ID   CPSB_STRA5              Reviewed;         243 AA.
AC   P0A364; Q9S0S9;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   27-MAR-2024, entry version 86.
DE   RecName: Full=Tyrosine-protein phosphatase CpsB;
DE            EC=3.1.3.48;
GN   Name=cpsB; Synonyms=cpsIaB; OrderedLocusNames=SAG1174;
OS   Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=208435;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CNCTC 1/82 / Serotype V;
RA   McKinnon K., Chaffin D.O., Rubens C.E.;
RT   "Streptococcus agalactiae type V polysaccharide synthesis operon complete
RT   sequence.";
RL   Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-611 / 2603 V/R;
RX   PubMed=12200547; DOI=10.1073/pnas.182380799;
RA   Tettelin H., Masignani V., Cieslewicz M.J., Eisen J.A., Peterson S.N.,
RA   Wessels M.R., Paulsen I.T., Nelson K.E., Margarit I., Read T.D.,
RA   Madoff L.C., Wolf A.M., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA   DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Lewis M.R., Radune D.,
RA   Fedorova N.B., Scanlan D., Khouri H.M., Mulligan S., Carty H.A.,
RA   Cline R.T., Van Aken S.E., Gill J., Scarselli M., Mora M., Iacobini E.T.,
RA   Brettoni C., Galli G., Mariani M., Vegni F., Maione D., Rinaudo D.,
RA   Rappuoli R., Telford J.L., Kasper D.L., Grandi G., Fraser C.M.;
RT   "Complete genome sequence and comparative genomic analysis of an emerging
RT   human pathogen, serotype V Streptococcus agalactiae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:12391-12396(2002).
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; AF349539; AAK29648.1; -; Genomic_DNA.
DR   EMBL; AE009948; AAN00056.1; -; Genomic_DNA.
DR   RefSeq; NP_688183.1; NC_004116.1.
DR   RefSeq; WP_000565383.1; NC_004116.1.
DR   AlphaFoldDB; P0A364; -.
DR   SMR; P0A364; -.
DR   STRING; 208435.SAG1174; -.
DR   DNASU; 1013981; -.
DR   KEGG; sag:SAG1174; -.
DR   PATRIC; fig|208435.3.peg.1180; -.
DR   HOGENOM; CLU_085966_1_0_9; -.
DR   OrthoDB; 9788539at2; -.
DR   UniPathway; UPA00934; -.
DR   Proteomes; UP000000821; Chromosome.
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; Reference proteome.
FT   CHAIN           1..243
FT                   /note="Tyrosine-protein phosphatase CpsB"
FT                   /id="PRO_0000057890"
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
//