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   25-MAY-2022, entry version 112.
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; 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 ArlS/ArlR
CC       involved in the regulation of adhesion, autolysis, multidrug resistance
CC       and virulence. ArlS probably functions as a sensor protein kinase which
CC       is autophosphorylated at a histidine residue and transfers its
CC       phosphate group to ArlR (By similarity). {ECO:0000250}.
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:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- PTM: Autophosphorylated. {ECO:0000250}.
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DR   EMBL; BX571856; CAG40423.1; -; Genomic_DNA.
DR   RefSeq; WP_000166793.1; NC_002952.2.
DR   AlphaFoldDB; Q6GGZ4; -.
DR   SMR; Q6GGZ4; -.
DR   KEGG; sar:SAR1426; -.
DR   HOGENOM; CLU_000445_89_6_9; -.
DR   OMA; TVIGNFR; -.
DR   OrthoDB; 692375at2; -.
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:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   InterPro; IPR041610; ArlS_N.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR003661; HisK_dim/P.
DR   InterPro; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   Pfam; PF18719; ArlS_N; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SUPFAM; SSF47384; SSF47384; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Kinase; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Transferase; Transmembrane; Transmembrane helix;
KW   Two-component regulatory system; Virulence.
FT   CHAIN           1..451
FT                   /note="Signal transduction histidine-protein kinase ArlS"
FT                   /id="PRO_0000074692"
FT   TRANSMEM        11..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        156..176
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          178..231
FT                   /note="HAMP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT   DOMAIN          239..451
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   MOD_RES         242
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
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