MSMK_STRMU
ID MSMK_STRMU Reviewed; 377 AA.
AC Q00752;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Multiple sugar-binding transport ATP-binding protein MsmK;
GN Name=msmK; OrderedLocusNames=SMU_882;
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 Probably responsible for energy coupling to the transport system.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Peripheral membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR EMBL; M77351; AAA26938.1; -; Genomic_DNA.
DR EMBL; AE014133; AAN58597.1; -; Genomic_DNA.
DR PIR; E42400; E42400.
DR RefSeq; NP_721291.1; NC_004350.2.
DR RefSeq; WP_002262876.1; NC_004350.2.
DR AlphaFoldDB; Q00752; -.
DR SMR; Q00752; -.
DR STRING; 210007.SMU_882; -.
DR TCDB; 3.A.1.1.28; the atp-binding cassette (abc) superfamily.
DR PRIDE; Q00752; -.
DR EnsemblBacteria; AAN58597; AAN58597; SMU_882.
DR KEGG; smu:SMU_882; -.
DR PATRIC; fig|210007.7.peg.788; -.
DR eggNOG; COG3842; Bacteria.
DR HOGENOM; CLU_000604_1_1_9; -.
DR OMA; PRNMYDK; -.
DR PhylomeDB; Q00752; -.
DR Proteomes; UP000002512; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR CDD; cd03301; ABC_MalK_N; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR015855; ABC_transpr_MalK-like.
DR InterPro; IPR008995; Mo/tungstate-bd_C_term_dom.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR040582; OB_MalK.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005116; Transp-assoc_OB_typ1.
DR Pfam; PF00005; ABC_tran; 1.
DR Pfam; PF17912; OB_MalK; 1.
DR Pfam; PF03459; TOBE; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF50331; SSF50331; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Membrane; Nucleotide-binding;
KW Reference proteome; Sugar transport; Transport.
FT CHAIN 1..377
FT /note="Multiple sugar-binding transport ATP-binding protein
FT MsmK"
FT /id="PRO_0000092612"
FT DOMAIN 4..246
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 38..45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 377 AA; 41964 MW; 640FAD092289736A CRC64;
MVELNLNHIY KKYPNSSHYS VEDFDLDIKN KEFIVFVGPS GCGKSTTLRM VAGLEDITKG
ELKIDGEVVN DKAPKDRDIA MVFQNYALYP HMSVYDNMAF GLKLRHYSKE AIDKRVKEAA
QILGLTEFLE RKPADLSGGQ RQRVAMGRAI VRDAKVFLMD EPLSNLDAKL RVSMRAEIAK
IHRRIGATTI YVTHDQTEAM TLADRIVIMS STKNEDGSGT IGRVEQVGTP QELYNRPANK
FVAGFIGSPA MNFFDVTIKD GHLVSKDGLT IAVTEGQLKM LESKGFKNKN LIFGIRPEDI
SSSLLVQETY PDATVDAEVV VSELLGSETM LYLKLGQTEF AARVDARDFH EPGEKVSLTF
NVAKGHFFDA ETEAAIR