ID   ABCX_STRMU              Reviewed;         260 AA.
AC   P72477; O06943;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Putative ABC transporter ATP-binding protein;
GN   Name=abcX; OrderedLocusNames=SMU_1695;
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=LT11;
RA   Boyd D.A., Hamilton I.R.;
RL   Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=LT11;
RX   PubMed=11029425; DOI=10.1128/jb.182.21.6055-6065.2000;
RA   Boyd D.A., Cvitkovitch D.G., Bleiweis A.S., Kiriukhin M.Y., Debabov D.V.,
RA   Neuhaus F.C., Hamilton I.R.;
RT   "Defects in D-alanyl-lipoteichoic acid synthesis in Streptococcus mutans
RT   results in acid sensitivity.";
RL   J. Bacteriol. 182:6055-6065(2000).
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 100-158.
RC   STRAIN=GS-5;
RA   Peruzzi F., Piggot P.J., Daneo-Moore L.;
RL   Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR   EMBL; U94990; AAC04616.1; -; Genomic_DNA.
DR   EMBL; AF051356; AAC05770.1; -; Genomic_DNA.
DR   EMBL; AE014133; AAN59332.1; -; Genomic_DNA.
DR   EMBL; U75475; AAB41193.1; -; Genomic_DNA.
DR   RefSeq; NP_722026.1; NC_004350.2.
DR   RefSeq; WP_002262577.1; NC_004350.2.
DR   AlphaFoldDB; P72477; -.
DR   SMR; P72477; -.
DR   STRING; 210007.SMU_1695; -.
DR   PRIDE; P72477; -.
DR   EnsemblBacteria; AAN59332; AAN59332; SMU_1695.
DR   KEGG; smu:SMU_1695; -.
DR   PATRIC; fig|210007.7.peg.1515; -.
DR   eggNOG; COG1119; Bacteria.
DR   HOGENOM; CLU_000604_1_11_9; -.
DR   OMA; HVLMIRQ; -.
DR   PhylomeDB; P72477; -.
DR   Proteomes; UP000002512; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:UniProt.
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; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 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; Nucleotide-binding; Reference proteome; Transport.
FT   CHAIN           1..260
FT                   /note="Putative ABC transporter ATP-binding protein"
FT                   /id="PRO_0000091921"
FT   DOMAIN          4..243
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         36..43
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   CONFLICT        115
FT                   /note="D -> G (in Ref. 4; AAB41193)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        127
FT                   /note="T -> S (in Ref. 4; AAB41193)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   260 AA;  29366 MW;  35D9F7379435D198 CRC64;
     MALISMKNVT LKKQGKILLN NLNWKVKKGE NWVILGLNGS GKTTLLKLIM AEYWSTQGQV
     EILNTRFGQG DIPNMRTKIG VVGSFIAERL PANMLAEKIV LTGKYKSSIL YKEYDETELN
     EARQMLTVIG GKHLLGRIYS SLSQGEKQLL LIARSLMEDP EIIILDEATS GLDLFAREKL
     LTQVEKITEL PHAPTILYVT HHAEEITDKM SHILLLRRGK IVAQGPKKDI ITPQVLENFY
     ESPVNIISID DKRFFIKPQV