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