ARLS_STAS1
ID ARLS_STAS1 Reviewed; 451 AA.
AC Q49XM6;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, 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=SSP1324;
OS Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM
OS 20229 / NCIMB 8711 / NCTC 7292 / S-41).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=342451;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41;
RX PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M.,
RA Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.;
RT "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT pathogenesis of uncomplicated urinary tract infection.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(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; AP008934; BAE18469.1; -; Genomic_DNA.
DR RefSeq; WP_011303105.1; NZ_MTGA01000038.1.
DR AlphaFoldDB; Q49XM6; -.
DR SMR; Q49XM6; -.
DR STRING; 342451.SSP1324; -.
DR EnsemblBacteria; BAE18469; BAE18469; SSP1324.
DR KEGG; ssp:SSP1324; -.
DR PATRIC; fig|342451.11.peg.1327; -.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000445_89_6_9; -.
DR OMA; TVIGNFR; -.
DR OrthoDB; 692375at2; -.
DR Proteomes; UP000006371; 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..451
FT /note="Signal transduction histidine-protein kinase ArlS"
FT /id="PRO_0000293452"
FT TRANSMEM 12..32
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; 52423 MW; 0750F2CF493D1AC8 CRC64;
MKQRKLKTKW MLITTTITFL TIFLFSIIII FFLSNSLRHN EVDEAERSSE DIVKLFESKQ
IEHVTPLDLN ASLGNFQKVM LFNEDGHKLM ETSNDNSITF SPNIVPTNVN RIAVKSDHKK
DYLIITDHIE SPKFNGYSVI VHSLEDYKAL VNSLYFIALI FGVIATFITA IISYFFSSQI
TKPLILMSNK MQQIRRDGFQ EKVELSTNYE ETDNLIVTFN EMMLQLEESF NQQRQFVEDA
SHELRTPLQI IQGHLNLINR WGKKDAAILE ESLDISLEEM TRITKLVEEL LLLTKDNNNS
RDGEIENVEI NQEIASRIKS LSQLHSDYTF EFDAFPKPLN IKIDRYQFEQ MLIIFIDNAM
KYDQINKYIQ IQTKLRNKQI SIEITDHGVG IPKEDIEFIF DRFYRVDKSR SRKLGGNGLG
LSIAKKIIEL NNGTIHVDSE VDKYTTFKIT F