ID   MTSA_STRPA              Reviewed;         309 AA.
AC   P31305;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Manganese ABC transporter substrate-binding lipoprotein {ECO:0000305};
DE   AltName: Full=Adhesin B;
DE   AltName: Full=FimA;
DE   AltName: Full=Saliva-binding protein;
DE   Flags: Precursor;
GN   Name=fimA;
OS   Streptococcus parasanguinis.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1318;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=FW213;
RX   PubMed=2572555; DOI=10.1128/iai.57.11.3527-3533.1989;
RA   Fenno J.C., Leblanc D.J., Fives-Taylor P.M.;
RT   "Nucleotide sequence analysis of a type 1 fimbrial gene of Streptococcus
RT   sanguis FW213.";
RL   Infect. Immun. 57:3527-3533(1989).
RN   [2]
RP   POSSIBLE FUNCTION.
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   [3]
RP   CHARACTERIZATION.
RC   STRAIN=FW213;
RX   PubMed=7596287; DOI=10.1111/j.1365-2958.1995.tb02355.x;
RA   Fenno J.C., Shaikh A., Spatafora G., Fives-Taylor P.;
RT   "The fimA locus of Streptococcus parasanguis encodes an ATP-binding
RT   membrane transport system.";
RL   Mol. Microbiol. 15:849-863(1995).
RN   [4]
RP   SUBCELLULAR LOCATION.
RC   STRAIN=FW213;
RX   PubMed=21862581; DOI=10.1074/jbc.m111.239350;
RA   Wu R., Wu H.;
RT   "A molecular chaperone mediates a two-protein enzyme complex and
RT   glycosylation of serine-rich streptococcal adhesins.";
RL   J. Biol. Chem. 286:34923-34931(2011).
CC   -!- FUNCTION: Part of an ABC transporter complex involved in manganese
CC       import. Also acts as an adhesin which is involved on adherence to
CC       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, ECO:0000305|PubMed:21862581}; Lipid-anchor
CC       {ECO:0000255|PROSITE-ProRule:PRU00303, ECO:0000305|PubMed:21862581}.
CC   -!- SIMILARITY: Belongs to the bacterial solute-binding protein 9 family.
CC       Lipoprotein receptor antigen (Lrai) subfamily. {ECO:0000305}.
CC   -!- CAUTION: Was originally thought to be a fimbrial subunit.
CC       {ECO:0000305|PubMed:2572555}.
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DR   EMBL; M26130; AAA53077.1; -; Genomic_DNA.
DR   PIR; A37186; A37186.
DR   RefSeq; WP_014712825.1; NZ_LAWB01000013.1.
DR   AlphaFoldDB; P31305; -.
DR   SMR; P31305; -.
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; Lipoprotein; Manganese; Membrane; Metal-binding; Palmitate;
KW   Signal; Transport; Zinc.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           21..309
FT                   /note="Manganese ABC transporter substrate-binding
FT                   lipoprotein"
FT                   /id="PRO_0000031890"
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           21
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           21
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ   SEQUENCE   309 AA;  34349 MW;  332F10BC858E8396 CRC64;
     MKKIASVLAL FVALLFGLLA CSKGSSSGAS GKLKVVTTNS ILADITKNIA GDKIELHSIV
     PVGKDPHEYE PLPEDVKKTS QADLIFYNGI NLETGGNAWF TKLVKNANKV ENKDYFAVSE
     GVDVIYLEGQ NQAGKEDPHA WLNLENGILY AKNIAKQLIA KDPKNKDFYE KNLAAYTEKL
     SKLDQKAKQA FKNIPEDKKM IVTSEGCFKY FSKAYGVPSA YIWEINTEEE GTPEQIKTLV
     EKLRQTKVPA LFVESSVDER PMKTVAKDTN IPIYAKIFTD SIAKEGEKGD SYYSMMKWNL
     DKIAEGLSQ