ID   DLTS_STRA3              Reviewed;         395 AA.
AC   Q8E3C7; Q8VM68;
DT   23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 113.
DE   RecName: Full=Sensor protein DltS;
DE            EC=2.7.13.3;
GN   Name=dltS; OrderedLocusNames=gbs1834;
OS   Streptococcus agalactiae serotype III (strain NEM316).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=211110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NEM316;
RX   PubMed=11591677; DOI=10.1128/jb.183.21.6324-6334.2001;
RA   Poyart C., Lamy M.C., Boumaila C., Fiedler F., Trieu-Cuot P.;
RT   "Regulation of D-alanyl-lipoteichoic acid biosynthesis in Streptococcus
RT   agalactiae involves a novel two-component regulatory system.";
RL   J. Bacteriol. 183:6324-6334(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NEM316;
RX   PubMed=12354221; DOI=10.1046/j.1365-2958.2002.03126.x;
RA   Glaser P., Rusniok C., Buchrieser C., Chevalier F., Frangeul L., Msadek T.,
RA   Zouine M., Couve E., Lalioui L., Poyart C., Trieu-Cuot P., Kunst F.;
RT   "Genome sequence of Streptococcus agalactiae, a pathogen causing invasive
RT   neonatal disease.";
RL   Mol. Microbiol. 45:1499-1513(2002).
CC   -!- FUNCTION: Member of the two-component regulatory system DltS/DltR.
CC       Regulates the expression of the dlt operon. Probably phosphorylates
CC       DltR.
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:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
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DR   EMBL; AJ291784; CAC83084.1; -; Genomic_DNA.
DR   EMBL; AL766853; CAD47493.1; -; Genomic_DNA.
DR   RefSeq; WP_000490537.1; NC_004368.1.
DR   AlphaFoldDB; Q8E3C7; -.
DR   SMR; Q8E3C7; -.
DR   STRING; 211110.gbs1834; -.
DR   EnsemblBacteria; CAD47493; CAD47493; CAD47493.
DR   KEGG; san:gbs1834; -.
DR   eggNOG; COG5002; Bacteria.
DR   HOGENOM; CLU_000445_89_6_9; -.
DR   OMA; KFVLINM; -.
DR   Proteomes; UP000000823; 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; 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   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SUPFAM; SSF47384; SSF47384; 1.
DR   SUPFAM; SSF55874; SSF55874; 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..395
FT                   /note="Sensor protein DltS"
FT                   /id="PRO_0000074730"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        136..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          177..387
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   MOD_RES         180
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   CONFLICT        302
FT                   /note="E -> A (in Ref. 1; CAC83084)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   395 AA;  45822 MW;  038738FF25A68811 CRC64;
     MFSDLRKKFV FLTMSILIVV VLFLFAVSNR YNQYWDEYDA YRIVKLVAKN DYLGIPGDEP
     IALVTIDNQK MVKIQSNNTD LTNDVIEKSS LKLLEQGKKS RKWKSFIYSI KEYKDKTYTI
     AIMDLASYEV PYARRFLILV FTIFGFCLLA AVSLYLSRFI VGPVETEMTR EKQFVSDASH
     ELKTPIAAIR ANVQVLEQQI PGNRYLDHVV SETKRMEFLI EDLLNLSRLD EKRSKVNFKK
     LNLSVLCQEV LLTYESLAYE EEKCLNDTIE DDVWIVGEES QIKQILIILL DNAIRHSLSK
     SEIQFSLKQA RRKAILTISN PSAIYSKEVM DNLFERFYQA KDDHADSLSF GLGLSIAKAI
     VERHKGRIRA YQEKDQLRLE VQLPIDGFWT NTMIN