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   25-MAY-2022, entry version 121.
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; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC1435;
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., Lee J.C.,
RA   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. ArlS
CC       probably functions as a sensor protein kinase which is
CC       autophosphorylated at a histidine residue and transfers its phosphate
CC       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; AP006716; BAE04800.1; -; Genomic_DNA.
DR   RefSeq; WP_011275786.1; NC_007168.1.
DR   AlphaFoldDB; Q4L6C5; -.
DR   SMR; Q4L6C5; -.
DR   STRING; 279808.SH1491; -.
DR   EnsemblBacteria; BAE04800; BAE04800; SH1491.
DR   KEGG; sha:SH1491; -.
DR   eggNOG; COG5002; Bacteria.
DR   HOGENOM; CLU_000445_89_6_9; -.
DR   OMA; TVIGNFR; -.
DR   OrthoDB; 692375at2; -.
DR   Proteomes; UP000000543; 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.
FT   CHAIN           1..453
FT                   /note="Signal transduction histidine-protein kinase ArlS"
FT                   /id="PRO_0000293451"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        157..177
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          179..232
FT                   /note="HAMP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT   DOMAIN          240..453
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   MOD_RES         243
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
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