CPSB_STRPN
ID CPSB_STRPN Reviewed; 243 AA.
AC Q9AHD4;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Tyrosine-protein phosphatase CpsB;
DE EC=3.1.3.48;
GN Name=cpsB; Synonyms=wzh; OrderedLocusNames=SP_0347;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=WCH35 / Serotype 4;
RX PubMed=11179285; DOI=10.1128/iai.69.3.1244-1255.2001;
RA Jiang S.-M., Wang L., Reeves P.R.;
RT "Molecular characterization of Streptococcus pneumoniae type 4, 6B, 8, and
RT 18C capsular polysaccharide gene clusters.";
RL Infect. Immun. 69:1244-1255(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
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; AF316639; AAK20667.1; -; Genomic_DNA.
DR EMBL; AE005672; AAK74520.1; -; Genomic_DNA.
DR PIR; G95040; G95040.
DR RefSeq; WP_000565352.1; NZ_AKVY01000001.1.
DR PDB; 2WJD; X-ray; 2.80 A; A=1-243.
DR PDB; 2WJE; X-ray; 1.90 A; A=1-243.
DR PDB; 2WJF; X-ray; 2.22 A; A=1-243.
DR PDB; 3QY8; X-ray; 2.00 A; A=1-243.
DR PDBsum; 2WJD; -.
DR PDBsum; 2WJE; -.
DR PDBsum; 2WJF; -.
DR PDBsum; 3QY8; -.
DR AlphaFoldDB; Q9AHD4; -.
DR SMR; Q9AHD4; -.
DR STRING; 170187.SP_0347; -.
DR EnsemblBacteria; AAK74520; AAK74520; SP_0347.
DR KEGG; spn:SP_0347; -.
DR eggNOG; COG4464; Bacteria.
DR OMA; VHPERNS; -.
DR PhylomeDB; Q9AHD4; -.
DR BioCyc; SPNE170187:G1FZB-357-MON; -.
DR UniPathway; UPA00934; -.
DR EvolutionaryTrace; Q9AHD4; -.
DR Proteomes; UP000000585; 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 1: Evidence at protein level;
KW 3D-structure; Capsule biogenesis/degradation; Exopolysaccharide synthesis;
KW Hydrolase; Manganese; Protein phosphatase.
FT CHAIN 1..243
FT /note="Tyrosine-protein phosphatase CpsB"
FT /id="PRO_0000057891"
FT STRAND 1..3
FT /evidence="ECO:0007829|PDB:2WJE"
FT STRAND 12..15
FT /evidence="ECO:0007829|PDB:2WJE"
FT HELIX 19..31
FT /evidence="ECO:0007829|PDB:2WJE"
FT STRAND 34..38
FT /evidence="ECO:0007829|PDB:2WJE"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:2WJE"
FT TURN 45..47
FT /evidence="ECO:0007829|PDB:2WJE"
FT HELIX 52..69
FT /evidence="ECO:0007829|PDB:2WJE"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:2WJE"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:2WJE"
FT HELIX 87..92
FT /evidence="ECO:0007829|PDB:2WJE"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:2WJE"
FT STRAND 102..108
FT /evidence="ECO:0007829|PDB:2WJE"
FT HELIX 115..126
FT /evidence="ECO:0007829|PDB:2WJE"
FT TURN 127..129
FT /evidence="ECO:0007829|PDB:2WJE"
FT STRAND 131..134
FT /evidence="ECO:0007829|PDB:2WJE"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:2WJE"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:2WJE"
FT HELIX 147..155
FT /evidence="ECO:0007829|PDB:2WJE"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:2WJE"
FT HELIX 164..167
FT /evidence="ECO:0007829|PDB:2WJE"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:3QY8"
FT HELIX 178..189
FT /evidence="ECO:0007829|PDB:2WJE"
FT STRAND 194..197
FT /evidence="ECO:0007829|PDB:2WJE"
FT STRAND 203..206
FT /evidence="ECO:0007829|PDB:2WJE"
FT HELIX 210..221
FT /evidence="ECO:0007829|PDB:2WJE"
FT HELIX 223..230
FT /evidence="ECO:0007829|PDB:2WJE"
FT HELIX 232..238
FT /evidence="ECO:0007829|PDB:2WJE"
SQ SEQUENCE 243 AA; 28131 MW; 1171C4A506FDE0D5 CRC64;
MIDIHSHIVF DVDDGPKSRE ESKALLAESY RQGVRTIVST SHRRKGMFET PEEKIAENFL
QVREIAKEVA SDLVIAYGAE IYYTPDVLDK LEKKRIPTLN DSRYALIEFS MNTPYRDIHS
ALSKILMLGI TPVIAHIERY DALENNEKRV RELIDMGCYT QVNSSHVLKP KLFGERYKFM
KKRAQYFLEQ DLVHVIASDM HNLDGRPPHM AEAYDLVTQK YGEAKAQELF IDNPRKIVMD
QLI
