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Manganese ABC transporter substrate-binding lipoprotein (Pneumococcal surface adhesin A)

 MTSA_STRPN              Reviewed;         309 AA.
P0A4G2; P72538; Q54720; Q9L5X2; Q9L5X3; Q9L5X4; Q9R6P5;
15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
15-MAR-2005, sequence version 1.
05-JUL-2017, entry version 87.
RecName: Full=Manganese ABC transporter substrate-binding lipoprotein;
AltName: Full=Pneumococcal surface adhesin A;
Flags: Precursor;
Name=psaA; OrderedLocusNames=SP_1650;
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
Streptococcus.
NCBI_TaxID=170187;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=6B;
Sampson J.S., Whitney A.M., Furlow Z.;
"Streptococcus pneumoniae surface adhesin A.";
Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=D39 / NCTC 7466 / Serotype 2;
PubMed=8945574;
Berry A.M., Paton J.C.;
"Sequence heterogeneity of PsaA, a 37-kilodalton putative adhesin
essential for virulence of Streptococcus pneumoniae.";
Infect. Immun. 64:5255-5262(1996).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9767595; DOI=10.1046/j.1365-2958.1998.01016.x;
Novak R., Braun J.S., Charpentier E., Tuomanen E.;
"Penicillin tolerance genes of Streptococcus pneumoniae: the ABC-type
manganese permease complex Psa.";
Mol. Microbiol. 29:1285-1296(1998).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=NA-1064/97, NA-1283/96, NA-1383/97, and NA-1508/92;
Perez A., Jado I., Casal J.;
"Identification of a psaA gene in viridans streptococcal strains.";
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC BAA-334 / TIGR4;
PubMed=11463916; DOI=10.1126/science.1061217;
Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T.,
Hickey E.K., Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C.,
Dougherty B.A., Morrison D.A., Hollingshead S.K., Fraser C.M.;
"Complete genome sequence of a virulent isolate of Streptococcus
pneumoniae.";
Science 293:498-506(2001).
[6]
FUNCTION.
PubMed=9379902; DOI=10.1046/j.1365-2958.1997.5111879.x;
Dintilhac A., Alloing G., Granadel C., Claverys J.-P.;
"Competence and virulence of Streptococcus pneumoniae: Adc and PsaA
mutants exhibit a requirement for Zn and Mn resulting from
inactivation of putative ABC metal permeases.";
Mol. Microbiol. 25:727-739(1997).
[7]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 19-309, AND METAL-BINDING
SITES.
PubMed=9862808; DOI=10.1016/S0969-2126(98)00153-1;
Lawrence M.C., Pilling P.A., Epa V.C., Berry A.M., Ogunniyi A.D.,
Paton J.C.;
"The crystal structure of pneumococcal surface antigen PsaA reveals a
metal-binding site and a novel structure for a putative ABC-type
binding protein.";
Structure 6:1553-1561(1998).
-!- FUNCTION: Part of an ATP-driven transport system for manganese.
Also act as an adhesin which is involved on adherence to
extracellular matrix. It is an important factor in pathogenesis
and infection. {ECO:0000269|PubMed:9379902}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-
ProRule:PRU00303}.
-!- SIMILARITY: Belongs to the bacterial solute-binding protein 9
family. Lipoprotein receptor antigen (Lrai) subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U53509; AAB09440.1; -; Genomic_DNA.
EMBL; U40786; AAC24470.1; -; Genomic_DNA.
EMBL; AF055088; AAD09975.1; -; Genomic_DNA.
EMBL; AF248229; AAF70663.1; -; Genomic_DNA.
EMBL; AF248231; AAF70665.1; -; Genomic_DNA.
EMBL; AF248232; AAF70666.1; -; Genomic_DNA.
EMBL; AF248233; AAF70667.1; -; Genomic_DNA.
EMBL; AF248234; AAF70668.1; -; Genomic_DNA.
EMBL; AE005672; AAK75729.1; -; Genomic_DNA.
PIR; H95191; H95191.
RefSeq; WP_000733059.1; NZ_AKVY01000001.1.
PDB; 1PSZ; X-ray; 2.00 A; A=19-309.
PDB; 3ZK7; X-ray; 1.69 A; A/B=32-309.
PDB; 3ZK8; X-ray; 1.65 A; A/B=32-309.
PDB; 3ZK9; X-ray; 1.45 A; A/B=32-309.
PDB; 3ZKA; X-ray; 1.55 A; A/B=32-309.
PDB; 3ZTT; X-ray; 2.70 A; A/B/C/D=19-309.
PDB; 4UTO; X-ray; 1.55 A; A/B=1-309.
PDB; 4UTP; X-ray; 2.00 A; A/B=1-309.
PDBsum; 1PSZ; -.
PDBsum; 3ZK7; -.
PDBsum; 3ZK8; -.
PDBsum; 3ZK9; -.
PDBsum; 3ZKA; -.
PDBsum; 3ZTT; -.
PDBsum; 4UTO; -.
PDBsum; 4UTP; -.
ProteinModelPortal; P0A4G2; -.
SMR; P0A4G2; -.
TCDB; 3.A.1.15.14; the atp-binding cassette (abc) superfamily.
EnsemblBacteria; AAK75729; AAK75729; SP_1650.
