Reviewed, UniProtKB/Swiss-Prot Q9KJN3 (ARLS_STAA8)

Names and origin

Protein names

Recommended name:
    Signal transduction histidine-protein kinase arlS
    EC=2.7.13.3

Gene names

Name:	arlS
Ordered Locus Names:	SAOUHSC_01419

Organism

Staphylococcus aureus (strain NCTC 8325) [Complete proteome] [HAMAP]

Taxonomic identifier

93061 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length	451 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Member of the two-component regulatory system arlS/arlR involved in the regulation of adhesion, autolysis, multidrug resistance and virulence. ArlS probably functions as a sensor protein kinase which is autophosphorylated at a histidine residue and transfers its phosphate group to arlR. ArlS/arlR affects expression of the multidrug resistance transporter norA and interacts with both agr (virulence accessory gene regulator) (negatively) and sarA (staphylococcal accessory regulator) (positively) to modulate several virulence factor genes, including ssp (serine protease), spa (surface protein A) and hla (alpha-hemolysin). Could inhibit biofilm development by a mechanism independent of the presence of the poly-N-acetylglucosamine (PNAG). Also, arl proteins are required for the efficient activity of DNA gyrase inhibitors and high osmolarity on spa expression. Ref.1 Ref.3 Ref.4 Ref.7 Ref.8
Catalytic activity	ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Subcellular location	Cell membrane; Multi-pass membrane protein Probable.
Induction	Activated by agr, sarA, sarV and mgrA.
Post-translational modification	Autophosphorylated Probable.
Sequence similarities	Contains 1 HAMP domain. Contains 1 histidine kinase domain.

Ontologies

Keywords
Biological process	Two-component regulatory system Virulence
Cellular component	Cell membrane Membrane
Domain	Transmembrane
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	pathogenesis Inferred from electronic annotation. Source: UniProtKB-KW peptidyl-histidine phosphorylation Inferred from electronic annotation. Source: InterPro two-component signal transduction system (phosphorelay) Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW two-component sensor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 451	451	Signal transduction histidine-protein kinase arlS		PRO_0000074688
Regions
	Transmembrane	11 – 31	21	Potential
	Transmembrane	156 – 176	21	Potential
	Domain	178 – 231	54	HAMP
	Domain	239 – 451	213	Histidine kinase
Amino acid modifications
	Modified residue	242	1	Phosphohistidine; by autocatalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9KJN3-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 6308576067A22438	FASTA	451	52,400
	10 20 30 40 50 60 MTKRKLRNNW IIVTTMITFV TIFLFCLIII FFLKDTLHNS ELDDAERSSS DINNLFHSKP 70 80 90 100 110 120 VKDISALDLN ASLGNFQEII IYDEHNNKLF ETSNDNTVRV EPGYEHRYFD RVIKKRYKGI 130 140 150 160 170 180 EYLIIKEPIT TQDFKGYSLL IHSLENYDNI VKSLYIIALA FGVIATIITA TISYVFSTQI 190 200 210 220 230 240 TKPLVSLSNK MIEIRRDGFQ NKLQLNTNYE EIDNLANTFN EMMSQIEESF NQQRQFVEDA 250 260 270 280 290 300 SHELRTPLQI IQGHLNLIQR WGKKDPAVLE ESLNISIEEM NRIIKLVEEL LELTKGDVND 310 320 330 340 350 360 ISSEAQTVHI NDEIRSRIHS LKQLHPDYQF DTDLTSKNLE IKMKPHQFEQ LFLIFIDNAI 370 380 390 400 410 420 KYDVKNKKIK VKTRLKNKQK IIEITDHGIG IPEEDQDFIF DRFYRVDKSR SRSQGGNGLG 430 440 450 LSIAQKIIQL NGGSIKIKSE INKGTTFKII F

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A new two-component regulatory system involved in adhesion, autolysis, and extracellular proteolytic activity of Staphylococcus aureus." Fournier B., Hooper D.C. J. Bacteriol. 182:3955-3964(2000) [PubMed: 10869073] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
[2]	"The Staphylococcus aureus NCTC8325 genome." Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J. Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"Expression of the multidrug resistance transporter NorA from Staphylococcus aureus is modified by a two-component regulatory system." Fournier B., Aras R., Hooper D.C. J. Bacteriol. 182:664-671(2000) [PubMed: 10633099] [Abstract] Cited for: FUNCTION.
[4]	"The two-component system ArlS-ArlR is a regulator of virulence gene expression in Staphylococcus aureus." Fournier B., Klier A., Rapoport G. Mol. Microbiol. 41:247-261(2001) [PubMed: 11454217] [Abstract] Cited for: FUNCTION, REGULATION.
[5]	"Characterization of RAT, an autolysis regulator in Staphylococcus aureus." Ingavale S.S., Van Wamel W., Cheung A.L. Mol. Microbiol. 48:1451-1466(2003) [PubMed: 12791130] [Abstract] Cited for: REGULATION BY MGRA.
[6]	"Identification of sarV (SA2062), a new transcriptional regulator, is repressed by SarA and MgrA (SA0641) and involved in the regulation of autolysis in Staphylococcus aureus." Manna A.C., Ingavale S.S., Maloney M., van Wamel W., Cheung A.L. J. Bacteriol. 186:5267-5280(2004) [PubMed: 15292128] [Abstract] Cited for: REGULATION BY SARV.
[7]	"Protein A gene expression is regulated by DNA supercoiling which is modified by the ArlS-ArlR two-component system of Staphylococcus aureus." Fournier B., Klier A. Microbiology 150:3807-3819(2004) [PubMed: 15528666] [Abstract] Cited for: FUNCTION.
[8]	"Staphylococcus aureus develops an alternative, ica-independent biofilm in the absence of the arlRS two-component system." Toledo-Arana A., Merino N., Vergara-Irigaray M., Debarbouille M., Penades J.R., Lasa I. J. Bacteriol. 187:5318-5329(2005) [PubMed: 16030226] [Abstract] Cited for: FUNCTION IN BIOFILM DEVELOPMENT.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF165314 Genomic DNA. Translation: AAF85897.1. CP000253 Genomic DNA. Translation: ABD30512.1.
RefSeq	YP_499945.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q9KJN3.
Genome annotation databases
GeneID	3920650.
GenomeReviews	Gene locus SAOUHSC_01419 in contig CP000253_GR.
KEGG	sao:SAOUHSC_01419.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q9KJN3.
OMA	FIDNAMK.
Enzyme and pathway databases
BioCyc	SAUR93061:SAOUHSC_01419-MON.
Family and domain databases
InterPro	IPR003594. ATP_bd_ATPase. IPR003660. HAMP_linker_domain. IPR004358. Sig_transdc_His_kin-like_C. IPR003661. Sig_transdc_His_kin_sub1_dim/P. IPR005467. Sig_transdc_His_kinase_core. [Graphical view]
Gene3D	G3DSA:3.30.565.10. ATP_bd_ATPase. 1 hit.
Pfam	PF00672. HAMP. 1 hit. PF02518. HATPase_c. 1 hit. PF00512. HisKA. 1 hit. [Graphical view]
PRINTS	PR00344. BCTRLSENSOR.
SMART	SM00304. HAMP. 1 hit. SM00387. HATPase_c. 1 hit. SM00388. HisKA. 1 hit. [Graphical view]
PROSITE	PS50885. HAMP. 1 hit. PS50109. HIS_KIN. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ARLS_STAA8

Accession

Primary (citable) accession number: Q9KJN3
Secondary accession number(s): Q2FYM0

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	October 1, 2000
Last modified:	November 3, 2009
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)