ID   MTSA_STRGN              Reviewed;         310 AA.
AC   P42364;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Manganese ABC transporter substrate-binding lipoprotein {ECO:0000305};
DE   AltName: Full=Coaggregation-mediating adhesin {ECO:0000303|PubMed:7927711};
DE   Flags: Precursor;
GN   Name=scaA {ECO:0000303|PubMed:7927711};
OS   Streptococcus gordonii.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1302;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=ATCC 51656 / PK488;
RX   PubMed=7927711; DOI=10.1128/iai.62.10.4469-4480.1994;
RA   Kolenbrander P.E., Andersen R.N., Ganeshkumar N.;
RT   "Nucleotide sequence of the Streptococcus gordonii PK488 coaggregation
RT   adhesin gene, scaA, and ATP-binding cassette.";
RL   Infect. Immun. 62:4469-4480(1994).
RN   [2]
RP   FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 51656 / PK488, and
RC   Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288;
RX   PubMed=9440518; DOI=10.1128/jb.180.2.290-295.1998;
RA   Kolenbrander P.E., Andersen R.N., Baker R.A., Jenkinson H.F.;
RT   "The adhesion-associated sca operon in Streptococcus gordonii encodes an
RT   inducible high-affinity ABC transporter for Mn2+ uptake.";
RL   J. Bacteriol. 180:290-295(1998).
CC   -!- FUNCTION: Part of the high-affinity ABC transporter complex ScaABC
CC       involved in manganese import. Essential for growth under Mn(2+)-
CC       limiting conditions (PubMed:9440518). Also acts as an adhesin which is
CC       involved on adherence to extracellular matrix. It is an important
CC       factor in pathogenesis and infection (PubMed:7927711).
CC       {ECO:0000269|PubMed:7927711, ECO:0000269|PubMed:9440518}.
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (ScaC),
CC       two transmembrane proteins (ScaB) and a solute-binding protein (ScaA).
CC       {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC       ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC   -!- INDUCTION: Induced at low concentrations of extracellular Mn(2+) and by
CC       the addition of Zn(2+). {ECO:0000269|PubMed:9440518}.
CC   -!- DISRUPTION PHENOTYPE: Inactivation of the gene results in both impaired
CC       growth and strong inhibition of Mn(2+) uptake.
CC       {ECO:0000269|PubMed:9440518}.
CC   -!- SIMILARITY: Belongs to the bacterial solute-binding protein 9 family.
CC       Lipoprotein receptor antigen (Lrai) subfamily. {ECO:0000305}.
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DR   EMBL; L11577; AAA71947.1; -; Genomic_DNA.
DR   PIR; T11551; T11551.
DR   AlphaFoldDB; P42364; -.
DR   SMR; P42364; -.
DR   TCDB; 3.A.1.15.2; the atp-binding cassette (abc) superfamily.
DR   PRIDE; P42364; -.
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   2: Evidence at transcript level;
KW   Cell membrane; Lipoprotein; Manganese; Membrane; Metal-binding; Palmitate;
KW   Signal; Transport; Zinc.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           20..310
FT                   /note="Manganese ABC transporter substrate-binding
FT                   lipoprotein"
FT                   /id="PRO_0000031886"
FT   BINDING         68
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         140
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         206
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         281
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"
SQ   SEQUENCE   310 AA;  34788 MW;  D1DEAB1A060BC252 CRC64;
     MKKCRFLVLL LLAFVGLAAC SSQKSSTDSS SSKLNVVATN SIIADITKNI AGDKINLHSI
     VPVGQDPHKY EPLPEDVKKT SKADLIFYNG INLETGGNAW FTKLVENAQK KENKDYYAVS
     EGVDVIYLEG QNEKGKEDPH AWLNLENGII YAQNIAKRLI EKDPDNKATY EKNLKAYIEK
     LTALDKEAKE KFNNIPEEKK MIVTSEGCPK YFSKAYNVPS AYIWEINTEE EGTPDQIKSL
     VEKLRKTKVP SLFVESSVDD RPMKTVSKDT NIPIYAKIFT DSIAEKGEDG DSYYSMMKYN
     LDKISEGLAK