ID   LYTS_STRMU              Reviewed;         580 AA.
AC   Q8DVB6;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Sensor protein LytS;
DE            EC=2.7.13.3;
GN   Name=lytS; OrderedLocusNames=SMU_577;
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159;
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA   Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA   Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
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; AE014133; AAN58318.1; -; Genomic_DNA.
DR   RefSeq; NP_721012.1; NC_004350.2.
DR   RefSeq; WP_002262109.1; NC_004350.2.
DR   AlphaFoldDB; Q8DVB6; -.
DR   SMR; Q8DVB6; -.
DR   STRING; 210007.SMU_577; -.
DR   PRIDE; Q8DVB6; -.
DR   EnsemblBacteria; AAN58318; AAN58318; SMU_577.
DR   KEGG; smu:SMU_577; -.
DR   PATRIC; fig|210007.7.peg.512; -.
DR   eggNOG; COG3275; Bacteria.
DR   HOGENOM; CLU_020473_3_3_9; -.
DR   OMA; RVARNEM; -.
DR   PhylomeDB; Q8DVB6; -.
DR   Proteomes; UP000002512; 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; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix; Two-component regulatory system.
FT   CHAIN           1..580
FT                   /note="Sensor protein LytS"
FT                   /id="PRO_0000074803"
FT   TRANSMEM        4..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        39..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        86..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        115..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        152..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        176..198
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          356..571
FT                   /note="Histidine kinase"
FT   MOD_RES         383
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   580 AA;  64274 MW;  BEB5B68D0C5EF4AF CRC64;
     MLMILLFQRL GIIMILAFLL VNNSYFRQLI EERSKREKLV LIIIFGIFVI ISNMTGIEIT
     SDKSLVERPI LTTISHSDSL ANTRTLVITT ASLVGGPLVG TVVGFIGGVH RFFQGNFSGA
     FYIVSSALVG YISGRLGDQL KTNNLYPSTS QVIVISIIAE SIQMLFVGFF TGWDLVKLIF
     IPMMLLNSLG STLFLAILKT YLSNERQLRA VQTRDVLDLT QQTLPYLRQG LSQQSATKVC
     NIIKQHTNFD AVGLTDRTNV LAHIGVGQDH HIAGQAVKTD LSKSVILNGQ PQIALDKTAI
     ACPDQSCLLN SAIVVPLKIN NETVGALKMY FSGDKKMTEV EENLALGLAQ IFSGQLAIGI
     AEEQNKLANI AEIKALQSQI NPHFFFNAIN TISALIRLDA NKARYALMQL STFFRTSLQG
     GQDREISLEQ EKAHVDAYMN LEKLRFPDKY QLDYHITVST KMTLPPFGLQ VLVENAVRHA
     FKERKKDNHI CISITDQGEF YKVAVSDNGQ GISPNMIDKL GQETVSESKG TGTALVNLNN
     RLNLLYGSAS QLHFDSTDQG TTVWYEIPYQ KGDKDEHFNS