ansB:Gene Product(s)

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Nomenclature Function Interactions Localization Sequence Domains Structure Resources Accessions Links References Suggestions

Nomenclature

See Help:Product_nomenclature for help entering or editing information in this section of EcoliWiki.

Standard name

AnsB

Synonyms

periplasmic L-asparaginase II[1], B2957[2][1], AnsB[2][1] , ECK2952, JW2924, b2957

Product description

AnsB[2][3];

Component of asparaginase II[2][3]

L-Asparaginase II[4]

EC number (for enzymes)

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Notes

Function

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<protect> Gene Ontology
See Help:Gene_ontology for help entering or editing GO terms and GO annotations in EcoliWiki.

Qualifier GO ID GO term name Reference Evidence Code with/from Aspect Notes Status
GO:0030288

outer membrane-bounded periplasmic space

C

Seeded from Riley et al 2006 [1].

Missing: evidence, reference

GO:0004067

asparaginase activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR004550

F

Seeded from EcoCyc (v14.0)

complete

GO:0004067

asparaginase activity

GOA:spec
GO_REF:0000003

IEA: Inferred from Electronic Annotation

EC:3.5.1.1

F

Seeded from EcoCyc (v14.0)

complete

GO:0005829

cytosol

PMID:16858726[5]

IDA: Inferred from Direct Assay

C

Seeded from EcoCyc (v14.0)

complete

GO:0006520

cellular amino acid metabolic process

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR006034

P

Seeded from EcoCyc (v14.0)

complete

GO:0006520

cellular amino acid metabolic process

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR020827

P

Seeded from EcoCyc (v14.0)

complete

GO:0006528

asparagine metabolic process

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR004550

P

Seeded from EcoCyc (v14.0)

complete

GO:0016787

hydrolase activity

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0378

F

Seeded from EcoCyc (v14.0)

complete

GO:0042597

periplasmic space

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0574

C

Seeded from EcoCyc (v14.0)

complete

GO:0042597

periplasmic space

GO_REF:0000023

IEA: Inferred from Electronic Annotation

SP_SL:SL-0200

C

Seeded from EcoCyc (v14.0)

complete

GO:0042597

periplasmic space

PMID:2407723[6]

ISM: Inferred from Sequence Model

PMID:3714490[7]


C

predicted signal sequence

complete

Interactions See Help:Product_interactions for help entering or editing information about gene product interactions in this section of EcoliWiki.

Partner Type Partner Notes References Evidence

Protein

Subunits of asparaginase II

could be indirect

Protein

visC

PMID:16606699[8]

Experiment(s):EBI-1144449

Protein

insI1

PMID:16606699[8]

Experiment(s):EBI-1144449

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Notes

Localization

See Help:Product_localization for how to add or edit information in this section of EcoliWiki.

Compartment Description Evidence Reference/Source Notes

periplasm

From EcoCyc[3]

Periplasm

PMID:387570[9], PMID:2407723[6]

EchoLocation:ansB


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Notes

Structure and Physical Properties

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<protect> Physical Properties See Help:Product_physical_properties for help entering or editing information about the physical properties of this gene product.

Name
Sequence

at EcoCyc

MEFFKKTALA ALVMGFSGAA LALPNITILA TGGTIAGGGD SATKSNYTVG KVGVENLVNA
VPQLKDIANV KGEQVVNIGS QDMNDNVWLT LAKKINTDCD KTDGFVITHG TDTMEETAYF
LDLTVKCDKP VVMVGAMRPS TSMSADGPFN LYNAVVTAAD KASANRGVLV VMNDTVLDGR
DVTKTNTTDV ATFKSVNYGP LGYIHNGKID YQRTPARKHT SDTPFDVSKL NELPKVGIVY
NYANASDLPA KALVDAGYDG IVSAGVGNGN LYKSVFDTLA TAAKTGTAVV RSSRVPTGAT
TQDAEVDDAK YGFVASGTLN PQKARVLLQL ALTQTKDPQQ IQQIFNQY
Length

348

Mol. Wt

36.85 kDa

pI

6.3 (calculated)

Extinction coefficient

23,380 - 23,630 (calc based on 12 Y, 1 W, and 2 C residues)


Domains/Motifs/Modification Sites

See Help:Product_domains_motifs for help entering or editing information in this section of EcoliWiki.

Type Residues Description Notes References

motif

1-22

UniProt Manual:Signal Peptides

UniProt:P00805

Domain

25..342

PF00710 Asparaginase

PMID:19920124[10]

<motif_map/>

Structure
See Help:Product_structure for help entering or editing information in this section of EcoliWiki.

Structures

<beststructure> gene=ansB taxon=562,83333 </beststructure>

Models

View models at:

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Structure figures

<protect>

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Notes

Gene Product Resources

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See Help:Product_resources for help with entering or editing information in this section of EcoliWiki.

Resource type Source Notes/Reference

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Notes

Accessions in Other Databases

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See Help:Gene_accessions for help with entering information into the Gene Accessions table.

Database Accession Notes

NCBI (Protein) (EcoliWiki Page)

GI:16130858

Escherichia coli str. K-12 substr. MG1655

NCBI (Protein) (EcoliWiki Page)

GeneID:947454

Escherichia coli str. K-12 substr. MG1655

ASAP

ASAP:ABE-0009700

Escherichia coli str. K-12 substr. MG1655

UniProt (EcoliWiki Page)

UniProtKB/Swiss-Prot:P00805

Escherichia coli str. K-12 substr. MG1655

EcoCyc

EcoCyc:EG10046

Escherichia coli str. K-12 substr. MG1655

EcoGene

EcoGene:EG10046

Escherichia coli str. K-12 substr. MG1655

NCBI (Gene) (EcoliWiki Page)

GeneID:947454

Escherichia coli str. K-12 substr. MG1655

RegulonDB

RegulonDB:ECK120000042

Escherichia coli str. K-12 substr. MG1655

EchoBASE

EchoBASE:EB0044

Escherichia coli str. K-12 substr. MG1655

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Notes

Links

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References

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See Help:References for how to manage references in EcoliWiki.

  1. 1.0 1.1 1.2 1.3 1.4 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
  2. 2.0 2.1 2.2 2.3 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  3. 3.0 3.1 3.2 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  4. EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.
  5. Lasserre, JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27 3306-21 PubMed
  6. 6.0 6.1 Jennings, MP & Beacham, IR (1990) Analysis of the Escherichia coli gene encoding L-asparaginase II, ansB, and its regulation by cyclic AMP receptor and FNR proteins. J. Bacteriol. 172 1491-8 PubMed
  7. von Heijne, G (1986) A new method for predicting signal sequence cleavage sites. Nucleic Acids Res. 14 4683-90 PubMed
  8. 8.0 8.1 Arifuzzaman, M et al. (2006) Large-scale identification of protein-protein interaction of Escherichia coli K-12. Genome Res. 16 686-91 PubMed
  9. Maita, T et al. (1979) Amino acid sequences of the tryptic peptides from carboxymethylated L-asparaginase from Escherichia coli. Hoppe-Seyler's Z. Physiol. Chem. 360 1483-95 PubMed
  10. Finn, RD et al. (2010) The Pfam protein families database. Nucleic Acids Res. 38 D211-22 PubMed

Categories

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