ID   LYTS_STAES              Reviewed;         591 AA.
AC   Q8CR79;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 119.
DE   RecName: Full=Sensor protein LytS;
DE            EC=2.7.13.3;
DE   AltName: Full=Autolysin sensor kinase;
GN   Name=lytS; OrderedLocusNames=SE_2011;
OS   Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12228 / FDA PCI 1200;
RX   PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA   Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA   Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA   Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT   "Genome-based analysis of virulence genes in a non-biofilm-forming
RT   Staphylococcus epidermidis strain (ATCC 12228).";
RL   Mol. Microbiol. 49:1577-1593(2003).
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; AE015929; AAO05652.1; -; Genomic_DNA.
DR   RefSeq; NP_765566.1; NC_004461.1.
DR   RefSeq; WP_002484941.1; NZ_WBME01000003.1.
DR   AlphaFoldDB; Q8CR79; -.
DR   SMR; Q8CR79; -.
DR   STRING; 176280.SE_2011; -.
DR   EnsemblBacteria; AAO05652; AAO05652; SE_2011.
DR   KEGG; sep:SE_2011; -.
DR   PATRIC; fig|176280.10.peg.1964; -.
DR   eggNOG; COG3275; Bacteria.
DR   HOGENOM; CLU_020473_3_3_9; -.
DR   OMA; SHFFRSN; -.
DR   Proteomes; UP000001411; 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; 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; 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..591
FT                   /note="Sensor protein LytS"
FT                   /id="PRO_0000074799"
FT   TRANSMEM        4..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        45..67
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        87..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        122..139
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        154..176
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        183..205
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          363..579
FT                   /note="Histidine kinase"
FT   MOD_RES         390
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   591 AA;  65452 MW;  CDD533D63C325244 CRC64;
     MLNLFILLLE RVGLIILLAY ILMNINHFKT MMSERDKWRS KFQLIIIFGI FSMISNFTGI
     EIENGHIVSS DIYYHLSKDA SMANTRVLTI GVSGLIGGPW VAIIVGIISG LCRLYIGGAD
     AYTYLISSIV IAIISGYFGH QTIKQNTYPS IKKGAIIGAI TEIIQMGCIL LFTNNLHHAI
     TLVSFIALPM IIINSLGTAI FLTIILSTIK QEEQMRAVQT HDVLQLANET LPYFRSGLNE
     KSAQQAAEII LKLMQVSAVA ITNKKDILTH IGAGSDHHVA RKEIITDLSK EVIQSGKLKV
     AHTREGIGCH HPNCPLEGAI VVPLYIHNEV AGTLKFYFTD NNIISTSDQQ LAKGLANIFS
     SQLELGQAEM QGQLLKDAEI KSLQAQVNPH FFFNAINTIS ALVRIDSEKA RRLLIQLSQF
     FRSNLNGARN NTITLQKELQ QVAAYLSLEQ ARYPNRFNIH YRIDDQCQDA LIPPFIIQIL
     VENSIKHAFK NRKKNNHIDV DVSMKQDCLS ISVQDNGQGI PADQLDTIGY TTVTSTTGTG
     NALVNLNKRL TGLFGTTSAL NIQSSQSGTT VSCLIPYKSS KEEHFNESVN R