ID   CPSB_STRA1              Reviewed;         243 AA.
AC   Q3K0S8; P0A365; Q9S0S9;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   RecName: Full=Tyrosine-protein phosphatase CpsB;
DE            EC=3.1.3.48;
GN   Name=cpsB; Synonyms=cpsIaB; OrderedLocusNames=SAK_1261;
OS   Streptococcus agalactiae serotype Ia (strain ATCC 27591 / A909 / CDC
OS   SS700).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=205921;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=OI1 / Serotype Ia;
RX   PubMed=10464185; DOI=10.1128/jb.181.17.5176-5184.1999;
RA   Yamamoto S., Miyake K., Koike Y., Watanabe M., Machida Y., Ohta M.,
RA   Iijima S.;
RT   "Molecular characterization of type-specific capsular polysaccharide
RT   biosynthesis genes of Streptococcus agalactiae type Ia.";
RL   J. Bacteriol. 181:5176-5184(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27591 / A909 / CDC SS700;
RX   PubMed=16172379; DOI=10.1073/pnas.0506758102;
RA   Tettelin H., Masignani V., Cieslewicz M.J., Donati C., Medini D.,
RA   Ward N.L., Angiuoli S.V., Crabtree J., Jones A.L., Durkin A.S., DeBoy R.T.,
RA   Davidsen T.M., Mora M., Scarselli M., Margarit y Ros I., Peterson J.D.,
RA   Hauser C.R., Sundaram J.P., Nelson W.C., Madupu R., Brinkac L.M.,
RA   Dodson R.J., Rosovitz M.J., Sullivan S.A., Daugherty S.C., Haft D.H.,
RA   Selengut J., Gwinn M.L., Zhou L., Zafar N., Khouri H., Radune D.,
RA   Dimitrov G., Watkins K., O'Connor K.J., Smith S., Utterback T.R., White O.,
RA   Rubens C.E., Grandi G., Madoff L.C., Kasper D.L., Telford J.L.,
RA   Wessels M.R., Rappuoli R., Fraser C.M.;
RT   "Genome analysis of multiple pathogenic isolates of Streptococcus
RT   agalactiae: implications for the microbial 'pan-genome'.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13950-13955(2005).
CC   -!- FUNCTION: Dephosphorylates CpsD. Involved in the regulation of capsular
CC       polysaccharide biosynthesis (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620; EC=3.1.3.48;
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC   -!- PATHWAY: Capsule biogenesis; capsule polysaccharide biosynthesis.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       CpsB/CapC family. {ECO:0000305}.
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DR   EMBL; AB028896; BAA82276.1; -; Genomic_DNA.
DR   EMBL; CP000114; ABA46124.1; -; Genomic_DNA.
DR   RefSeq; WP_000565383.1; NC_007432.1.
DR   AlphaFoldDB; Q3K0S8; -.
DR   SMR; Q3K0S8; -.
DR   KEGG; sak:SAK_1261; -.
DR   HOGENOM; CLU_085966_1_0_9; -.
DR   UniPathway; UPA00934; -.
DR   GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045227; P:capsule polysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   InterPro; IPR048208; Caps_polysacc_synth_CpsB.
DR   InterPro; IPR016667; Caps_polysacc_synth_CpsB/CapC.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   NCBIfam; NF041488; caps_synth_Cps4B; 1.
DR   PANTHER; PTHR39181; TYROSINE-PROTEIN PHOSPHATASE YWQE; 1.
DR   PANTHER; PTHR39181:SF1; TYROSINE-PROTEIN PHOSPHATASE YWQE; 1.
DR   Pfam; PF19567; CpsB_CapC; 1.
DR   PIRSF; PIRSF016557; Caps_synth_CpsB; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE   3: Inferred from homology;
KW   Capsule biogenesis/degradation; Exopolysaccharide synthesis; Hydrolase;
KW   Manganese; Protein phosphatase.
FT   CHAIN           1..243
FT                   /note="Tyrosine-protein phosphatase CpsB"
FT                   /id="PRO_0000057888"
SQ   SEQUENCE   243 AA;  28600 MW;  319CA48CCB310123 CRC64;
     MIDIHSHIVF DVDDGPKTLE ESLSLIEESY RQGVRIIVST SHRRKGMFET PEDIIFKNFS
     IVKHEAEKRF EHLQILYGGE LYYTSDMLEK LKLKQIPTLN NTKFALIEFS MQTSWKDIHT
     ALSNVLMLGI TPVVAHIERY NALENQKERV KEIINMGCYT QINSSHILKQ KLFNDKHKRF
     KKRARYFLEE NLVHFVASDM HNLDVRPPFL AEAYKIICRD FGKERANQLF IENAQSILKN
     HYI
//