MTSA_STRPN
ID MTSA_STRPN Reviewed; 309 AA.
AC P0A4G2; P72538; Q54720; Q9L5X2; Q9L5X3; Q9L5X4; Q9R6P5;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Manganese ABC transporter substrate-binding lipoprotein;
DE AltName: Full=Pneumococcal surface adhesin A;
DE Flags: Precursor;
GN Name=psaA; OrderedLocusNames=SP_1650;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=6B;
RA Sampson J.S., Whitney A.M., Furlow Z.;
RT "Streptococcus pneumoniae surface adhesin A.";
RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=D39 / NCTC 7466 / Serotype 2;
RX PubMed=8945574; DOI=10.1128/iai.64.12.5255-5262.1996;
RA Berry A.M., Paton J.C.;
RT "Sequence heterogeneity of PsaA, a 37-kilodalton putative adhesin essential
RT for virulence of Streptococcus pneumoniae.";
RL Infect. Immun. 64:5255-5262(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9767595; DOI=10.1046/j.1365-2958.1998.01016.x;
RA Novak R., Braun J.S., Charpentier E., Tuomanen E.;
RT "Penicillin tolerance genes of Streptococcus pneumoniae: the ABC-type
RT manganese permease complex Psa.";
RL Mol. Microbiol. 29:1285-1296(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NA-1064/97, NA-1283/96, NA-1383/97, and NA-1508/92;
RA Perez A., Jado I., Casal J.;
RT "Identification of a psaA gene in viridans streptococcal strains.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
RN [6]
RP FUNCTION.
RX PubMed=9379902; DOI=10.1046/j.1365-2958.1997.5111879.x;
RA Dintilhac A., Alloing G., Granadel C., Claverys J.-P.;
RT "Competence and virulence of Streptococcus pneumoniae: Adc and PsaA mutants
RT exhibit a requirement for Zn and Mn resulting from inactivation of putative
RT ABC metal permeases.";
RL Mol. Microbiol. 25:727-739(1997).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 19-309, AND METAL-BINDING SITES.
RX PubMed=9862808; DOI=10.1016/s0969-2126(98)00153-1;
RA Lawrence M.C., Pilling P.A., Epa V.C., Berry A.M., Ogunniyi A.D.,
RA Paton J.C.;
RT "The crystal structure of pneumococcal surface antigen PsaA reveals a
RT metal-binding site and a novel structure for a putative ABC-type binding
RT protein.";
RL Structure 6:1553-1561(1998).
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.
CC {ECO:0000269|PubMed:9379902}.
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; U53509; AAB09440.1; -; Genomic_DNA.
DR EMBL; U40786; AAC24470.1; -; Genomic_DNA.
DR EMBL; AF055088; AAD09975.1; -; Genomic_DNA.
DR EMBL; AF248229; AAF70663.1; -; Genomic_DNA.
DR EMBL; AF248231; AAF70665.1; -; Genomic_DNA.
DR EMBL; AF248232; AAF70666.1; -; Genomic_DNA.
DR EMBL; AF248233; AAF70667.1; -; Genomic_DNA.
DR EMBL; AF248234; AAF70668.1; -; Genomic_DNA.
DR EMBL; AE005672; AAK75729.1; -; Genomic_DNA.
DR PIR; H95191; H95191.
DR RefSeq; WP_000733059.1; NZ_AKVY01000001.1.
DR PDB; 1PSZ; X-ray; 2.00 A; A=19-309.
DR PDB; 3ZK7; X-ray; 1.69 A; A/B=32-309.
DR PDB; 3ZK8; X-ray; 1.65 A; A/B=32-309.
DR PDB; 3ZK9; X-ray; 1.45 A; A/B=32-309.
DR PDB; 3ZKA; X-ray; 1.55 A; A/B=32-309.
DR PDB; 3ZTT; X-ray; 2.70 A; A/B/C/D=19-309.
DR PDB; 4UTO; X-ray; 1.55 A; A/B=1-309.
DR PDB; 4UTP; X-ray; 2.00 A; A/B=1-309.
DR PDBsum; 1PSZ; -.
DR PDBsum; 3ZK7; -.
DR PDBsum; 3ZK8; -.
DR PDBsum; 3ZK9; -.
DR PDBsum; 3ZKA; -.
DR PDBsum; 3ZTT; -.
DR PDBsum; 4UTO; -.
DR PDBsum; 4UTP; -.
DR AlphaFoldDB; P0A4G2; -.
DR SMR; P0A4G2; -.
DR STRING; 170187.SP_1650; -.
DR TCDB; 3.A.1.15.14; the atp-binding cassette (abc) superfamily.
DR PRIDE; P0A4G2; -.
DR EnsemblBacteria; AAK75729; AAK75729; SP_1650.
DR GeneID; 60233751; -.
DR KEGG; spn:SP_1650; -.
DR eggNOG; COG0803; Bacteria.
DR OMA; HHVFGYL; -.
DR PhylomeDB; P0A4G2; -.
DR BioCyc; SPNE170187:G1FZB-1671-MON; -.
DR EvolutionaryTrace; P0A4G2; -.
