ID   ARLS_STAAR              Reviewed;         451 AA.
AC   Q6GGZ4;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   16-JUN-2009, entry version 41.
DE   RecName: Full=Signal transduction histidine-protein kinase arlS;
DE            EC=2.7.13.3;
GN   Name=arlS; OrderedLocusNames=SAR1426;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.,
RA   Churcher C., Clark L., Corton C., Cronin A., Doggett J., Dowd L.,
RA   Feltwell T., Hance Z., Harris B., Hauser H., Holroyd S., Jagels K.,
RA   James K.D., Lennard N., Line A., Mayes R., Moule S., Mungall K.,
RA   Ormond D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Sanders M.,
RA   Sharp S., Simmonds M., Stevens K., Whitehead S., Barrell B.G.,
RA   Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains:
RT   evidence 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 arlS/arlR
CC       involved in the regulation of adhesion, autolysis, multidrug
CC       resistance and virulence. ArlS probably functions as a sensor
CC       protein kinase which is autophosphorylated at a histidine residue
CC       and transfers its phosphate group to arlR (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + protein L-histidine = ADP + protein N-
CC       phospho-L-histidine.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (By similarity).
CC   -!- PTM: Autophosphorylated (By similarity).
CC   -!- SIMILARITY: Contains 1 HAMP domain.
CC   -!- SIMILARITY: Contains 1 histidine kinase domain.
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DR   EMBL; BX571856; CAG40423.1; -; Genomic_DNA.
DR   RefSeq; YP_040828.1; -.
DR   GeneID; 2859859; -.
DR   GenomeReviews; BX571856_GR; SAR1426.
DR   KEGG; sar:SAR1426; -.
DR   HOGENOM; Q6GGZ4; -.
DR   OMA; Q6GGZ4; FIDNAMK.
DR   BioCyc; SAUR282458:SAR1426-MON; -.
DR   GO; GO:0016021; C:integral to 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:two-component sensor activity; IEA:InterPro.
DR   GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0018106; P:peptidyl-histidine phosphorylation; IEA:InterPro.
DR   GO; GO:0000160; P:two-component signal transduction system (p...; IEA:UniProtKB-KW.
DR   InterPro; IPR003594; ATP_bd_ATPase.
DR   InterPro; IPR003660; HAMP_linker_domain.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR003661; Sig_transdc_His_kin_sub1_dim/P.
DR   InterPro; IPR005467; Sig_transdc_His_kinase_core.
DR   Gene3D; G3DSA:3.30.565.10; ATP_bd_ATPase; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Complete proteome; Kinase; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Transferase; Transmembrane;
KW   Two-component regulatory system; Virulence.
FT   CHAIN         1    451       Signal transduction histidine-protein
FT                                kinase arlS.
FT                                /FTId=PRO_0000074692.
FT   TRANSMEM     11     31       Potential.
FT   TRANSMEM    156    176       Potential.
FT   DOMAIN      178    231       HAMP.
FT   DOMAIN      239    451       Histidine kinase.
FT   MOD_RES     242    242       Phosphohistidine; by autocatalysis (By
FT                                similarity).
SQ   SEQUENCE   451 AA;  52386 MW;  F3D99C9F42B371E2 CRC64;
     MTKRKLRNNW IIVTTMITFV TIFLFCLIII FFLKDTLHNS ELDDAERSSS DINNLFHSKP
     VKDISALDLN ASLGNFQEII IYDEHNNKLF ETSNDNTVRV EPGYEHRYFD RVIKKRYKGI
     DYLIIKEPIT TQDFKGYSLL IHSLENYDNI VKSLYIIALA FGVIATIITA TISYVFSTQI
     TKPLVSLSNK MIEIRRDGFQ NKLQLNTNYE EIDNLANTFN EMMSQIEESF NQQRQFVEDA
     SHELRTPLQI IQGHLNLIQR WGKKDPAVLE ESLNISIEEM NRIIKLVEEL LELTKGDVND
     ISSEAQTVHI NDEIRSRIHS LKQLHPDYQF DTDLTSKNLE IKMKPHQFEQ LFLIFIDNAI
     KYDVKNKKIK VKTRLKNKQK IIEITDHGIG IPEEDQDFIF DRFYRVDKSR SRSQGGNGLG
     LSIAQKIIQL NGGSIKIKSE INKGTTFKII F
//