MSMF_STRMU
ID MSMF_STRMU Reviewed; 290 AA.
AC Q00750;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2002, sequence version 2.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=Multiple sugar-binding transport system permease protein MsmF;
GN Name=msmF; OrderedLocusNames=SMU_879;
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; AAA26935.1; -; Genomic_DNA.
DR EMBL; AE014133; AAN58594.1; -; Genomic_DNA.
DR PIR; C42400; C42400.
DR RefSeq; NP_721288.1; NC_004350.2.
DR RefSeq; WP_002262873.1; NC_004350.2.
DR AlphaFoldDB; Q00750; -.
DR SMR; Q00750; -.
DR STRING; 210007.SMU_879; -.
DR TCDB; 3.A.1.1.28; the atp-binding cassette (abc) superfamily.
DR EnsemblBacteria; AAN58594; AAN58594; SMU_879.
DR GeneID; 66817685; -.
DR KEGG; smu:SMU_879; -.
DR PATRIC; fig|210007.7.peg.785; -.
DR eggNOG; COG1175; Bacteria.
DR HOGENOM; CLU_016047_0_0_9; -.
DR OMA; WLAYPFM; -.
DR PhylomeDB; Q00750; -.
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..290
FT /note="Multiple sugar-binding transport system permease
FT protein MsmF"
FT /id="PRO_0000060117"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 231..253
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 70..281
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT CONFLICT 40
FT /note="T -> I (in Ref. 1; AAA26935)"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="L -> S (in Ref. 1; AAA26935)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 290 AA; 31917 MW; 7EF61595A899E7FD CRC64;
MTIRKVLNKY WGWTFLIVPL ILQVVFFYFP MFQGAFYSFT NWTGLTYNFD FVGINNYKIL
MTDGKFMKAI GFTLVLTLAL IVGEIVLGII IARALNAKIK GKTFFRAWFF FPAVLSGLTV
SLIFKQVFNY GLPAVGSALG IKFLETSMLG TANGAVIASI FVLLWQGVAM PIILFLSGLQ
SIPSEIVEAA AIDGADSKQT FWSVELPYLL PSISMVFIMA LKAGLTAFDQ IFALTGGGPN
NSTTSLGLLV YNYAFKSNQY GYANAIALIL FIIIGIVSVL QIKLSKKFEV