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Protein

Tyrosine-protein phosphatase CpsB

Gene

cpsB

Organism
Streptococcus pneumoniae
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Dephosphorylates CpsD. Involved in the regulation of capsular polysaccharide biosynthesis.

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Cofactori

Pathway: capsule polysaccharide biosynthesis

This protein is involved in the pathway capsule polysaccharide biosynthesis, which is part of Capsule biogenesis.
View all proteins of this organism that are known to be involved in the pathway capsule polysaccharide biosynthesis and in Capsule biogenesis.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Capsule biogenesis/degradation, Exopolysaccharide synthesis

Keywords - Ligandi

Manganese

Enzyme and pathway databases

UniPathwayiUPA00934.

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein phosphatase CpsB (EC:3.1.3.48)
Gene namesi
Name:cpsB
Synonyms:cap1B, cps19fB
OrganismiStreptococcus pneumoniae
Taxonomic identifieri1313 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi199 – 1991D → N: Loss of activity; when associated with Q-201. 1 Publication
Mutagenesisi201 – 2011H → Q: Loss of activity; when associated with N-199. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 243243Tyrosine-protein phosphatase CpsBPRO_0000057892Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ54518.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the CpsB/CapC family.Curated

Family and domain databases

InterProiIPR016667. Caps_polysacc_synth_CpsB/CapC.
IPR004013. PHP_C.
[Graphical view]
PfamiPF02811. PHP. 1 hit.
[Graphical view]
PIRSFiPIRSF016557. Caps_synth_CpsB. 1 hit.

Sequencei

Sequence statusi: Complete.

Q54518-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIDIHSHIVF DVDDGPKSRE ESKALLAESY RQGVRTIVST SHRRKGMFET
60 70 80 90 100
PEEKIAENFL QVREIAKEVA DDLVIAYGAE IYYTLDALEK LEKKEIPTLN
110 120 130 140 150
DSRYALIEFS MHTSYRQIHT GLSNILMLGI TPVIAHIERY DALENNEKRV
160 170 180 190 200
RELIDMGCYT QINSYHVSKP KFFGEKYKFM KKRARYFLER DLVHVVASDM
210 220 230 240
HNLDSRPPYM QQAYDIIAKK YGAKKAKELF VDNPRKIIMD QLI
Length:243
Mass (Da):28,354
Last modified:November 1, 1996 - v1
Checksum:i810A4C802EC43079
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti226 – 2261A → V in strain: NCTC 11906.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U09239 Genomic DNA. Translation: AAC44959.1.
Z83335 Genomic DNA. Translation: CAB05935.1.
AF030367 Genomic DNA. Translation: AAC38717.1.
AF030368 Genomic DNA. Translation: AAC38722.1.
AF030369 Genomic DNA. Translation: AAC38727.1.
AF030370 Genomic DNA. Translation: AAC38731.1.
AF030371 Genomic DNA. Translation: AAC38736.1.
AF030372 Genomic DNA. Translation: AAC38741.1.
AF106137 Genomic DNA. Translation: AAD17985.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U09239 Genomic DNA. Translation: AAC44959.1.
Z83335 Genomic DNA. Translation: CAB05935.1.
AF030367 Genomic DNA. Translation: AAC38717.1.
AF030368 Genomic DNA. Translation: AAC38722.1.
AF030369 Genomic DNA. Translation: AAC38727.1.
AF030370 Genomic DNA. Translation: AAC38731.1.
AF030371 Genomic DNA. Translation: AAC38736.1.
AF030372 Genomic DNA. Translation: AAC38741.1.
AF106137 Genomic DNA. Translation: AAD17985.1.

3D structure databases

ProteinModelPortaliQ54518.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00934.

Family and domain databases

InterProiIPR016667. Caps_polysacc_synth_CpsB/CapC.
IPR004013. PHP_C.
[Graphical view]
PfamiPF02811. PHP. 1 hit.
[Graphical view]
PIRSFiPIRSF016557. Caps_synth_CpsB. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Nucleotide sequence analysis of genes essential for capsular polysaccharide biosynthesis in Streptococcus pneumoniae type 19F."
    Guidolin A., Morona J.K., Morona R., Hansman D., Paton J.C.
    Infect. Immun. 62:5384-5396(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Serotype 19F.
  2. "Molecular organization of the genes required for the synthesis of type 1 capsular polysaccharide of Streptococcus pneumoniae: formation of binary encapsulated pneumococci and identification of cryptic dTDP-rhamnose biosynthesis genes."
    Munoz R., Mollerach M.E., Lopez R., Garcia E.
    Mol. Microbiol. 25:79-92(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Recombinational exchanges at the capsular polysaccharide biosynthetic locus lead to frequent serotype changes among natural isolates of Streptococcus pneumoniae."
    Coffey T.J., Enright M.C., Daniels M., Morona J.K., Morona R., Hryniewicz W., Paton J.C., Spratt B.G.
    Mol. Microbiol. 27:73-83(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: NCTC 11906 / Serotype 19F, PO-329 / Serotype 19F, SP-496 / Serotype 19F, SP-GA71 / Serotype 19F, SP-VA92 / Serotype 19F and SP-VA96 / Serotype 19F.
  4. "Analysis of capsule loci from various Streptococcus pneumoniae serotypes using long-range PCR identifies two classes of cpsC."
    Morona J.K., Morona R., Paton J.C.
    Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 220-243.
    Strain: Serotype 19B.
  5. "Streptococcus pneumoniae capsule biosynthesis protein CpsB is a novel manganese-dependent phosphotyrosine-protein phosphatase."
    Morona J.K., Morona R., Miller D.C., Paton J.C.
    J. Bacteriol. 184:577-583(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, MUTAGENESIS OF ASP-199 AND HIS-201.
    Strain: Rx1-19F / Serotype 19F.

Entry informationi

Entry nameiCPSB_STREE
AccessioniPrimary (citable) accession number: Q54518
Secondary accession number(s): O08049, O08278, O52232
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2003
Last sequence update: November 1, 1996
Last modified: March 4, 2015
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.