ID   MTSA_STRMU              Reviewed;         306 AA.
AC   Q9KIJ3;
DT   18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2002, sequence version 2.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Metal ABC transporter substrate-binding lipoprotein;
DE   Flags: Precursor;
GN   Name=sloC; OrderedLocusNames=SMU_184;
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=ATCC 25175 / DSM 20523 / JCM 5705 / NBRC 13955 / NCIMB 702062 / NCTC
RC   10449;
RX   PubMed=10899841; DOI=10.1128/iai.68.8.4441-4451.2000;
RA   Kitten T., Munro C.L., Michalek S.M., Macrina F.L.;
RT   "Genetic characterization of a Streptococcus mutans LraI family operon and
RT   role in virulence.";
RL   Infect. Immun. 68:4441-4451(2000).
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: Part of an ATP-driven transport system for a metal; probably
CC       for manganese. Also acts as an adhesin which is involved on adherence
CC       to extracellular matrix. It is an important factor in pathogenesis and
CC       infection. It may contribute to the formation and accumulation of
CC       dental plaque.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC       ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC   -!- SIMILARITY: Belongs to the bacterial solute-binding protein 9 family.
CC       Lipoprotein receptor antigen (Lrai) subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF232688; AAF81674.1; -; Genomic_DNA.
DR   EMBL; AE014133; AAN57959.1; -; Genomic_DNA.
DR   RefSeq; NP_720653.1; NC_004350.2.
DR   RefSeq; WP_002262031.1; NC_004350.2.
DR   AlphaFoldDB; Q9KIJ3; -.
DR   SMR; Q9KIJ3; -.
DR   STRING; 210007.SMU_184; -.
DR   TCDB; 3.A.1.15.20; the atp-binding cassette (abc) superfamily.
DR   PRIDE; Q9KIJ3; -.
DR   EnsemblBacteria; AAN57959; AAN57959; SMU_184.
DR   KEGG; smu:SMU_184; -.
DR   PATRIC; fig|210007.7.peg.160; -.
DR   eggNOG; COG0803; Bacteria.
DR   HOGENOM; CLU_016838_1_1_9; -.
DR   OMA; HHVFGYL; -.
DR   PhylomeDB; Q9KIJ3; -.
DR   Proteomes; UP000002512; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   GO; GO:0030001; P:metal ion transport; IEA:InterPro.
DR   InterPro; IPR006129; AdhesinB.
DR   InterPro; IPR006128; Lipoprotein_4.
DR   InterPro; IPR006127; ZnuA-like.
DR   Pfam; PF01297; ZnuA; 1.
DR   PRINTS; PR00691; ADHESINB.
DR   PRINTS; PR00690; ADHESNFAMILY.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Lipoprotein; Manganese; Membrane; Metal-binding; Palmitate;
KW   Reference proteome; Signal; Transport; Zinc.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           20..306
FT                   /note="Metal ABC transporter substrate-binding lipoprotein"
FT                   /id="PRO_0000031888"
FT   BINDING         64
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         136
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         202
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         277
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   LIPID           20
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           20
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CONFLICT        108
FT                   /note="T -> A (in Ref. 1; AAF81674)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        302
FT                   /note="N -> D (in Ref. 1; AAF81674)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   306 AA;  34365 MW;  CDA294394F24AB29 CRC64;
     MKKLSLLLLV CLSLLGLFAC TSKKTADKKL TVVATNSIIA DITKNIAGNK VVLHSIVPVG
     RDPHEYEPLP EDVKKTSQAD VIFYNGINLE NGGNAWFTKL VKNAHKKTDK DYFAVSDSVK
     TIYLENAKEK GKEDPHAWLD LKNGIIYAKN IMKRLSEKDP KNKSYYQKNF QAYSAKLEKL
     HKVAKEKISR IPTEKKMIVT SEGCFKYFSK AYDIPSAYIW EINTEEEGTP NQIKALVKKL
     RKSRVSALFV ESSVDDRPMK TVSKDTGIPI AAKIFTDSVA KKGQAGDSYY AMMKWNIDKI
     ANGLSQ