LYTS_STAA8
ID LYTS_STAA8 Reviewed; 584 AA.
AC Q53705; P72361; Q2G1B5;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 2.
DT 25-MAY-2022, entry version 140.
DE RecName: Full=Sensor histidine kinase/phosphatase LytS {ECO:0000303|PubMed:25491472};
DE EC=2.7.13.3 {ECO:0000269|PubMed:25491472};
DE EC=3.1.3.- {ECO:0000269|PubMed:25491472};
DE AltName: Full=Autolysin sensor kinase;
GN Name=lytS; OrderedLocusNames=SAOUHSC_00230;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8550490; DOI=10.1128/jb.178.3.611-618.1996;
RA Brunskill E.W., Bayles K.W.;
RT "Identification and molecular characterization of a putative regulatory
RT locus that affects autolysis in Staphylococcus aureus.";
RL J. Bacteriol. 178:611-618(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23.
RX PubMed=9308171; DOI=10.1099/00221287-143-9-2877;
RA Brunskill E.W., de Jonge B.L.M., Bayles K.W.;
RT "The Staphylococcus aureus scdA gene: a novel locus that affects cell
RT division and morphogenesis.";
RL Microbiology 143:2877-2882(1997).
RN [4]
RP FUNCTION.
RC STRAIN=UAMS-1;
RX PubMed=19502411; DOI=10.1128/jb.00348-09;
RA Sharma-Kuinkel B.K., Mann E.E., Ahn J.S., Kuechenmeister L.J., Dunman P.M.,
RA Bayles K.W.;
RT "The Staphylococcus aureus LytSR two-component regulatory system affects
RT biofilm formation.";
RL J. Bacteriol. 191:4767-4775(2009).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=UAMS-1;
RX PubMed=23733465; DOI=10.1128/aac.00412-13;
RA Yang S.J., Xiong Y.Q., Yeaman M.R., Bayles K.W., Abdelhady W., Bayer A.S.;
RT "Role of the LytSR two-component regulatory system in adaptation to
RT cationic antimicrobial peptides in Staphylococcus aureus.";
RL Antimicrob. Agents Chemother. 57:3875-3882(2013).
RN [6]
RP FUNCTION, MUTAGENESIS OF HIS-390 AND ASN-394, CATALYTIC ACTIVITY,
RP AUTOPHOSPHORYLATION, AND PHOSPHORYLATION AT HIS-390.
RC STRAIN=UAMS-1;
RX PubMed=25491472; DOI=10.1111/mmi.12902;
RA Lehman M.K., Bose J.L., Sharma-Kuinkel B.K., Moormeier D.E., Endres J.L.,
RA Sadykov M.R., Biswas I., Bayles K.W.;
RT "Identification of the amino acids essential for LytSR-mediated signal
RT transduction in Staphylococcus aureus and their roles in biofilm-specific
RT gene expression.";
RL Mol. Microbiol. 95:723-737(2015).
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 (PubMed:19502411). Participates also
CC in sensing and responding to host defense cationic antimicrobial
CC peptides (CAMPs) (PubMed:23733465). Functions as a sensor protein
CC kinase which is autophosphorylated at a histidine residue and transfers
CC its phosphate group to the conserved aspartic acid residue in the
CC regulatory domain of LytR (PubMed:25491472). In turn, LytR binds to the
CC upstream promoter regions of target genes including lrgA and lrgB, to
CC positively regulate their expression. Possesses also a phosphatase
CC activity that dephosphorylates and thus inactivates LytR
CC (PubMed:25491472). {ECO:0000269|PubMed:19502411,
CC ECO:0000269|PubMed:23733465, ECO:0000269|PubMed:25491472}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000269|PubMed:25491472};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- PTM: Autophosphorylated on His-390. {ECO:0000269|PubMed:25491472}.
CC -!- DISRUPTION PHENOTYPE: Deletion significantly reduces target tissue
CC survival during calcium-daptomycin treatment and increases
CC susceptibility to host defense cationic antimicrobial peptides.
CC {ECO:0000269|PubMed:23733465}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABD29405.1; 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; L42945; AAB48182.1; -; Genomic_DNA.
DR EMBL; CP000253; ABD29405.1; ALT_INIT; Genomic_DNA.
DR EMBL; U57060; AAB81288.1; -; Genomic_DNA.
DR RefSeq; WP_000950281.1; NZ_LS483365.1.
DR RefSeq; YP_498825.1; NC_007795.1.
DR AlphaFoldDB; Q53705; -.
DR SMR; Q53705; -.
DR STRING; 1280.SAXN108_0240; -.
DR EnsemblBacteria; ABD29405; ABD29405; SAOUHSC_00230.
DR GeneID; 3920305; -.
DR KEGG; sao:SAOUHSC_00230; -.
DR PATRIC; fig|93061.5.peg.211; -.
DR eggNOG; COG3275; Bacteria.
DR HOGENOM; CLU_020473_3_3_9; -.
DR Proteomes; UP000008816; 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 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Hydrolase; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix; Two-component regulatory system.
FT CHAIN 1..584
FT /note="Sensor histidine kinase/phosphatase LytS"
FT /id="PRO_0000074797"
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:0000269|PubMed:25491472"
FT MUTAGEN 390
FT /note="H->A: Complete loss of autophosphorylation."
FT /evidence="ECO:0000269|PubMed:25491472"
FT MUTAGEN 394
FT /note="N->A: Abolishes phosphatase activity."
FT /evidence="ECO:0000269|PubMed:25491472"
FT CONFLICT 198
FT /note="T -> P (in Ref. 1; AAB48182)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="S -> P (in Ref. 1; AAB48182)"
FT /evidence="ECO:0000305"
FT CONFLICT 213
FT /note="E -> D (in Ref. 1; AAB48182)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="A -> P (in Ref. 1; AAB48182)"
FT /evidence="ECO:0000305"
FT CONFLICT 231
FT /note="L -> F (in Ref. 1; AAB48182)"
FT /evidence="ECO:0000305"
FT CONFLICT 258
FT /note="A -> S (in Ref. 1; AAB48182)"
FT /evidence="ECO:0000305"
FT CONFLICT 273
FT /note="A -> G (in Ref. 1; AAB48182)"
FT /evidence="ECO:0000305"
FT CONFLICT 398
FT /note="T -> P (in Ref. 1; AAB48182)"
FT /evidence="ECO:0000305"
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
