ID   MTSA_STRSA              Reviewed;         309 AA.
AC   P31304;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Manganese ABC transporter substrate-binding lipoprotein;
DE   AltName: Full=Adhesin B;
DE   AltName: Full=Saliva-binding protein;
DE   Flags: Precursor;
GN   Name=ssaB;
OS   Streptococcus sanguinis.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 25-53.
RC   STRAIN=12;
RX   PubMed=1671775; DOI=10.1128/iai.59.3.1093-1099.1991;
RA   Ganeshkumar N., Hannam P.M., Kolenbrander P.E., McBride B.C.;
RT   "Nucleotide sequence of a gene coding for a saliva-binding protein (SsaB)
RT   from Streptococcus sanguis 12 and possible role of the protein in
RT   coaggregation with actinomyces.";
RL   Infect. Immun. 59:1093-1099(1991).
RN   [2]
RP   SUBCELLULAR LOCATION, DIACYLGLYCEROL AT CYS-20, PALMITOYLATION AT CYS-20,
RP   AND MUTAGENESIS OF CYS-20.
RX   PubMed=8419308; DOI=10.1128/jb.175.2.572-574.1993;
RA   Ganeshkumar N., Arora N., Kolenbrander P.E.;
RT   "Saliva-binding protein (SsaB) from Streptococcus sanguis 12 is a
RT   lipoprotein.";
RL   J. Bacteriol. 175:572-574(1993).
CC   -!- FUNCTION: Part of an ATP-driven transport system for manganese. Also
CC       acts as an adhesin which is involved on adherence to extracellular
CC       matrix. It is an important factor in the pathogenesis and infection. It
CC       may contribute to the formation and accumulation of dental plaque.
CC   -!- SUBUNIT: Homodimer and homotrimer.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC       ProRule:PRU00303, ECO:0000269|PubMed:8419308}; Lipid-anchor
CC       {ECO:0000255|PROSITE-ProRule:PRU00303, ECO:0000269|PubMed:8419308}.
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; M63481; AAC98426.1; -; Genomic_DNA.
DR   PIR; A43583; A43583.
DR   AlphaFoldDB; P31304; -.
DR   SMR; P31304; -.
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   1: Evidence at protein level;
KW   Cell membrane; Direct protein sequencing; Lipoprotein; Manganese; Membrane;
KW   Metal-binding; Palmitate; Signal; Transport; Zinc.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           20..309
FT                   /note="Manganese ABC transporter substrate-binding
FT                   lipoprotein"
FT                   /id="PRO_0000031898"
FT   BINDING         67
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         139
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         205
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         280
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                   ECO:0000269|PubMed:8419308"
FT   LIPID           20
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303,
FT                   ECO:0000269|PubMed:8419308"
FT   MUTAGEN         15
FT                   /note="C->G: No loss of acylation."
FT   MUTAGEN         20
FT                   /note="C->G: Loss of acylation."
FT                   /evidence="ECO:0000269|PubMed:8419308"
SQ   SEQUENCE   309 AA;  34684 MW;  8FC8AF434AB18977 CRC64;
     MKKLGFLSLL LLAVCTLFAC SNQKNASSDS SKLKVVATNS IIADITKNIA GDKIDLHSIV
     PVGKDPHEYE PLPEDVKKTS QADLIFYNGI NLETGGNAWF TKLVKNANKE ENKDYYAVSD
     GVDVIYLEGQ SEKGKEDPHA WLNLENGIIY AQNIAKRLIE KDPDNKATYE KNLKAYVEKL
     TALDKEAKEK FNNIPEEKKM IVTSEGCFKY FSKAYNVPSA YIWEINTEEE GTPDQIKSLV
     EKLRKTKVPS LFVESSVDDR PMKTVSKDTN IPIHAKIFTD SIADQGEEGD TYYSMMKYNL
     DKISEGLAK