MSMG_STRMU
ID MSMG_STRMU Reviewed; 277 AA.
AC Q00751;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 25-MAY-2022, entry version 119.
DE RecName: Full=Multiple sugar-binding transport system permease protein MsmG;
GN Name=msmG; OrderedLocusNames=SMU_880;
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: Involved in a binding protein-dependent transport system
CC responsible for the uptake of melibiose, raffinose and isomaltotriose.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. MalFG subfamily. {ECO:0000305}.
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DR EMBL; M77351; AAA26936.1; -; Genomic_DNA.
DR EMBL; AE014133; AAN58595.1; -; Genomic_DNA.
DR PIR; B27626; B27626.
DR PIR; D42400; D42400.
DR RefSeq; NP_721289.1; NC_004350.2.
DR RefSeq; WP_002262874.1; NC_004350.2.
DR AlphaFoldDB; Q00751; -.
DR SMR; Q00751; -.
DR STRING; 210007.SMU_880; -.
DR TCDB; 3.A.1.1.28; the atp-binding cassette (abc) superfamily.
DR EnsemblBacteria; AAN58595; AAN58595; SMU_880.
DR GeneID; 66817684; -.
DR KEGG; smu:SMU_880; -.
DR PATRIC; fig|210007.7.peg.786; -.
DR eggNOG; COG0395; Bacteria.
DR HOGENOM; CLU_016047_1_2_9; -.
DR OMA; YIVFQRQ; -.
DR PhylomeDB; Q00751; -.
DR Proteomes; UP000002512; 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:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR CDD; cd06261; TM_PBP2; 1.
DR Gene3D; 1.10.3720.10; -; 1.
DR InterPro; IPR000515; MetI-like.
DR InterPro; IPR035906; MetI-like_sf.
DR Pfam; PF00528; BPD_transp_1; 1.
DR SUPFAM; SSF161098; SSF161098; 1.
DR PROSITE; PS50928; ABC_TM1; 1.
PE 3: Inferred from homology;
KW Cell membrane; Membrane; Reference proteome; Sugar transport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..277
FT /note="Multiple sugar-binding transport system permease
FT protein MsmG"
FT /id="PRO_0000060118"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 69..263
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ SEQUENCE 277 AA; 31654 MW; C6B6D5C2F805B61A CRC64;
MKKEEKINYF WKYVLLTVGG ILILIPLMVT VFSSFKKTKD IMNHFFAFPN PITLDNYKRL
LADGVGGYFW NSTVITVLSV LVVMLFIPAA AYSIARNMSR RKAFNIMYSL LILGIFVPFQ
VIMIPITVMM SKLGLANMWG LIILYLTYAI PQTLFLYVGY IKLSVPDSLD EAAEIDGADK
LTTYRKIIFP MLKPMHATTL IINALWFWND FMLPLLILNK DSSMWTLPLF QYNYSGQYFN
DYGPSFASYI VGIITITIVY LIFQKHIIAG MSNGAVK