ID CPSB1_STRPN Reviewed; 243 AA. AC Q9AHD4; DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 16-JUN-2009, entry version 42. DE RecName: Full=Tyrosine-protein phosphatase cpsB; DE EC=3.1.3.48; GN Name=cpsB; Synonyms=wzh; OrderedLocusNames=SP_0347; OS Streptococcus pneumoniae. OC Bacteria; Firmicutes; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1313; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=WCH35 / Serotype 4; RX MEDLINE=21116929; PubMed=11179285; RX DOI=10.1128/IAI.69.3.1244-1255.2001; RA Jiang S.-M., Wang L., Reeves P.R.; RT "Molecular characterization of Streptococcus pneumoniae type 4, 6B, 8, RT and 18C capsular polysaccharide gene clusters."; RL Infect. Immun. 69:1244-1255(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-334 / TIGR4; RX MEDLINE=21357209; 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). CC -!- FUNCTION: Dephosphorylates cpsD. Involved in the regulation of CC capsular polysaccharide biosynthesis (By similarity). CC -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein CC tyrosine + phosphate. CC -!- COFACTOR: Manganese (By similarity). CC -!- PATHWAY: Capsule biogenesis; capsule polysaccharide biosynthesis. CC -!- SIMILARITY: Belongs to the cpsB/capC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF316639; AAK20667.1; -; Genomic_DNA. DR EMBL; AE005672; AAK74520.1; -; Genomic_DNA. DR PIR; G95040; G95040. DR RefSeq; NP_344880.1; -. DR GeneID; 930166; -. DR GenomeReviews; AE005672_GR; SP_0347. DR KEGG; spn:SP_0347; -. DR TIGR; SP_0347; -. DR HOGENOM; Q9AHD4; -. DR OMA; Q9AHD4; ITPVIAH. DR BRENDA; 3.1.3.48; 600. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-KW. DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:EC. DR GO; GO:0000271; P:polysaccharide biosynthetic process; IEA:UniProtKB-KW. DR InterPro; IPR016667; Caps_polysacc_synth_CpsB/CapC. DR InterPro; IPR004013; PHP_C. DR Pfam; PF02811; PHP; 1. DR PIRSF; PIRSF016557; Caps_synth_CpsB; 1. PE 3: Inferred from homology; KW Capsule biogenesis/degradation; Complete proteome; KW Exopolysaccharide synthesis; Hydrolase; Manganese; KW Protein phosphatase. FT CHAIN 1 243 Tyrosine-protein phosphatase cpsB. FT /FTId=PRO_0000057891. SQ SEQUENCE 243 AA; 28131 MW; 1171C4A506FDE0D5 CRC64; MIDIHSHIVF DVDDGPKSRE ESKALLAESY RQGVRTIVST SHRRKGMFET PEEKIAENFL QVREIAKEVA SDLVIAYGAE IYYTPDVLDK LEKKRIPTLN DSRYALIEFS MNTPYRDIHS ALSKILMLGI TPVIAHIERY DALENNEKRV RELIDMGCYT QVNSSHVLKP KLFGERYKFM KKRAQYFLEQ DLVHVIASDM HNLDGRPPHM AEAYDLVTQK YGEAKAQELF IDNPRKIVMD QLI //