CPSB_STRA3
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 25-MAY-2022, entry version 103.
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; Firmicutes; 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 STRING; 211110.gbs1246; -.
DR EnsemblBacteria; CAD46906; CAD46906; CAD46906.
DR KEGG; san:cpsB; -.
DR eggNOG; COG4464; Bacteria.
DR HOGENOM; CLU_085966_1_0_9; -.
DR OMA; VHPERNS; -.
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 InterPro; IPR016667; Caps_polysacc_synth_CpsB/CapC.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR39181; PTHR39181; 1.
DR Pfam; PF19567; CpsB_CapC; 1.
DR PIRSF; PIRSF016557; Caps_synth_CpsB; 1.
DR SUPFAM; SSF51556; SSF51556; 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
