ID   LYTS_BACCR              Reviewed;         589 AA.
AC   Q814J0;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 110.
DE   RecName: Full=Sensor protein LytS;
DE            EC=2.7.13.3;
GN   Name=lytS; OrderedLocusNames=BC_5441;
OS   Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS   15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=226900;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC   / NCTC 2599 / NRRL B-3711;
RX   PubMed=12721630; DOI=10.1038/nature01582;
RA   Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA   Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA   Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA   Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT   "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT   anthracis.";
RL   Nature 423:87-91(2003).
CC   -!- FUNCTION: Member of the two-component regulatory system LytS/LytT that
CC       probably regulates genes involved in cell wall metabolism.
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:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
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DR   EMBL; AE016877; AAP12303.1; -; Genomic_DNA.
DR   RefSeq; NP_835102.1; NC_004722.1.
DR   RefSeq; WP_000933560.1; NC_004722.1.
DR   AlphaFoldDB; Q814J0; -.
DR   SMR; Q814J0; -.
DR   STRING; 226900.BC_5441; -.
DR   EnsemblBacteria; AAP12303; AAP12303; BC_5441.
DR   KEGG; bce:BC5441; -.
DR   PATRIC; fig|226900.8.peg.5621; -.
DR   HOGENOM; CLU_020473_3_3_9; -.
DR   OMA; SHFFRSN; -.
DR   Proteomes; UP000001417; 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; IPR005467; His_kinase_dom.
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; PF13492; GAF_3; 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.
DR   PROSITE; PS50109; HIS_KIN; 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..589
FT                   /note="Sensor protein LytS"
FT                   /id="PRO_0000074788"
FT   TRANSMEM        4..25
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        116..138
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        153..172
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        184..206
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          235..360
FT                   /note="GAF"
FT   DOMAIN          360..577
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   MOD_RES         387
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ   SEQUENCE   589 AA;  65319 MW;  58957B6DF6470FAF CRC64;
     MLNLVLMMIE RVGLIVILGF LLSHIKTFRR LLHKQDGYVD KLKLICIFSV FTIVSNYTGI
     EIAGNTIMNE NWLQGVSSSS TIANTRIMGV GISGLLGGPI VGIGVGSIAG IHRYMLGGTT
     ALSCAISSIL AGVITGYIGY IFKKYNRTIT PKFSAILSVF IVSLEMIMIL LIVEDGMSIV
     KTIAIPMILV NSFGSFILLS MIQAILRQEE NAKALQTHKV LRIADKTLPY FRQGLTEESC
     KHVAQIIHRF PGTDAVSLTD TEKILAHVGL ASDHHIPSHS LITGLSKEVL HTGQIMKAKS
     REVINCQHEG CPLQAAIVIP LTSHGNTIGT LKLYFKNPNQ LSRVEEELAE GLAKIFSTQL
     ELGEAELQSK LLQDAEIKAL QAQINPHFLF NAINTVSALC RTDVEKARKL LLQLSVYFRC
     NLQGARQLLI PLEQELNHVQ AYLSLEQARF PNKYEVKMYI EDELKTTLVP PFVLQLLVEN
     ALRHAFPKKQ PVCEVEVHVF EKEGMVHFEV KDNGQGIEEE RLEQLGKMVV SSKKGTGTAL
     YNINERLIGL FGKETMLHIE SELNEGTEIT FVIPKKVGEE EQIVKSISS