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P0AE23 (APHA_SHIFL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Class B acid phosphatase

Short name=CBAP
EC=3.1.3.2
Gene names
Name:aphA
Ordered Locus Names:SF4149, S3580
OrganismShigella flexneri [Complete proteome] [HAMAP]
Taxonomic identifier623 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella

Protein attributes

Sequence length237 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Dephosphorylates several organic phosphate monoesters. Also has a phosphotransferase activity catalyzing the transfer of low-energy phosphate groups from organic phosphate monoesters to free hydroxyl groups of various organic compounds By similarity.

Catalytic activity

A phosphate monoester + H2O = an alcohol + phosphate.

Cofactor

Binds 1 magnesium ion per subunit By similarity.

Subunit structure

Homotetramer By similarity.

Subcellular location

Periplasm By similarity.

Sequence similarities

Belongs to the class B bacterial acid phosphatase family.

Ontologies

Keywords
   Cellular componentPeriplasm
   DomainSignal
   LigandMagnesium
Metal-binding
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Cellular_componentouter membrane-bounded periplasmic space

Inferred from electronic annotation. Source: InterPro

   Molecular_functionacid phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525Or 23 Potential
Chain26 – 237212Class B acid phosphatase
PRO_0000043379

Regions

Region137 – 1382Substrate binding By similarity

Sites

Active site691Nucleophile By similarity
Active site711Proton donor By similarity
Metal binding691Magnesium By similarity
Metal binding711Magnesium; via carbonyl oxygen By similarity
Metal binding1921Magnesium By similarity
Binding site1771Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
P0AE23 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: 35C1BFE6DF9E530D

FASTA23726,104
        10         20         30         40         50         60 
MRKITQAISA VCLLFALNSS AVALASSPSP LNPGTNVARL AEQAPIHWVS VAQIENSLAG 

        70         80         90        100        110        120 
RPPMAVGFDI DDTVLFSSPG FWRGKKTFSP ESEDYLKNPV FWEKMNNGWD EFSIPKEVAR 

       130        140        150        160        170        180 
QLIDMHVRRG DAIFFVTGRS PTKTETVSKT LADNFHIPAT NMNPVIFAGD KPGQNTKSQW 

       190        200        210        220        230 
LQDKNIRIFY GDSDNDITAA RDVGARGIRI LRASNSTYKP LPQAGAFGEE VIVNSEY 

« Hide

References

[1]"Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157."
Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y. expand/collapse author list , Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.
Nucleic Acids Res. 30:4432-4441(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 301 / Serotype 2a.
[2]"Complete genome sequence and comparative genomics of Shigella flexneri serotype 2a strain 2457T."
Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.
Infect. Immun. 71:2775-2786(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700930 / 2457T / Serotype 2a.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE005674 Genomic DNA. Translation: AAN45571.2.
AE014073 Genomic DNA. Translation: AAP18626.1.
RefSeqNP_709864.2. NC_004337.2.
NP_838815.1. NC_004741.1.

3D structure databases

ProteinModelPortalP0AE23.
SMRP0AE23. Positions 27-237.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING198214.SF4149.

Proteomic databases

PaxDbP0AE23.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN45571; AAN45571; SF4149.
AAP18626; AAP18626; S3580.
GeneID1027006.
1079802.
KEGGsfl:SF4149.
sfx:S3580.
PATRIC18708940. VBIShiFle31049_3908.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3700.
HOGENOMHOG000270623.
KOK03788.
OrthoDBEOG6HTNVZ.
ProtClustDBPRK11009.

Family and domain databases

Gene3D3.40.50.1000. 1 hit.
InterProIPR005519. Acid_phosphat_B.
IPR023214. HAD-like_dom.
IPR010025. HAD-SF_ppase_IIIB_AphA.
[Graphical view]
PfamPF03767. Acid_phosphat_B. 1 hit.
[Graphical view]
PIRSFPIRSF017818. Acid_Ptase_B. 1 hit.
SUPFAMSSF56784. SSF56784. 1 hit.
TIGRFAMsTIGR01672. AphA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameAPHA_SHIFL
AccessionPrimary (citable) accession number: P0AE23
Secondary accession number(s): P32697, P76787, Q57085
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: December 6, 2005
Last modified: April 16, 2014
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families