DLTS_STRA5
ID DLTS_STRA5 Reviewed; 395 AA.
AC Q8DXQ8;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=Sensor protein DltS;
DE EC=2.7.13.3;
GN Name=dltS; OrderedLocusNames=SAG1791;
OS Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=208435;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-611 / 2603 V/R;
RX PubMed=12200547; DOI=10.1073/pnas.182380799;
RA Tettelin H., Masignani V., Cieslewicz M.J., Eisen J.A., Peterson S.N.,
RA Wessels M.R., Paulsen I.T., Nelson K.E., Margarit I., Read T.D.,
RA Madoff L.C., Wolf A.M., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Lewis M.R., Radune D.,
RA Fedorova N.B., Scanlan D., Khouri H.M., Mulligan S., Carty H.A.,
RA Cline R.T., Van Aken S.E., Gill J., Scarselli M., Mora M., Iacobini E.T.,
RA Brettoni C., Galli G., Mariani M., Vegni F., Maione D., Rinaudo D.,
RA Rappuoli R., Telford J.L., Kasper D.L., Grandi G., Fraser C.M.;
RT "Complete genome sequence and comparative genomic analysis of an emerging
RT human pathogen, serotype V Streptococcus agalactiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:12391-12396(2002).
CC -!- FUNCTION: Member of the two-component regulatory system DltS/DltR.
CC Regulates the expression of the dlt operon. Probably phosphorylates
CC DltR (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:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
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DR EMBL; AE009948; AAN00654.1; -; Genomic_DNA.
DR RefSeq; NP_688781.1; NC_004116.1.
DR RefSeq; WP_000490535.1; NC_004116.1.
DR AlphaFoldDB; Q8DXQ8; -.
DR SMR; Q8DXQ8; -.
DR STRING; 208435.SAG1791; -.
DR EnsemblBacteria; AAN00654; AAN00654; SAG1791.
DR GeneID; 66886630; -.
DR KEGG; sag:SAG1791; -.
DR PATRIC; fig|208435.3.peg.1799; -.
DR HOGENOM; CLU_000445_89_6_9; -.
DR OMA; KFVLINM; -.
DR Proteomes; UP000000821; 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; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix; Two-component regulatory system.
FT CHAIN 1..395
FT /note="Sensor protein DltS"
FT /id="PRO_0000074731"
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"
SQ SEQUENCE 395 AA; 45764 MW; 6FEDFE55E5A2CC15 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
SAIQFSLKQA RRKAILTISN PSAIYSKEVM DNLFERFYQA KDDHADSLSF GLGLSIAKAI
VERHKGRIRA YQEKDQLRLE VQLPIDGFWT NTMIN