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MTSA_STROR
ID   MTSA_STROR              Reviewed;         309 AA.
AC   Q9L5W9;
DT   18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Manganese ABC transporter substrate-binding lipoprotein;
DE   AltName: Full=Pneumococcal surface adhesin A;
DE   Flags: Precursor;
GN   Name=psaA;
OS   Streptococcus oralis.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 35037 / CIP 102922 / DSM 20627 / KCTC 13048 / LMG 14532 / NCTC
RC   11427 / PB182;
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. {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; AF248237; AAF64230.1; -; Genomic_DNA.
DR   RefSeq; WP_000733080.1; NZ_RMVL01000002.1.
DR   AlphaFoldDB; Q9L5W9; -.
DR   SMR; Q9L5W9; -.
DR   STRING; 1303.SORDD17_00683; -.
DR   GeneID; 49599273; -.
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_0000031889"
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;  34616 MW;  81F0C41F91E5C954 CRC64;
     MKKLGTLLVL FLSVIALVAC ASGKKDATSG QKLKVVATNS IIADITKNIA GDKIDLHSIV
     PVGQDPHEYE PLPEDVKKTS EADLIFYNGI NLETGGNAWF TKLVENAKKT ENKDYFAVSE
     GVDVIYLEGQ NEKGKEDPHA WLNLENGMIY AKNIAKQLIA KDPSNKEFYE KNLKDYTEKL
     DKLDKEAKEK FNNIPAEKKL IVTSEGCFKY FSKAYGVPSA YIWEINTEEE GTPEQIKTLV
     EKLRQTKVPS LFVESSVDDR PMKTVSQDTN IPIYAQIFTD SIAEEGKEGD SYYSMMKYNL
     DKIAEGLSK
 
 
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