ID   LYTS_STAA3              Reviewed;         584 AA.
AC   Q2FK10;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 2.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Sensor histidine kinase/phosphatase LytS;
DE            EC=2.7.13.3 {ECO:0000250|UniProtKB:Q53705};
DE            EC=3.1.3.- {ECO:0000250|UniProtKB:Q53705};
DE   AltName: Full=Autolysin sensor kinase;
GN   Name=lytS; OrderedLocusNames=SAUSA300_0254;
OS   Staphylococcus aureus (strain USA300).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=367830;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USA300;
RX   PubMed=16517273; DOI=10.1016/s0140-6736(06)68231-7;
RA   Diep B.A., Gill S.R., Chang R.F., Phan T.H., Chen J.H., Davidson M.G.,
RA   Lin F., Lin J., Carleton H.A., Mongodin E.F., Sensabaugh G.F.,
RA   Perdreau-Remington F.;
RT   "Complete genome sequence of USA300, an epidemic clone of community-
RT   acquired meticillin-resistant Staphylococcus aureus.";
RL   Lancet 367:731-739(2006).
CC   -!- FUNCTION: Member of the two-component regulatory system LytR/LytS that
CC       regulates genes involved in autolysis, programmed cell death, biofilm
CC       formation and cell wall metabolism. Participates also in sensing and
CC       responding to host defense cationic antimicrobial peptides (HDPs).
CC       Functions as a sensor protein kinase which is autophosphorylated at a
CC       histidine residue and transfers its phosphate group to the conserved
CC       aspartic acid residue in the regulatory domain of LytR. In turn, LytR
CC       binds to the upstream promoter regions of target genes including lrgA
CC       and lrgB, to positively regulate their expression. Possesses also a
CC       phosphatase activity that dephosphorylates and thus inactivates LytR.
CC       {ECO:0000250|UniProtKB:Q53705}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3; Evidence={ECO:0000250|UniProtKB:Q53705};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- PTM: Autophosphorylated on His-390. {ECO:0000250|UniProtKB:Q53705}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABD21266.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000255; ABD21266.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_000950281.1; NZ_CP027476.1.
DR   AlphaFoldDB; Q2FK10; -.
DR   SMR; Q2FK10; -.
DR   EnsemblBacteria; ABD21266; ABD21266; SAUSA300_0254.
DR   KEGG; saa:SAUSA300_0254; -.
DR   HOGENOM; CLU_020473_3_3_9; -.
DR   Proteomes; UP000001939; 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:0016787; F:hydrolase activity; 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; Hydrolase; Kinase; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Transferase; Transmembrane;
KW   Transmembrane helix; Two-component regulatory system.
FT   CHAIN           1..584
FT                   /note="Sensor histidine kinase/phosphatase LytS"
FT                   /id="PRO_0000292215"
FT   TRANSMEM        2..22
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        42..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        92..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        121..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        154..174
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        186..206
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          311..363
FT                   /note="GAF"
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;  65029 MW;  6E8342DEF0057E43 CRC64;
     MLSLTMLLLE RVGLIIILAY VLMNIPYFKN LMNRRRTWKA RWQLCIIFSL FALMSNLTGI
     VIDHQHSLSG SVYFRLDDDV SLANTRVLTI GVAGLVGGPF VGLFVGVISG IFRVYMGGAD
     AQVYLISSIF IGIIAGYFGL QAQRRKRYPS IAKSAMIGIV MEMIQMLSIL TFSHDKAYAV
     DLISLIALPM IIVNSVGTAI FMSIIISTLK QEEQMKAVQT HDVLQLMNQT LPYFKEGLNR
     ESAQQIAMII KNLMKVSAVA ITSKNEILSH VGAGSDHHIP TNEILTSLSK DVLKSGKLKE
     VHTKEEIGCS HPNCPLRAAI VIPLEMHGSI VGTLKMYFTN PNDLTFVERQ LAEGLANIFS
     SQIELGEAET QSKLLKDAEI KSLQAQVSPH FFFNSINTIS ALVRINSEKA RELLLELSYF
     FRANLQGSKQ HTITLDKELS QVRAYLSLEQ ARYPGRFNIN INVEDKYRDV LVPPFLIQIL
     VENAIKHAFT NRKQGNDIDV SVIKETATHV RIIVQDNGQG ISKDKMHLLG ETSVESESGT
     GSALENLNLR LKGLFGKSAA LQFESTSSGT TFWCVLPYER QEEE