ID ARLS_STAAM Reviewed; 451 AA.
AC Q7A2R7;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 131.
DE RecName: Full=Signal transduction histidine-protein kinase ArlS;
DE EC=2.7.13.3;
GN Name=arlS; OrderedLocusNames=SAV1414;
OS Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158878;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu50 / ATCC 700699;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
CC -!- FUNCTION: Member of the two-component regulatory system ArlS/ArlR
CC involved in the regulation of adhesion, autolysis, multidrug resistance
CC and virulence. ArlS probably functions as a sensor protein kinase which
CC is autophosphorylated at a histidine residue and transfers its
CC phosphate 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; BA000017; BAB57576.1; -; Genomic_DNA.
DR RefSeq; WP_000166801.1; NC_002758.2.
DR AlphaFoldDB; Q7A2R7; -.
DR SMR; Q7A2R7; -.
DR KEGG; sav:SAV1414; -.
DR HOGENOM; CLU_000445_89_6_9; -.
DR PhylomeDB; Q7A2R7; -.
DR Proteomes; UP000002481; Chromosome.
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; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 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 PANTHER; PTHR45528; SENSOR HISTIDINE KINASE CPXA; 1.
DR PANTHER; PTHR45528:SF9; SENSOR HISTIDINE KINASE YRKQ; 1.
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; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 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; Virulence.
FT CHAIN 1..451
FT /note="Signal transduction histidine-protein kinase ArlS"
FT /id="PRO_0000074690"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 178..231
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 239..451
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 242
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ SEQUENCE 451 AA; 52400 MW; 6308576067A22438 CRC64;
MTKRKLRNNW IIVTTMITFV TIFLFCLIII FFLKDTLHNS ELDDAERSSS DINNLFHSKP
VKDISALDLN ASLGNFQEII IYDEHNNKLF ETSNDNTVRV EPGYEHRYFD RVIKKRYKGI
EYLIIKEPIT TQDFKGYSLL IHSLENYDNI VKSLYIIALA FGVIATIITA TISYVFSTQI
TKPLVSLSNK MIEIRRDGFQ NKLQLNTNYE EIDNLANTFN EMMSQIEESF NQQRQFVEDA
SHELRTPLQI IQGHLNLIQR WGKKDPAVLE ESLNISIEEM NRIIKLVEEL LELTKGDVND
ISSEAQTVHI NDEIRSRIHS LKQLHPDYQF DTDLTSKNLE IKMKPHQFEQ LFLIFIDNAI
KYDVKNKKIK VKTRLKNKQK IIEITDHGIG IPEEDQDFIF DRFYRVDKSR SRSQGGNGLG
LSIAQKIIQL NGGSIKIKSE INKGTTFKII F
//
