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