LYTS_STAAM
ID LYTS_STAAM Reviewed; 584 AA.
AC P60612; Q99WW3;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 1.
DT 25-MAY-2022, entry version 119.
DE RecName: Full=Sensor histidine kinase/phosphatase LytS;
DE EC=2.7.13.3 {ECO:0000269|PubMed:27127614};
DE EC=3.1.3.- {ECO:0000269|PubMed:27127614};
DE AltName: Full=Autolysin sensor kinase;
GN Name=lytS; OrderedLocusNames=SAV0260;
OS Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158878;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu50 / ATCC 700699;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND AUTOPHOSPHORYLATION.
RX PubMed=27127614; DOI=10.12688/f1000research.6213.2;
RA Patel K., Golemi-Kotra D.;
RT "Signaling mechanism by the Staphylococcus aureus two-component system
RT LytSR: role of acetyl phosphate in bypassing the cell membrane electrical
RT potential sensor LytS.";
RL F1000Research 4:79-79(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 (By similarity). Participates also
CC in sensing and responding to host defense cationic antimicrobial
CC peptides (HDPs) (By similarity). Functions as a sensor protein kinase
CC which is autophosphorylated at a histidine residue and transfers its
CC phosphate group to the conserved aspartic acid residue in the
CC regulatory domain of LytR (PubMed:27127614). In turn, LytR binds to the
CC upstream promoter regions of target genes including lrgA and lrgB, to
CC positively regulate their expression (PubMed:27127614). Possesses also
CC a phosphatase activity that dephosphorylates and thus inactivates LytR
CC (PubMed:27127614). {ECO:0000250|UniProtKB:Q53705,
CC ECO:0000269|PubMed:27127614}.
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:27127614};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- PTM: Autophosphorylated on His-390. {ECO:0000250|UniProtKB:Q53705}.
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; BA000017; BAB56422.1; -; Genomic_DNA.
DR RefSeq; WP_000950281.1; NC_002758.2.
DR AlphaFoldDB; P60612; -.
DR SMR; P60612; -.
DR PaxDb; P60612; -.
DR EnsemblBacteria; BAB56422; BAB56422; SAV0260.
DR KEGG; sav:SAV0260; -.
DR HOGENOM; CLU_020473_3_3_9; -.
DR OMA; SHFFRSN; -.
DR PhylomeDB; P60612; -.
DR Proteomes; UP000002481; 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; Transferase; Transmembrane;
KW Transmembrane helix; Two-component regulatory system.
FT CHAIN 1..584
FT /note="Sensor histidine kinase/phosphatase LytS"
FT /id="PRO_0000074793"
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; 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
