ID   MTSA_STRAP              Reviewed;         309 AA.
AC   Q9L5X1;
DT   18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Manganese ABC transporter substrate-binding lipoprotein;
DE   AltName: Full=Pneumococcal surface adhesin A;
DE   Flags: Precursor;
GN   Name=psaA;
OS   Streptococcus anginosus.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus; Streptococcus anginosus group.
OX   NCBI_TaxID=1328;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NCTC 10713;
RX   PubMed=11527799; DOI=10.1128/cdli.8.5.895-898.2001;
RA   Jado I., Fenoll A., Casal J., Perez A.;
RT   "Identification of the psaA gene, coding for pneumococcal surface adhesin
RT   A, in viridans group streptococci other than Streptococcus pneumoniae.";
RL   Clin. Diagn. Lab. Immunol. 8:895-898(2001).
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 pathogenesis and infection (By
CC       similarity). {ECO:0000250}.
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}.
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DR   EMBL; AF248235; AAF64228.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9L5X1; -.
DR   SMR; Q9L5X1; -.
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   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_0000031884"
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   LIPID           20
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ   SEQUENCE   309 AA;  34615 MW;  966EBDF808F0580D CRC64;
     MKKLGTLLVL FLSVIALVAC ASGKKDATSG QKLKVVATNS IIADITKNIA GDKIDLHSIV
     PVGQDPHEYE PLPEDVKKTS QADLIFYNGI NLETGGNAWF TKLVENAKKT ENKDYFAVSE
     GVDVIYLEGQ NEKGKEDPHA WLNLENGMIY AKNIAKQLIA KDPSNKEFYE KNLKDYTEKL
     DKLDKEAKEK FNNIPAEKKL IVTSEGCFKY FSKAYGVPSA YIWEINTEEE GTPEQIKTLV
     EKLRQTKVPS LFVESSVDDR PMKTVSQDTN IPIYAQIFTD SIAEEGKEGD SYYSMMKYNL
     DKIAEGLSK