ID   TCMPA_STRMU             Reviewed;         271 AA.
AC   Q8DUY4;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Putative two-component membrane permease complex subunit SMU_746c;
GN   OrderedLocusNames=SMU_746c;
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 [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).
RN   [2]
RP   FUNCTION, SUBUNIT, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 700610 / UA159;
RX   PubMed=24142257; DOI=10.1128/jb.00960-13;
RA   Krol J.E., Biswas S., King C., Biswas I.;
RT   "SMU.746-SMU.747, a putative membrane permease complex, is involved in
RT   aciduricity, acidogenesis, and biofilm formation in Streptococcus mutans.";
RL   J. Bacteriol. 196:129-139(2014).
CC   -!- FUNCTION: Could be part of a two-component membrane permease system
CC       responsible for amino acid transport under low pH. Involved in
CC       acidogenesis, biofilm formation and low-pH survival.
CC       {ECO:0000269|PubMed:24142257}.
CC   -!- SUBUNIT: Interacts with SMU_747c. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: SMU_746c-SMU_747c deletion affects biofilm
CC       formation in a medium- and pH-dependent manner. Mutants show a reduced
CC       ability to grow in acidified medium, but they survive both short-term
CC       or long-term acid stress. Mutants have lower glycolytic activity.
CC       Deletion does not affect membrane proton permeability.
CC       {ECO:0000269|PubMed:24142257}.
CC   -!- SIMILARITY: Belongs to the UPF0703 family. {ECO:0000305}.
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DR   EMBL; AE014133; AAN58470.1; -; Genomic_DNA.
DR   RefSeq; NP_721164.1; NC_004350.2.
DR   RefSeq; WP_002263632.1; NC_004350.2.
DR   AlphaFoldDB; Q8DUY4; -.
DR   SMR; Q8DUY4; -.
DR   STRING; 210007.SMU_746c; -.
DR   PRIDE; Q8DUY4; -.
DR   EnsemblBacteria; AAN58470; AAN58470; SMU_746c.
DR   GeneID; 66817807; -.
DR   KEGG; smu:SMU_746c; -.
DR   PATRIC; fig|210007.7.peg.660; -.
DR   eggNOG; COG3689; Bacteria.
DR   HOGENOM; CLU_070027_1_0_9; -.
DR   OMA; YINMKYS; -.
DR   PhylomeDB; Q8DUY4; -.
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:0006865; P:amino acid transport; IEA:UniProtKB-KW.
DR   InterPro; IPR015402; DUF1980.
DR   PANTHER; PTHR40047; PTHR40047; 1.
DR   Pfam; PF09323; DUF1980; 1.
DR   TIGRFAMs; TIGR03943; TIGR03943; 1.
PE   1: Evidence at protein level;
KW   Amino-acid transport; Cell membrane; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..271
FT                   /note="Putative two-component membrane permease complex
FT                   subunit SMU_746c"
FT                   /id="PRO_0000426728"
FT   TRANSMEM        34..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        70..90
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   271 AA;  30839 MW;  52EB6D559B12B9AF CRC64;
     MIRFLILAGY FELGMYLQLS GKLDRYINSH YSYLAYISMA LSFILALVQL TIWMKRLKMH
     SHLSGKAAKF FSPIILAIPV FIGLLVPTVP LDSTTVSAKG YHFPLAAGST TSGTSSDGTR
     VQYLKPDTSL YFTKSAYQKE MRATLKKYKG SGKLQITTQN YMEVMEIIYL FPDEFKNRQI
     EYVGFIYNDP KDKNSQFLFR FGIIHCIADS GVYGLLTTGG QTHYQNNTWV TVSGKLAIEY
     NQNLKQTLPV LHISQSSQTM QPKNPYVYRV F