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erfK: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

ErfK

Synonyms

conserved protein with NAD(P)-binding Rossmann-fold domain[1], B1990[2][1], YzzT[2][1], YeeG[2][1], ErfK[2][1]

Product description

conserved protein with NAD(P)-binding Rossmann-fold domain[2][3]

L,D-transpeptidase linking Lpp to murein, periplasmic[4]

EC number (for enzymes)


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Notes

Function

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

QualifierGO IDGO term nameReference(s)Evidence Codewith/fromAspectNotesStatus
GO:0042597

periplasmic space

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0574

C

Seeded from EcoCyc 12.5 [5]

complete

GO:0005515

protein binding

PMID:16606699[6]

IPI: Inferred from Physical Interaction

UniProtKB:P0A717

F

Seeded from EcoCyc [7]

complete

GO:0008954

peptidoglycan synthetase activity

PMID:17369299[8]

IMP: Inferred from Mutant Phenotype

F

Seeded from EcoCyc 12.5 [5]

complete

GO:0008954

peptidoglycan synthetase activity

PMID:18456808[9]

IMP: Inferred from Mutant Phenotype

F

Seeded from EcoCyc 12.5 [5]

complete

GO:0010382

cell wall metabolic process

PMID:17369299[8]

IMP: Inferred from Mutant Phenotype

P

Seeded from EcoCyc 12.5 [5]

complete

GO:0010382

cell wall metabolic process

PMID:18456808[9]

IMP: Inferred from Mutant Phenotype

P

Seeded from EcoCyc 12.5 [5]

complete

GO:0016755

transferase activity, transferring amino-acyl groups

PMID:17369299[8]

IMP: Inferred from Mutant Phenotype

F

Seeded from EcoCyc 12.5 [5]

complete

GO:0016755

transferase activity, transferring amino-acyl groups

PMID:18456808[9]

IMP: Inferred from Mutant Phenotype

F

Seeded from EcoCyc 12.5 [5]

complete

GO:0016807

cysteine-type carboxypeptidase activity

PMID:17369299[8]

IMP: Inferred from Mutant Phenotype

F

Seeded from EcoCyc 12.5 [5]

complete

GO:0016807

cysteine-type carboxypeptidase activity

PMID:18456808[9]

IMP: Inferred from Mutant Phenotype

F

Seeded from EcoCyc 12.5 [5]

complete

GO:0018104

peptidoglycan-protein cross-linking

PMID:17369299[8]

IMP: Inferred from Mutant Phenotype

P

Seeded from EcoCyc 12.5 [5]

complete

GO:0018104

peptidoglycan-protein cross-linking

PMID:18456808[9]

IMP: Inferred from Mutant Phenotype

P

Seeded from EcoCyc 12.5 [5]

complete

GO:0043164

Gram-negative-bacterium-type cell wall biogenesis

PMID:17369299[8]

IMP: Inferred from Mutant Phenotype

P

Seeded from EcoCyc 12.5 [5]

complete

GO:0043164

Gram-negative-bacterium-type cell wall biogenesis

PMID:18456808[9]

IMP: Inferred from Mutant Phenotype

P

Seeded from EcoCyc 12.5 [5]

complete

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

Partner TypePartnerNotesReferencesEvidence

Protein

prs

PMID:16606699[6]

Experiment(s):EBI-1141581

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Notes

Localization

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

CompartmentDescriptionEvidenceSourceNotes

Periplasm

PMID:9298646[10]

EchoLocation:erfK


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Notes

Structure and Physical Properties

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

Sequence

at EcoCyc 

MRRVNILCSF ALLFASHTSL AVTYPLPPEG SRLVGQSFTV TVPDHNTQPL ETFAAQYGQG
LSNMLEANPG ADVFLPKSGS QLTIPQQLIL PDTVRKGIVV NVAEMRLYYY PPDSNTVEVF
PIGIGQAGRE TPRNWVTTVE RKQEAPTWTP TPNTRREYAK RGESLPAFVP AGPDNPMGLY
AIYIGRLYAI HGTNANFGIG LRVSQGCIRL RNDDIKYLFD NVPVGTRVQI IDQPVKYTTE
PDGSNWLEVH EPLSRNRAEY ESDRKVPLPV TPSLRAFING QEVDVNRANA ALQRRSGMPV
QISSGSRQMF
Length

310

Mol. Wt

34.41 kDa

pI

9.1 (calculated)

Extinction coefficient

34,380 - 34,630 (calc based on 12 Y, 3 W, and 2 C residues)

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Domains/Motifs/Modification Sites

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

TypeResiduesDescriptionNotesReferences

motif

1-21

UniProt Manual:Signal Peptides

UniProt:P39176


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rectanglemotifs

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

Structures
Models

View models at:

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Structure figures

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 typeSourceNotes/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.

DatabaseAccessionNotes

EcoCyc (EcoliWiki Page)

EcoCyc:G7073-MONOMER

UniProt (EcoliWiki Page)

UniProt:P39176

PFAM (EcoliWiki Page)

PFAM:PF03734

RefSeq (EcoliWiki Page)

RefSeq:NP_416494


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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 2.4 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  3. ↑ 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. ↑ 5.00 5.01 5.02 5.03 5.04 5.05 5.06 5.07 5.08 5.09 5.10 5.11 5.12 EcoCyc (release 12.5; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  6. ↑ 6.0 6.1 Arifuzzaman M et al. (2006) Large-scale identification of protein-protein interaction of Escherichia coli K-12. Genome Res 16: 686-91 PubMed EcoliWiki page
  7. ↑ EcoCyc (release 13.0; 2009) Keseler, IM et al. (2009) Nucleic Acids Res. 37(Database issue):D464-70
  8. ↑ 8.0 8.1 8.2 8.3 8.4 8.5 Magnet S et al. (2007) Identification of the L,D-transpeptidases responsible for attachment of the Braun lipoprotein to Escherichia coli peptidoglycan. J Bacteriol 189: 3927-31 PubMed EcoliWiki page
  9. ↑ 9.0 9.1 9.2 9.3 9.4 9.5 Magnet S et al. (2008) Identification of the L,D-transpeptidases for peptidoglycan cross-linking in Escherichia coli. J Bacteriol 190: 4782-5 PubMed EcoliWiki page
  10. ↑ Link AJ et al. (1997) Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12. Electrophoresis 18: 1259-313 PubMed EcoliWiki page

Categories

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