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 01-MAY-2013, entry version 61.
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;
RA Berry A.M., Paton J.C.;
RT "Sequence heterogeneity of PsaA, a 37-kilodalton putative adhesin
RT essential 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.,
RA Hickey E.K., Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C.,
RA Dougherty B.A., 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
RT mutants exhibit a requirement for Zn and Mn resulting from
RT inactivation of putative 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
RP 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
RT binding protein.";
RL Structure 6:1553-1561(1998).
CC -!- FUNCTION: Part of an ATP-driven transport system for manganese.
CC Also act as an adhesin which is involved on adherence to
CC extracellular matrix. It is an important factor in pathogenesis
CC and infection.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor (By similarity).
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 9
CC family. Lipoprotein receptor antigen (Lrai) subfamily.
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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; NP_346089.1; NC_003028.3.
DR PDB; 1PSZ; X-ray; 2.00 A; A=19-309.
DR PDB; 3ZTT; X-ray; 2.70 A; A/B/C/D=19-309.
DR PDBsum; 1PSZ; -.
DR PDBsum; 3ZTT; -.
DR ProteinModelPortal; P0A4G2; -.
DR SMR; P0A4G2; 24-309.
DR STRING; 170187.SP_1650; -.
DR EnsemblBacteria; AAK75729; AAK75729; SP_1650.
DR GeneID; 931186; -.
DR KEGG; spn:SP_1650; -.
DR PATRIC; 19707735; VBIStrPne105772_1710.
DR eggNOG; COG0803; -.
DR KO; K11704; -.
DR OMA; IPSAYIW; -.
DR ProtClustDB; CLSK876868; -.
DR EvolutionaryTrace; P0A4G2; -.
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; Perip_solute-bd_prot_fam.
DR Pfam; PF01297; SBP_bac_9; 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; Complete proteome; Lipoprotein;
KW Manganese; Membrane; Metal-binding; Palmitate; Signal; Transport;
KW Zinc.
FT SIGNAL 1 19 Probable.
FT CHAIN 20 309 Manganese ABC transporter substrate-
FT binding lipoprotein.
FT /FTId=PRO_0000031891.
FT METAL 67 67 Zinc (Probable).
FT METAL 139 139 Zinc (Probable).
FT METAL 205 205 Zinc (Probable).
FT METAL 280 280 Zinc (Probable).
FT LIPID 20 20 N-palmitoyl cysteine (Probable).
FT LIPID 20 20 S-diacylglycerol cysteine (Probable).
FT VARIANT 8 8 L -> F (in strain: NA-1508/92).
FT VARIANT 9 9 V -> I (in strain: NA-1064/97).
FT VARIANT 14 14 A -> V (in strain: NA-1064/97, NA-1383/97
FT and NA-1508/92).
FT VARIANT 16 16 I -> A (in strain: NA-1064/97 and NA-
FT 1383/97).
FT VARIANT 16 16 I -> V (in strain: NA-1508/92).
FT VARIANT 27 28 TT -> AA (in strain: NA-1064/97, NA-1383/
FT 97 and NA-1508/92).
FT VARIANT 30 30 G -> S (in strain: NA-1064/97).
FT VARIANT 62 62 I -> V (in strain: NA-1383/97).
FT VARIANT 81 81 E -> Q (in strain: NA-1383/97).
FT VARIANT 83 83 D -> N (in strain: TIGR4).
FT VARIANT 120 120 D -> E (in strain: NA-1064/97, NA-1383/97
FT and NA-1508/92).
FT VARIANT 130 130 Q -> K (in strain: NA-1064/97 and NA-
FT 1508/92).
FT VARIANT 148 148 I -> M (in strain: NA-1383/97).
FT VARIANT 164 164 N -> S (in strain: NA-1383/97).
FT VARIANT 187 189 SKD -> AKE (in strain: NA-1383/97).
FT VARIANT 193 193 K -> N (in strain: NA-1064/97, NA-1383/97
FT and NA-1508/92).
FT VARIANT 207 207 A -> C (in strain: NA-1383/97).
FT VARIANT 234 234 E -> D (in strain: NA-1383/97).
FT VARIANT 248 248 V -> T (in strain: NA-1383/97).
FT VARIANT 285 285 Q -> E (in strain: NA-1508/92).
FT VARIANT 294 294 S -> N (in strain: NA-1383/97).
FT HELIX 27 29
FT STRAND 33 39
FT HELIX 40 50
FT HELIX 51 53
FT STRAND 54 60
FT STRAND 66 68
FT HELIX 73 81
FT STRAND 83 87
FT HELIX 95 106
FT TURN 111 113
FT STRAND 114 117
FT TURN 118 121
FT HELIX 140 142
FT HELIX 144 161
FT HELIX 163 165
FT HELIX 166 187
FT TURN 188 193
FT TURN 196 198
FT STRAND 201 205
FT HELIX 209 215
FT STRAND 219 225
FT HELIX 233 244
FT STRAND 251 254
FT HELIX 260 269
FT STRAND 273 277
FT STRAND 279 281
FT HELIX 292 307
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
//
