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Database: UniProt
Entry: P0A4G2
LinkDB: P0A4G2
Original site: P0A4G2 
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-OCT-2014, entry version 69.
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. {ECO:0000269|PubMed:9379902}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC       ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-
CC       ProRule:PRU00303}.
CC   -!- SIMILARITY: Belongs to the bacterial solute-binding protein 9
CC       family. Lipoprotein receptor antigen (Lrai) subfamily.
CC       {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; NP_346089.1; NC_003028.3.
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   PDBsum; 1PSZ; -.
DR   PDBsum; 3ZK7; -.
DR   PDBsum; 3ZK8; -.
DR   PDBsum; 3ZK9; -.
DR   PDBsum; 3ZKA; -.
DR   PDBsum; 3ZTT; -.
DR   ProteinModelPortal; P0A4G2; -.
DR   SMR; P0A4G2; 24-309.
DR   STRING; 170187.SP_1650; -.
DR   TCDB; 3.A.1.15.14; the atp-binding cassette (abc) superfamily.
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; FERFFEN; -.
DR   OrthoDB; EOG6B3601; -.
DR   BioCyc; SPNE170187:GHGN-1657-MONOMER; -.
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; TroA; 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       {ECO:0000305}.
FT   CHAIN        20    309       Manganese ABC transporter substrate-
FT                                binding lipoprotein.
FT                                /FTId=PRO_0000031891.
FT   METAL        67     67       Zinc. {ECO:0000305}.
FT   METAL       139    139       Zinc. {ECO:0000305}.
FT   METAL       205    205       Zinc. {ECO:0000305}.
FT   METAL       280    280       Zinc. {ECO:0000305}.
FT   LIPID        20     20       N-palmitoyl cysteine. {ECO:0000305}.
FT   LIPID        20     20       S-diacylglycerol cysteine. {ECO:0000305}.
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   TURN         90     94
FT   TURN         96     98
FT   HELIX        99    106
FT   TURN        111    113
FT   STRAND      114    117
FT   TURN        118    121
FT   HELIX       127    129
FT   HELIX       140    142
FT   HELIX       144    161
FT   HELIX       163    165
FT   HELIX       166    193
FT   HELIX       196    198
FT   STRAND      201    206
FT   HELIX       209    215
FT   STRAND      219    223
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
//
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