CPSB_STRA5
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 25-MAY-2022, entry version 80.
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; Firmicutes; 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 EnsemblBacteria; AAN00056; AAN00056; SAG1174.
DR KEGG; sag:SAG1174; -.
DR PATRIC; fig|208435.3.peg.1180; -.
DR HOGENOM; CLU_085966_1_0_9; -.
DR OMA; VHPERNS; -.
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 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; 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