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Entry version 183 (11 Dec 2019)
Sequence version 2 (23 Jan 2007)
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Protein

UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase

Gene

murE

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. Is also able to use many meso-diaminopimelate analogs as substrates, although much less efficiently, but not L-lysine.3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+UniRule annotation

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Activated by potassium phosphate.1 Publication

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=76 µM for UDP-N-acetylmuramoyl-L-Ala-D-Glu2 Publications
  2. KM=36 µM for meso-diaminopimelate2 Publications
  3. KM=1500 µM for meso-lanthionine2 Publications
  4. KM=3900 µM for L-allo-cystathionine2 Publications
  5. KM=10000 µM for D-allo-cystathionine2 Publications
  6. KM=620 µM for ATP2 Publications
  1. Vmax=32 nmol/min/mg enzyme with meso-diaminopimelate as substrate2 Publications
  2. Vmax=23 nmol/min/mg enzyme with meso-lanthionine as substrate2 Publications
  3. Vmax=19 nmol/min/mg enzyme with L-allo-cystathionine as substrate2 Publications
  4. Vmax=23 nmol/min/mg enzyme with L-allo-cystathionine as substrate2 Publications

pH dependencei

Optimum pH is about 8.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: peptidoglycan biosynthesis

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei27UDP-MurNAc-L-Ala-D-Glu; via carbonyl oxygen1
Binding sitei29UDP-MurNAc-L-Ala-D-Glu1
Binding sitei157UDP-MurNAc-L-Ala-D-Glu1
Binding sitei185UDP-MurNAc-L-Ala-D-Glu1
Binding sitei191UDP-MurNAc-L-Ala-D-Glu1
Binding sitei193UDP-MurNAc-L-Ala-D-Glu1
Binding sitei390Meso-diaminopimelate1
Binding sitei465Meso-diaminopimelate; via carbonyl oxygen1
Binding sitei469Meso-diaminopimelate1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi116 – 122ATPSequence analysis7

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

  • cell cycle Source: UniProtKB-KW
  • cell division Source: UniProtKB-KW
  • cell wall organization Source: UniProtKB-KW
  • peptidoglycan biosynthetic process Source: EcoCyc
  • regulation of cell shape Source: UniProtKB-KW

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionLigase
Biological processCell cycle, Cell division, Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis
LigandATP-binding, Magnesium, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:UDP-NACMURALGLDAPLIG-MONOMER
ECOL316407:JW0083-MONOMER
MetaCyc:UDP-NACMURALGLDAPLIG-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
6.3.2.13 2026

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00219

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase (EC:6.3.2.132 Publications)
Alternative name(s):
Meso-A2pm-adding enzyme
Meso-diaminopimelate-adding enzyme
UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligase
UDP-MurNAc-tripeptide synthetase
UDP-N-acetylmuramyl-tripeptide synthetase
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:murE
Ordered Locus Names:b0085, JW0083
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3309032

Drug and drug target database

More...
DrugBanki
DB03590 2,6-Diaminopimelic Acid
DB03801 Lysine Nz-Carboxylic Acid
DB02314 Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine-D-Glutamate

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved2 Publications
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001018932 – 495UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligaseAdd BLAST494

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei225N6-carboxylysine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Carboxylation is probably crucial for Mg2+ binding and, consequently, for the gamma-phosphate positioning of ATP.1 Publication

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P22188

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P22188

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P22188

PRoteomics IDEntifications database

More...
PRIDEi
P22188

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

More...
SWISS-2DPAGEi
P22188

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Show more details

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
4261641, 527 interactors
849192, 4 interactors

Database of interacting proteins

More...
DIPi
DIP-10280N

Protein interaction database and analysis system

More...
IntActi
P22188, 20 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b0085

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P22188

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1495
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P22188

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P22188

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni44 – 46UDP-MurNAc-L-Ala-D-Glu binding3
Regioni158 – 159UDP-MurNAc-L-Ala-D-Glu binding2
Regioni414 – 417Meso-diaminopimelate binding4

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi414 – 417Meso-diaminopimelate recognition motif4

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the MurCDEF family. MurE subfamily.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4107EEN Bacteria
COG0769 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000268118

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P22188

KEGG Orthology (KO)

More...
KOi
K01928

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P22188

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.1190.10, 1 hit
3.90.190.20, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_00208 MurE, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR036565 Mur-like_cat_sf
IPR004101 Mur_ligase_C
IPR036615 Mur_ligase_C_dom_sf
IPR013221 Mur_ligase_cen
IPR000713 Mur_ligase_N
IPR035911 MurE/MurF_N
IPR005761 UDP-N-AcMur-Glu-dNH2Pim_ligase

