ID   MTSA_STRMT              Reviewed;         309 AA.
AC   Q9L5X0;
DT   18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Manganese ABC transporter substrate-binding lipoprotein;
DE   AltName: Full=Pneumococcal surface adhesin A;
DE   Flags: Precursor;
GN   Name=psaA;
OS   Streptococcus mitis.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=28037;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 49456 / DSM 12643 / LMG 14557 / NCTC 12261;
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; AF248236; AAF64229.1; -; Genomic_DNA.
DR   RefSeq; WP_000733052.1; NZ_UHFS01000002.1.
DR   AlphaFoldDB; Q9L5X0; -.
DR   SMR; Q9L5X0; -.
DR   STRING; 585202.SMSK321_0954; -.
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_0000031887"
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;  34595 MW;  112423C9F4873D25 CRC64;
     MKKLGTLFVL FLSVIVLVAC ASGKKDAASG QKLKVVATNS IIADITKNIA GDKIDLHSIV
     PIGQDPHEYE PLPEDVKKTS EADLIFYNGI NLETGGNAWF SKLVENAKKT ENKDYFAVSE
     GVDVIYLEGK NEKGKEDPHA WLNLENGIIF AKNIAKQLSA KDPNNKEFYE KNLKEYTDKL
     DKLDKESKDK FNNIPAEKKL IVTSEGAFKY FSKAYGVPSA YIWEINTEEE GTPEQIKTLV
     EKLRQTKVPS LFVESSVDDR PMKTVSQDTN IPIYAQIFTD SIAEQGKEGD SYYNMMKYNL
     DKIAEGLAK