MSMR_STRMU
ID MSMR_STRMU Reviewed; 278 AA.
AC Q00753;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2002, sequence version 2.
DT 25-MAY-2022, entry version 131.
DE RecName: Full=Msm operon regulatory protein;
GN Name=msmR; OrderedLocusNames=SMU_876;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Ingbritt;
RX PubMed=1537846; DOI=10.1016/s0021-9258(18)42880-3;
RA Russell R.R.B., Aduse-Opoku J., Sutcliffe I.C., Tao L., Ferretti J.J.;
RT "A binding protein-dependent transport system in Streptococcus mutans
RT responsible for multiple sugar metabolism.";
RL J. Biol. Chem. 267:4631-4637(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
CC -!- FUNCTION: Regulatory protein for the msm operon for multiple sugar
CC metabolism. Activates the transcription of the msmEFGK, aga, dexB and
CC gftA genes.
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DR EMBL; M77351; AAA26932.1; -; Genomic_DNA.
DR EMBL; AE014133; AAN58591.1; -; Genomic_DNA.
DR RefSeq; NP_721285.1; NC_004350.2.
DR RefSeq; WP_002262870.1; NC_004350.2.
DR AlphaFoldDB; Q00753; -.
DR SMR; Q00753; -.
DR STRING; 210007.SMU_876; -.
DR DNASU; 1028226; -.
DR EnsemblBacteria; AAN58591; AAN58591; SMU_876.
DR GeneID; 66817688; -.
DR KEGG; smu:SMU_876; -.
DR PATRIC; fig|210007.7.peg.782; -.
DR eggNOG; COG2207; Bacteria.
DR HOGENOM; CLU_000445_88_6_9; -.
DR OMA; GFEDQLY; -.
DR PhylomeDB; Q00753; -.
DR Proteomes; UP000002512; Chromosome.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR InterPro; IPR003313; AraC-bd.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR037923; HTH-like.
DR InterPro; IPR018060; HTH_AraC.
DR InterPro; IPR018062; HTH_AraC-typ_CS.
DR InterPro; IPR020449; Tscrpt_reg_HTH_AraC-type.
DR Pfam; PF02311; AraC_binding; 1.
DR Pfam; PF12833; HTH_18; 1.
DR PRINTS; PR00032; HTHARAC.
DR SMART; SM00342; HTH_ARAC; 1.
DR SUPFAM; SSF46689; SSF46689; 2.
DR SUPFAM; SSF51215; SSF51215; 1.
DR PROSITE; PS00041; HTH_ARAC_FAMILY_1; 1.
DR PROSITE; PS01124; HTH_ARAC_FAMILY_2; 1.
PE 4: Predicted;
KW Activator; DNA-binding; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..278
FT /note="Msm operon regulatory protein"
FT /id="PRO_0000194540"
FT DOMAIN 176..274
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00593"
FT DNA_BIND 193..214
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00593"
FT DNA_BIND 241..264
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00593"
FT CONFLICT 4
FT /note="L -> V (in Ref. 1; AAA26932)"
FT /evidence="ECO:0000305"
FT CONFLICT 94..110
FT /note="SGSKAENILKQSSLFKR -> RVQKPKIFLSSQAFLNL (in Ref. 1;
FT AAA26932)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 278 AA; 31968 MW; 9A8E28ABEF6CCCEA CRC64;
MNILNIYNEF DINNFDLSVD HYGSEKCDRG YSFGPTIRDN YVIHFILEGK GKLTINQHTL
DLAAGDIFLL PKDISTFYQA DLQMPWSYIW IGFSGSKAEN ILKQSSLFKR FYCHSGRSSK
LFSQMMTIIQ FANTPLTSVN ELLMVGELYK LLAALIEEFP LSHLEESNSS TKAYVNQVKK
IIHSQYGSSL RVNDIAKKLN LSRSYLYKIF RKSTNLSIKE YILQVRMKRS QYLLENPKLS
IAEISNSVGF SDSLAFSKAF KNYFGKSPSK FRKEIQNN