LYTS_STAAR
ID LYTS_STAAR Reviewed; 584 AA.
AC Q6GK52;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 109.
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=SAR0257;
OS Staphylococcus aureus (strain MRSA252).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282458;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSA252;
RX PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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}.
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DR EMBL; BX571856; CAG39283.1; -; Genomic_DNA.
DR RefSeq; WP_000950282.1; NC_002952.2.
DR AlphaFoldDB; Q6GK52; -.
DR SMR; Q6GK52; -.
DR KEGG; sar:SAR0257; -.
DR HOGENOM; CLU_020473_3_3_9; -.
DR OMA; SHFFRSN; -.
DR Proteomes; UP000000596; 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_0000074795"
FT TRANSMEM 6..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 311..362
FT /note="GAF"
FT DOMAIN 363..580
FT /note="Histidine kinase"
FT MOD_RES 390
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 584 AA; 65028 MW; 9E8942D946D3A52E 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 INVEDKYRNV LVPPFLIQIL
VENAIKHAFT NRKQGNDIDV SVIKETATHV RIIVQDNGQG ISKDKMHLLG ETSVESESGT
GSALENLNLR LKGLFGKSAA LQFESTSSGT TFWCVLPYER QEEE
