ARLS_STAES
ID ARLS_STAES Reviewed; 456 AA.
AC Q8CSL7;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 114.
DE RecName: Full=Signal transduction histidine-protein kinase ArlS;
DE EC=2.7.13.3;
GN Name=arlS; OrderedLocusNames=SE_1099;
OS Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176280;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12228 / FDA PCI 1200;
RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT "Genome-based analysis of virulence genes in a non-biofilm-forming
RT Staphylococcus epidermidis strain (ATCC 12228).";
RL Mol. Microbiol. 49:1577-1593(2003).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE015929; AAO04696.1; -; Genomic_DNA.
DR RefSeq; NP_764654.1; NC_004461.1.
DR RefSeq; WP_001831043.1; NZ_WBME01000002.1.
DR AlphaFoldDB; Q8CSL7; -.
DR SMR; Q8CSL7; -.
DR STRING; 176280.SE_1099; -.
DR EnsemblBacteria; AAO04696; AAO04696; SE_1099.
DR GeneID; 50018776; -.
DR KEGG; sep:SE_1099; -.
DR PATRIC; fig|176280.10.peg.1074; -.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000445_89_6_9; -.
DR OMA; TVIGNFR; -.
DR Proteomes; UP000001411; 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..456
FT /note="Signal transduction histidine-protein kinase ArlS"
FT /id="PRO_0000293449"
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; 52860 MW; 8ACF8A6CF9D7F77B CRC64;
MIKRQKLKYK WMLITTLITF TTILLFCLII IFFLKDTLRS SEIDEAERSS NDIANLFHSK
SLSDISALDL NASLENFQEI LIYDDKGRKL IQTSNDNTLA YDNKIDFKHP ERIHIQRSHG
INYLVITEPI RSKDFSGYSV LVHSLQNYDN LVKSLYIVAL AFGLIATIIT AGVSYIFSSQ
ITKPIVTMSN KMNQIRRDGF QNKLELTTNY EETDNLIDTF NEMMYQIEES FNQQRQFVED
ASHELRTPLQ IIQGHLNLIQ RWGKKDPAVL EESLNISIEE VNRITKLVEE LLLLTKDRVN
HNVLECENVD VNSEIQSRVK SLQHLHPDYT FETHLATKPI QLKINRHQFE QLLLIFIDNA
MKYDTEHKHI KIVTQLKNKM IMIDITDHGM GIPKADLEFI FDRFYRVDKS RARSQGGNGL
GLSIAEKIVQ LNGGMIQVES ELQKYTTFKI SFPVLN