TCMPB_STRMU
ID TCMPB_STRMU Reviewed; 301 AA.
AC Q8DUY3;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=Putative two-component membrane permease complex subunit SMU_747c;
GN OrderedLocusNames=SMU_747c;
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_746c. {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 UPF0718 family. {ECO:0000305}.
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DR EMBL; AE014133; AAN58471.1; -; Genomic_DNA.
DR RefSeq; NP_721165.1; NC_004350.2.
DR RefSeq; WP_002263631.1; NC_004350.2.
DR AlphaFoldDB; Q8DUY3; -.
DR STRING; 210007.SMU_747c; -.
DR DNASU; 1029471; -.
DR EnsemblBacteria; AAN58471; AAN58471; SMU_747c.
DR KEGG; smu:SMU_747c; -.
DR PATRIC; fig|210007.7.peg.661; -.
DR eggNOG; COG0701; Bacteria.
DR HOGENOM; CLU_039914_2_0_9; -.
DR OMA; IPMYICA; -.
DR PhylomeDB; Q8DUY3; -.
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; IPR005524; DUF318.
DR Pfam; PF03773; ArsP_1; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..301
FT /note="Putative two-component membrane permease complex
FT subunit SMU_747c"
FT /id="PRO_0000426729"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 211..231
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 301 AA; 33274 MW; E4C0A39AFA683F3E CRC64;
MAIFNHLPSS VLQCLAIFLS IIIEALPFIL LGAILSGFIE VYLTPDIVQK YLPKNKIGRI
LFGTFVGFIF PSCECGIVPI VNRFLEKKVP SYTAIPFLAT APIINPIVLF ATFSAFGNSW
RFVFLRLFGA IIVAISLGIL LGFIVDEHII KESAKPCHFH DYSHKKAYQK IFYALAHAVD
ELFDTGRYLI FGSFVAASMQ IYVPTRILTS IGHNPLTAIL IMMLLAFILS LCSEADAFIG
TSLLATFGVA PVVAFLLIGP MVDIKNLMMM KNAFKTKFIL QFVGTSSLII IIYCLIVGVM
Q