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Q54518

- CPSB_STREE

UniProt

Q54518 - CPSB_STREE

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Protein
Tyrosine-protein phosphatase CpsB
Gene
cpsB, cap1B, cps19fB
Organism
Streptococcus pneumoniae
Status
Reviewed - 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

Manganese.

Pathwayi

GO - Molecular functioni

  1. manganese ion binding Source: InterPro
  2. protein tyrosine phosphatase activity Source: UniProtKB-EC

GO - Biological processi

  1. capsule polysaccharide biosynthetic process Source: UniProtKB-UniPathway
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.

Protein family/group databases

PptaseDBiP3D0411155.

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 CpsB
PRO_0000057892Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ54518.

Family & Domainsi

Sequence similaritiesi

Belongs to the CpsB/CapC family.

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

MIDIHSHIVF DVDDGPKSRE ESKALLAESY RQGVRTIVST SHRRKGMFET    50
PEEKIAENFL QVREIAKEVA DDLVIAYGAE IYYTLDALEK LEKKEIPTLN 100
DSRYALIEFS MHTSYRQIHT GLSNILMLGI TPVIAHIERY DALENNEKRV 150
RELIDMGCYT QINSYHVSKP KFFGEKYKFM KKRARYFLER DLVHVVASDM 200
HNLDSRPPYM QQAYDIIAKK YGAKKAKELF VDNPRKIIMD QLI 243
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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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

ProteinModelPortali Q54518.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

PptaseDBi P3D0411155.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00934 .

Family and domain databases

InterProi IPR016667. Caps_polysacc_synth_CpsB/CapC.
IPR004013. PHP_C.
[Graphical view ]
Pfami PF02811. PHP. 1 hit.
[Graphical view ]
PIRSFi PIRSF016557. Caps_synth_CpsB. 1 hit.
ProtoNeti Search...

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: April 16, 2014
This is version 59 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

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