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MTSA_STREE
ID   MTSA_STREE              Reviewed;         310 AA.
AC   P42363;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Manganese ABC transporter substrate-binding lipoprotein {ECO:0000305};
DE   AltName: Full=Pneumococcal surface adhesin A;
DE   Flags: Precursor;
GN   Name=psaA {ECO:0000303|PubMed:7505262}; Synonyms=papA;
OS   Streptococcus pneumoniae.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1313;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=R36A;
RX   PubMed=7505262; DOI=10.1128/iai.62.1.319-324.1994;
RA   Sampson J.S., O'Connor S.P., Stinson A.R., Tharpe J.A., Russell H.;
RT   "Cloning and nucleotide sequence analysis of psaA, the Streptococcus
RT   pneumoniae gene encoding a 37-kilodalton protein homologous to previously
RT   reported Streptococcus sp. adhesins.";
RL   Infect. Immun. 62:319-324(1994).
CC   -!- FUNCTION: Part of an ABC transporter complex involved in manganese
CC       import. {ECO:0000250|UniProtKB:P42364}.
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; L19055; AAA16798.1; -; Unassigned_DNA.
DR   AlphaFoldDB; P42363; -.
DR   SMR; P42363; -.
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..20
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           21..310
FT                   /note="Manganese ABC transporter substrate-binding
FT                   lipoprotein"
FT                   /id="PRO_0000031892"
FT   BINDING         68
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         140
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         206
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         281
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   310 AA;  34538 MW;  9BBC8E84E572F8B8 CRC64;
     MKKIASVLAL FVALLFGLLA CSKGTSSKSS SDKLKVVTTN SILADITKNI AGDKIELHSI
     VPVGQDPHEY EPLPEDVKKT SQADLIFYNG INLETGGNAW FTKLVKNANK VENKDYFAAS
     DGVEVIYLEG QNQAGKEDPH AWLNLENGII YAKNIAKQLI AKDPKNKDFY EKNLAAYTEK
     LSKLDQEAKQ AFNNIPAEKK MIVTSEGCFK YFSKAYGVPS AYIWEINTEV EGTPEQIKTL
     LEKLRQTKVP SLFVESSVDE RPMKTVSKDS NIPIFAKIFT DSIAKEGEEG DSYYSMMKWN
     LEKIAEGLNK
 
 
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