ID   ARLS_STAHJ              Reviewed;         453 AA.
AC   Q4L6C5;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   16-JUN-2009, entry version 33.
DE   RecName: Full=Signal transduction histidine-protein kinase arlS;
DE            EC=2.7.13.3;
GN   Name=arlS; OrderedLocusNames=SH1491;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16237012; DOI=10.1128/JB.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S.,
RA   Lee J.C., Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(2005).
CC   -!- FUNCTION: Member of the two-component regulatory system arlS/arlR.
CC       ArlS probably functions as a sensor protein kinase which is
CC       autophosphorylated at a histidine residue and transfers its
CC       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; AP006716; BAE04800.1; -; Genomic_DNA.
DR   RefSeq; YP_253406.1; -.
DR   GeneID; 3482387; -.
DR   GenomeReviews; AP006716_GR; SH1491.
DR   KEGG; sha:SH1491; -.
DR   NMPDR; fig|279808.3.peg.2138; -.
DR   HOGENOM; Q4L6C5; -.
DR   OMA; Q4L6C5; FIDNAMK.
DR   BioCyc; SHAE279808:SH1491-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: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; 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.
FT   CHAIN         1    453       Signal transduction histidine-protein
FT                                kinase arlS.
FT                                /FTId=PRO_0000293451.
FT   TRANSMEM     14     34       Potential.
FT   TRANSMEM    157    177       Potential.
FT   DOMAIN      179    232       HAMP.
FT   DOMAIN      240    453       Histidine kinase.
FT   MOD_RES     243    243       Phosphohistidine; by autocatalysis (By
FT                                similarity).
SQ   SEQUENCE   453 AA;  52861 MW;  D8021E99B1E335BF CRC64;
     MIKKGTLKYK WMMITTLIMF STIILFCLVI IFFLKDTLRD GEIDEAEHSS SEIVNLVESR
     SMNNITTLDL TAMLENFEKA IIYDRNGKQL MQSSNENMIN FKPDIDFVDP ETIQISKHNG
     IPYLIITEPI HSERFEGYSV LIHSLEGYNN VVRSLYFVAI AFGLLATFIM AGISYIFSTQ
     LTKPLVTMSN KMIQIRRDGF QNKLELKTNY EETDNLIDTF NDMMYQIEES FNQQRQFVED
     ASHELRTPLQ IIQGHLNLIQ RWGKKDPAVL EESLNISLEE MNRITKLVEE LLLLTKDKVN
     IQALEFEEVN INEEIRSRIK SLKQLHPDYQ FKTHLSKKPL TLQINRHQFE QLLLIFIDNA
     MKYDKDNKQI EIATQLRNKQ ISIEITDHGL GIPKEDQEFI FDRFYRVDKS RSRSQGGNGL
     GLFIAEKIVQ QYGGYITVDS EVNQYTTFKI IFK
//