfam; PF07694; 5TM-5TMR_LYT; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF06580; His_kinase; 1.
DR   SMART; SM00065; GAF; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Kinase; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Transferase; Transmembrane; Transmembrane helix;
KW   Two-component regulatory system.
FT   CHAIN           1..584
FT                   /note="Sensor protein LytS"
FT                   /id="PRO_0000292216"
FT   TRANSMEM        2..22
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        42..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        87..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        114..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        152..172
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        185..205
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          379..461
FT                   /note="Histidine kinase"
FT   MOD_RES         390
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   584 AA;  64861 MW;  AEEB5209CC764F0B CRC64;
     MFNLFILLLE RVGLIIIIAY MLMNINHFKT MMGEREKLRS QWQLTILFAL FAITSNFTGI
     EIENGHIVSS NIYYQLNDDA SMANTRVLTI GMSGLIGGPF VAIIVGIVSG LSRLYIGGAN
     AYTYLISSIF IALISGFYGY RTMRRYTYPT VLMGAIIGAL NEAIQMACIL IFANDTASAW
     SLVQFIALPM ILINSIGTAI FLSIILSTLK QEEQTRAIQT HDVFEIANKT LPYFRSGLTE
     QSARSVAEII LKLMNVSAVA ITNRTDILTH VGAASDHHVA KKAIITDLSK EVIKTGHLKE
     AHSKEEIGCN NPNCSLTSAI VIPLMINQEV AGTLKFYFTN EYENTTSTKQ LARGLADIFS
     SQLELGQAEM QSKLLKDAEI KSLQAQVNPH FFFNSINTIS ALVRIDSEKA RKLLLQLSQF
     FRSNLQGARN NTITLGKELQ QVEAYLALEQ ARFPDRFTIQ YHIDSSCKHV LIPPFVIQIL
     VENAIKHAFK HRRKDNIIDV VAHHDNEELT LTVRDNGSGI DDDKLPLIGQ MSVDSETGTG
     SALENLNRRL IGLYGTKAAL HFESTEIGTT VSCHIPSHTI KEDI