DR Proteomes; UP000000585; Chromosome.
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 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Lipoprotein; Manganese; Membrane;
KW Metal-binding; Palmitate; 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_0000031891"
FT BINDING 67
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305"
FT BINDING 139
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305"
FT BINDING 205
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305"
FT BINDING 280
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305"
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"
FT VARIANT 8
FT /note="L -> F (in strain: NA-1508/92)"
FT VARIANT 9
FT /note="V -> I (in strain: NA-1064/97)"
FT VARIANT 14
FT /note="A -> V (in strain: NA-1064/97, NA-1383/97 and NA-
FT 1508/92)"
FT VARIANT 16
FT /note="I -> A (in strain: NA-1064/97 and NA-1383/97)"
FT VARIANT 16
FT /note="I -> V (in strain: NA-1508/92)"
FT VARIANT 27..28
FT /note="TT -> AA (in strain: NA-1064/97, NA-1383/97 and NA-
FT 1508/92)"
FT VARIANT 30
FT /note="G -> S (in strain: NA-1064/97)"
FT VARIANT 62
FT /note="I -> V (in strain: NA-1383/97)"
FT VARIANT 81
FT /note="E -> Q (in strain: NA-1383/97)"
FT VARIANT 83
FT /note="D -> N (in strain: TIGR4)"
FT VARIANT 120
FT /note="D -> E (in strain: NA-1064/97, NA-1383/97 and NA-
FT 1508/92)"
FT VARIANT 130
FT /note="Q -> K (in strain: NA-1064/97 and NA-1508/92)"
FT VARIANT 148
FT /note="I -> M (in strain: NA-1383/97)"
FT VARIANT 164
FT /note="N -> S (in strain: NA-1383/97)"
FT VARIANT 187..189
FT /note="SKD -> AKE (in strain: NA-1383/97)"
FT VARIANT 193
FT /note="K -> N (in strain: NA-1064/97, NA-1383/97 and NA-
FT 1508/92)"
FT VARIANT 207
FT /note="A -> C (in strain: NA-1383/97)"
FT VARIANT 234
FT /note="E -> D (in strain: NA-1383/97)"
FT VARIANT 248
FT /note="V -> T (in strain: NA-1383/97)"
FT VARIANT 285
FT /note="Q -> E (in strain: NA-1508/92)"
FT VARIANT 294
FT /note="S -> N (in strain: NA-1383/97)"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:1PSZ"
FT STRAND 33..39
FT /evidence="ECO:0007829|PDB:3ZK9"
FT HELIX 40..50
FT /evidence="ECO:0007829|PDB:3ZK9"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:3ZK9"
FT STRAND 54..60
FT /evidence="ECO:0007829|PDB:3ZK9"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:3ZKA"
FT HELIX 73..81
FT /evidence="ECO:0007829|PDB:3ZK9"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:3ZK9"
FT TURN 90..94
FT /evidence="ECO:0007829|PDB:3ZK9"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:3ZTT"
FT HELIX 99..106
FT /evidence="ECO:0007829|PDB:3ZK9"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:3ZK9"
FT STRAND 114..117
FT /evidence="ECO:0007829|PDB:3ZK9"
FT TURN 118..121
FT /evidence="ECO:0007829|PDB:3ZK9"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:3ZK9"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:3ZK9"
FT HELIX 144..161
FT /evidence="ECO:0007829|PDB:3ZK9"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:3ZK9"
FT HELIX 166..193
FT /evidence="ECO:0007829|PDB:3ZK9"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:3ZK9"
FT STRAND 201..206
FT /evidence="ECO:0007829|PDB:3ZK9"
FT HELIX 209..215
FT /evidence="ECO:0007829|PDB:3ZK9"
FT STRAND 219..223
FT /evidence="ECO:0007829|PDB:3ZK9"
FT HELIX 233..244
FT /evidence="ECO:0007829|PDB:3ZK9"
FT STRAND 251..254
FT /evidence="ECO:0007829|PDB:3ZK9"
FT HELIX 260..269
FT /evidence="ECO:0007829|PDB:3ZK9"
FT STRAND 273..277
FT /evidence="ECO:0007829|PDB:3ZK9"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:1PSZ"
FT HELIX 292..307
FT /evidence="ECO:0007829|PDB:3ZK9"
SQ SEQUENCE 309 AA; 34594 MW; B125E7FE3DA6F67C CRC64;
MKKLGTLLVL FLSAIILVAC ASGKKDTTSG QKLKVVATNS IIADITKNIA GDKIDLHSIV
PIGQDPHEYE PLPEDVKKTS EADLIFYNGI NLETGGNAWF TKLVENAKKT ENKDYFAVSD
GVDVIYLEGQ NEKGKEDPHA WLNLENGIIF AKNIAKQLSA KDPNNKEFYE KNLKEYTDKL
DKLDKESKDK FNKIPAEKKL IVTSEGAFKY FSKAYGVPSA YIWEINTEEE GTPEQIKTLV
EKLRQTKVPS LFVESSVDDR PMKTVSQDTN IPIYAQIFTD SIAEQGKEGD SYYSMMKYNL
DKIAEGLAK