KEGG; spn:SP_1650; -.
eggNOG; ENOG4105DSE; Bacteria.
eggNOG; COG0803; LUCA.
KO; K19971; -.
OMA; PDPHVWG; -.
EvolutionaryTrace; P0A4G2; -.
Proteomes; UP000000585; Chromosome.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0007155; P:cell adhesion; IEA:InterPro.
GO; GO:0030001; P:metal ion transport; IEA:InterPro.
InterPro; IPR006129; AdhesinB.
InterPro; IPR006128; Lipoprotein_4.
InterPro; IPR006127; ZnuA-like.
Pfam; PF01297; ZnuA; 1.
PRINTS; PR00691; ADHESINB.
PRINTS; PR00690; ADHESNFAMILY.
PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Complete proteome; Lipoprotein;
Manganese; Membrane; Metal-binding; Palmitate; Signal; Transport;
Zinc.
SIGNAL 1 19 {ECO:0000305}.
CHAIN 20 309 Manganese ABC transporter substrate-
binding lipoprotein.
/FTId=PRO_0000031891.
METAL 67 67 Zinc. {ECO:0000305}.
METAL 139 139 Zinc. {ECO:0000305}.
METAL 205 205 Zinc. {ECO:0000305}.
METAL 280 280 Zinc. {ECO:0000305}.
LIPID 20 20 N-palmitoyl cysteine. {ECO:0000305}.
LIPID 20 20 S-diacylglycerol cysteine. {ECO:0000305}.
VARIANT 8 8 L -> F (in strain: NA-1508/92).
VARIANT 9 9 V -> I (in strain: NA-1064/97).
VARIANT 14 14 A -> V (in strain: NA-1064/97, NA-1383/97
and NA-1508/92).
VARIANT 16 16 I -> A (in strain: NA-1064/97 and NA-
1383/97).
VARIANT 16 16 I -> V (in strain: NA-1508/92).
VARIANT 27 28 TT -> AA (in strain: NA-1064/97, NA-1383/
97 and NA-1508/92).
VARIANT 30 30 G -> S (in strain: NA-1064/97).
VARIANT 62 62 I -> V (in strain: NA-1383/97).
VARIANT 81 81 E -> Q (in strain: NA-1383/97).
VARIANT 83 83 D -> N (in strain: TIGR4).
VARIANT 120 120 D -> E (in strain: NA-1064/97, NA-1383/97
and NA-1508/92).
VARIANT 130 130 Q -> K (in strain: NA-1064/97 and NA-
1508/92).
VARIANT 148 148 I -> M (in strain: NA-1383/97).
VARIANT 164 164 N -> S (in strain: NA-1383/97).
VARIANT 187 189 SKD -> AKE (in strain: NA-1383/97).
VARIANT 193 193 K -> N (in strain: NA-1064/97, NA-1383/97
and NA-1508/92).
VARIANT 207 207 A -> C (in strain: NA-1383/97).
VARIANT 234 234 E -> D (in strain: NA-1383/97).
VARIANT 248 248 V -> T (in strain: NA-1383/97).
VARIANT 285 285 Q -> E (in strain: NA-1508/92).
VARIANT 294 294 S -> N (in strain: NA-1383/97).
HELIX 27 29 {ECO:0000244|PDB:1PSZ}.
STRAND 33 39 {ECO:0000244|PDB:3ZK9}.
HELIX 40 50 {ECO:0000244|PDB:3ZK9}.
HELIX 51 53 {ECO:0000244|PDB:3ZK9}.
STRAND 54 60 {ECO:0000244|PDB:3ZK9}.
STRAND 66 68 {ECO:0000244|PDB:3ZKA}.
HELIX 73 81 {ECO:0000244|PDB:3ZK9}.
STRAND 83 87 {ECO:0000244|PDB:3ZK9}.
TURN 90 94 {ECO:0000244|PDB:3ZK9}.
TURN 96 98 {ECO:0000244|PDB:3ZTT}.
HELIX 99 106 {ECO:0000244|PDB:3ZK9}.
TURN 111 113 {ECO:0000244|PDB:3ZK9}.
STRAND 114 117 {ECO:0000244|PDB:3ZK9}.
TURN 118 121 {ECO:0000244|PDB:3ZK9}.
HELIX 127 129 {ECO:0000244|PDB:3ZK9}.
HELIX 140 142 {ECO:0000244|PDB:3ZK9}.
HELIX 144 161 {ECO:0000244|PDB:3ZK9}.
HELIX 163 165 {ECO:0000244|PDB:3ZK9}.
HELIX 166 193 {ECO:0000244|PDB:3ZK9}.
HELIX 196 198 {ECO:0000244|PDB:3ZK9}.
STRAND 201 206 {ECO:0000244|PDB:3ZK9}.
HELIX 209 215 {ECO:0000244|PDB:3ZK9}.
STRAND 219 223 {ECO:0000244|PDB:3ZK9}.
HELIX 233 244 {ECO:0000244|PDB:3ZK9}.
STRAND 251 254 {ECO:0000244|PDB:3ZK9}.
HELIX 260 269 {ECO:0000244|PDB:3ZK9}.
STRAND 273 277 {ECO:0000244|PDB:3ZK9}.
STRAND 279 281 {ECO:0000244|PDB:1PSZ}.
HELIX 292 307 {ECO:0000244|PDB:3ZK9}.
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


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