ID   CPSB_STRA3              Reviewed;         243 AA.
AC   Q04661;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   17-JAN-2003, sequence version 2.
DT   27-MAR-2024, entry version 109.
DE   RecName: Full=Tyrosine-protein phosphatase CpsB;
DE            EC=3.1.3.48;
GN   Name=cpsB; OrderedLocusNames=gbs1247;
OS   Streptococcus agalactiae serotype III (strain NEM316).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=211110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=COH1 / Serotype III;
RX   PubMed=8355611; DOI=10.1111/j.1365-2958.1993.tb01631.x;
RA   Rubens C.E., Heggen L.M., Haft R.F., Wessels M.R.;
RT   "Identification of cpsD, a gene essential for type III capsule expression
RT   in group B streptococci.";
RL   Mol. Microbiol. 8:843-855(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NEM316;
RX   PubMed=12354221; DOI=10.1046/j.1365-2958.2002.03126.x;
RA   Glaser P., Rusniok C., Buchrieser C., Chevalier F., Frangeul L., Msadek T.,
RA   Zouine M., Couve E., Lalioui L., Poyart C., Trieu-Cuot P., Kunst F.;
RT   "Genome sequence of Streptococcus agalactiae, a pathogen causing invasive
RT   neonatal disease.";
RL   Mol. Microbiol. 45:1499-1513(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}.
CC   -!- CAUTION: Was originally called CpsA. {ECO:0000305|PubMed:8355611}.
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DR   EMBL; AF163833; AAB00361.1; -; Genomic_DNA.
DR   EMBL; AL766849; CAD46906.1; -; Genomic_DNA.
DR   PIR; S34974; S34974.
DR   RefSeq; WP_000565385.1; NC_004368.1.
DR   AlphaFoldDB; Q04661; -.
DR   SMR; Q04661; -.
DR   KEGG; san:cpsB; -.
DR   eggNOG; COG4464; Bacteria.
DR   HOGENOM; CLU_085966_1_0_9; -.
DR   UniPathway; UPA00934; -.
DR   Proteomes; UP000000823; 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.
FT   CHAIN           1..243
FT                   /note="Tyrosine-protein phosphatase CpsB"
FT                   /id="PRO_0000057889"
FT   CONFLICT        66
FT                   /note="A -> T (in Ref. 1; AAB00361)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        142
FT                   /note="S -> A (in Ref. 1; AAB00361)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        165
FT                   /note="S -> F (in Ref. 1; AAB00361)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   243 AA;  28616 MW;  B747C92DB128FF5A CRC64;
     MIDIHSHIVF DVDDGPKTLE ESLSLIEESY RQGVRIIVST SHRRKGMFET PEDIIFKNFS
     IVKHEAEKRF EHLQILYGGE LYYTSDMLEK LKLKQIPTLN NTKFALIEFS MQTSWKDIHT
     ALSNVLMLGI TPVVAHIERY NSLENQKERV KEIINMGCYT QINSSHILKQ KLFNDKHKRF
     KKRARYFLEE NLVHFVASDM HNLDVRPPFL AEAYKIICRD FGKERANQLF IENAQSILKN
     HYI
//