ARLS_STAA8
ID ARLS_STAA8 Reviewed; 451 AA.
AC Q9KJN3; Q2FYM0;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 144.
DE RecName: Full=Signal transduction histidine-protein kinase ArlS;
DE EC=2.7.13.3;
GN Name=arlS; OrderedLocusNames=SAOUHSC_01419;
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], AND FUNCTION.
RX PubMed=10869073; DOI=10.1128/jb.182.14.3955-3964.2000;
RA Fournier B., Hooper D.C.;
RT "A new two-component regulatory system involved in adhesion, autolysis, and
RT extracellular proteolytic activity of Staphylococcus aureus.";
RL J. Bacteriol. 182:3955-3964(2000).
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 FUNCTION.
RX PubMed=10633099; DOI=10.1128/jb.182.3.664-671.2000;
RA Fournier B., Aras R., Hooper D.C.;
RT "Expression of the multidrug resistance transporter NorA from
RT Staphylococcus aureus is modified by a two-component regulatory system.";
RL J. Bacteriol. 182:664-671(2000).
RN [4]
RP FUNCTION, AND REGULATION.
RX PubMed=11454217; DOI=10.1046/j.1365-2958.2001.02515.x;
RA Fournier B., Klier A., Rapoport G.;
RT "The two-component system ArlS-ArlR is a regulator of virulence gene
RT expression in Staphylococcus aureus.";
RL Mol. Microbiol. 41:247-261(2001).
RN [5]
RP REGULATION BY MGRA.
RX PubMed=12791130; DOI=10.1046/j.1365-2958.2003.03503.x;
RA Ingavale S.S., Van Wamel W., Cheung A.L.;
RT "Characterization of RAT, an autolysis regulator in Staphylococcus
RT aureus.";
RL Mol. Microbiol. 48:1451-1466(2003).
RN [6]
RP REGULATION BY SARV.
RX PubMed=15292128; DOI=10.1128/jb.186.16.5267-5280.2004;
RA Manna A.C., Ingavale S.S., Maloney M., van Wamel W., Cheung A.L.;
RT "Identification of sarV (SA2062), a new transcriptional regulator, is
RT repressed by SarA and MgrA (SA0641) and involved in the regulation of
RT autolysis in Staphylococcus aureus.";
RL J. Bacteriol. 186:5267-5280(2004).
RN [7]
RP FUNCTION.
RX PubMed=15528666; DOI=10.1099/mic.0.27194-0;
RA Fournier B., Klier A.;
RT "Protein A gene expression is regulated by DNA supercoiling which is
RT modified by the ArlS-ArlR two-component system of Staphylococcus aureus.";
RL Microbiology 150:3807-3819(2004).
RN [8]
RP FUNCTION IN BIOFILM DEVELOPMENT.
RX PubMed=16030226; DOI=10.1128/jb.187.15.5318-5329.2005;
RA Toledo-Arana A., Merino N., Vergara-Irigaray M., Debarbouille M.,
RA Penades J.R., Lasa I.;
RT "Staphylococcus aureus develops an alternative, ica-independent biofilm in
RT the absence of the arlRS two-component system.";
RL J. Bacteriol. 187:5318-5329(2005).
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. ArlS/ArlR affects expression of the multidrug
CC resistance transporter norA and interacts with both Agr (virulence
CC accessory gene regulator) (negatively) and SarA (staphylococcal
CC accessory regulator) (positively) to modulate several virulence factor
CC genes, including ssp (serine protease), spa (surface protein A) and hla
CC (alpha-hemolysin). Could inhibit biofilm development by a mechanism
CC independent of the presence of the poly-N-acetylglucosamine (PNAG).
CC Also, Arl proteins are required for the efficient activity of DNA
CC gyrase inhibitors and high osmolarity on spa expression.
CC {ECO:0000269|PubMed:10633099, ECO:0000269|PubMed:10869073,
CC ECO:0000269|PubMed:11454217, ECO:0000269|PubMed:15528666,
CC ECO:0000269|PubMed:16030226}.
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:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: Activated by agr, SarA, SarV and MgrA.
CC -!- PTM: Autophosphorylated. {ECO:0000305}.
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DR EMBL; AF165314; AAF85897.1; -; Genomic_DNA.
DR EMBL; CP000253; ABD30512.1; -; Genomic_DNA.
DR RefSeq; WP_000166801.1; NZ_LS483365.1.
DR RefSeq; YP_499945.1; NC_007795.1.
DR AlphaFoldDB; Q9KJN3; -.
DR SMR; Q9KJN3; -.
DR STRING; 1280.SAXN108_1433; -.
DR EnsemblBacteria; ABD30512; ABD30512; SAOUHSC_01419.
DR GeneID; 3920650; -.
DR KEGG; sao:SAOUHSC_01419; -.
DR PATRIC; fig|93061.5.peg.1298; -.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000445_89_6_9; -.
DR OMA; TVIGNFR; -.
DR PRO; PR:Q9KJN3; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0009927; F:histidine phosphotransfer kinase activity; IBA:GO_Central.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IBA:GO_Central.
DR GO; GO:0008236; F:serine-type peptidase activity; IMP:CACAO.
DR GO; GO:0046777; P:protein autophosphorylation; IBA:GO_Central.
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 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Kinase; Membrane; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix; Two-component regulatory system; Virulence.
FT CHAIN 1..451
FT /note="Signal transduction histidine-protein kinase ArlS"
FT /id="PRO_0000074688"
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; 52400 MW; 6308576067A22438 CRC64;
MTKRKLRNNW IIVTTMITFV TIFLFCLIII FFLKDTLHNS ELDDAERSSS DINNLFHSKP
VKDISALDLN ASLGNFQEII IYDEHNNKLF ETSNDNTVRV EPGYEHRYFD RVIKKRYKGI
EYLIIKEPIT 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
