ID   ARLS_STAEQ              Reviewed;         456 AA.
AC   Q5HPC4;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=Signal transduction histidine-protein kinase ArlS;
DE            EC=2.7.13.3;
GN   Name=arlS; OrderedLocusNames=SERP0988;
OS   Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35984 / RP62A;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(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; CP000029; AAW54342.1; -; Genomic_DNA.
DR   RefSeq; WP_002446426.1; NC_002976.3.
DR   AlphaFoldDB; Q5HPC4; -.
DR   SMR; Q5HPC4; -.
DR   STRING; 176279.SERP0988; -.
DR   EnsemblBacteria; AAW54342; AAW54342; SERP0988.
DR   KEGG; ser:SERP0988; -.
DR   eggNOG; COG5002; Bacteria.
DR   HOGENOM; CLU_000445_89_6_9; -.
DR   OMA; TVIGNFR; -.
DR   OrthoDB; 692375at2; -.
DR   Proteomes; UP000000531; 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; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix; Two-component regulatory system.
FT   CHAIN           1..456
FT                   /note="Signal transduction histidine-protein kinase ArlS"
FT                   /id="PRO_0000293450"
FT   TRANSMEM        13..33
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..456
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   456 AA;  52883 MW;  BF6EEFFE13E92013 CRC64;
     MIKRQKLKYK WMLITTLITF TTILLFCLII IFFLKDTLRS SEIDEAERSS NDIANLFHSK
     SLSDISALDL NASLENFQEI LIYDDKGRKL IQTSNDNTLA YDNKIDFKHP ERIHIHRSHG
     INYLVITEPI RSKEFSGYSV LVHSLQNYDN LVKSLYIVAL AFGLIATIIT AGVSYIFSSQ
     ITKPIVTMSN KMNQIRRDGF QNKLELTTNY EETDNLIDTF NEMMYQIEES FNQQRQFVED
     ASHELRTPLQ IIQGHLNLIQ RWGKKDPAVL EESLNISIEE VNRITKLVEE LLLLTKDRVN
     HNVLECENVD INSEIQSRVK SLQHLHPDYT FETHLATKPI QLKINRHQFE QLLLIFIDNA
     MKYDTEHKHI KIVTQLKNKM IMIDITDHGM GIPKADLEFI FDRFYRVDKS RARSQGGNGL
     GLSIAEKIVQ LNGGMIQVES ELQNYTTFKI SFPVLN