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01225 Mur_ligase, 1 hit
PF02875 Mur_ligase_C, 1 hit
PF08245 Mur_ligase_M, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF53244 SSF53244, 1 hit
SSF53623 SSF53623, 1 hit
SSF63418 SSF63418, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01085 murE, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P22188-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MADRNLRDLL APWVPDAPSR ALREMTLDSR VAAAGDLFVA VVGHQADGRR
60 70 80 90 100
YIPQAIAQGV AAIIAEAKDE ATDGEIREMH GVPVIYLSQL NERLSALAGR
110 120 130 140 150
FYHEPSDNLR LVGVTGTNGK TTTTQLLAQW SQLLGEISAV MGTVGNGLLG
160 170 180 190 200
KVIPTENTTG SAVDVQHELA GLVDQGATFC AMEVSSHGLV QHRVAALKFA
210 220 230 240 250
ASVFTNLSRD HLDYHGDMEH YEAAKWLLYS EHHCGQAIIN ADDEVGRRWL
260 270 280 290 300
AKLPDAVAVS MEDHINPNCH GRWLKATEVN YHDSGATIRF SSSWGDGEIE
310 320 330 340 350
SHLMGAFNVS NLLLALATLL ALGYPLADLL KTAARLQPVC GRMEVFTAPG
360 370 380 390 400
KPTVVVDYAH TPDALEKALQ AARLHCAGKL WCVFGCGGDR DKGKRPLMGA
410 420 430 440 450
IAEEFADVAV VTDDNPRTEE PRAIINDILA GMLDAGHAKV MEGRAEAVTC
460 470 480 490
AVMQAKENDV VLVAGKGHED YQIVGNQRLD YSDRVTVARL LGVIA
Length:495
Mass (Da):53,344
Last modified:January 23, 2007 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iD4A7A3E56D6C7E49
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti344E → K in murE1. 1
Natural varianti495A → S in murE1. 1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X55814 Genomic DNA Translation: CAA39334.1
X55034 Genomic DNA Translation: CAA38862.1
U00096 Genomic DNA Translation: AAC73196.1
AP009048 Genomic DNA Translation: BAB96653.1
U67894 Genomic DNA Translation: AAB60789.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S14384

NCBI Reference Sequences

More...
RefSeqi
NP_414627.1, NC_000913.3
WP_000775093.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC73196; AAC73196; b0085
BAB96653; BAB96653; BAB96653

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
944791

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW0083
eco:b0085

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.2195

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X55814 Genomic DNA Translation: CAA39334.1
X55034 Genomic DNA Translation: CAA38862.1
U00096 Genomic DNA Translation: AAC73196.1
AP009048 Genomic DNA Translation: BAB96653.1
U67894 Genomic DNA Translation: AAB60789.1
PIRiS14384
RefSeqiNP_414627.1, NC_000913.3
WP_000775093.1, NZ_LN832404.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1E8CX-ray2.00A/B2-495[»]
SMRiP22188
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi4261641, 527 interactors
849192, 4 interactors
DIPiDIP-10280N
IntActiP22188, 20 interactors
STRINGi511145.b0085

Chemistry databases

BindingDBiP22188
ChEMBLiCHEMBL3309032
DrugBankiDB03590 2,6-Diaminopimelic Acid
DB03801 Lysine Nz-Carboxylic Acid
DB02314 Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine-D-Glutamate

2D gel databases

SWISS-2DPAGEiP22188

Proteomic databases

EPDiP22188
jPOSTiP22188
PaxDbiP22188
PRIDEiP22188

Genome annotation databases

EnsemblBacteriaiAAC73196; AAC73196; b0085
BAB96653; BAB96653; BAB96653
GeneIDi944791
KEGGiecj:JW0083
eco:b0085
PATRICifig|1411691.4.peg.2195

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...
EchoBASEi
EB0616

Phylogenomic databases

eggNOGiENOG4107EEN Bacteria
COG0769 LUCA
HOGENOMiHOG000268118
InParanoidiP22188
KOiK01928
PhylomeDBiP22188

Enzyme and pathway databases

UniPathwayiUPA00219
BioCyciEcoCyc:UDP-NACMURALGLDAPLIG-MONOMER
ECOL316407:JW0083-MONOMER
MetaCyc:UDP-NACMURALGLDAPLIG-MONOMER
BRENDAi6.3.2.13 2026

Miscellaneous databases

EvolutionaryTraceiP22188

Protein Ontology

More...
PROi
PR:P22188

Family and domain databases

Gene3Di3.40.1190.10, 1 hit
3.90.190.20, 1 hit
HAMAPiMF_00208 MurE, 1 hit
InterProiView protein in InterPro
IPR036565 Mur-like_cat_sf
IPR004101 Mur_ligase_C
IPR036615 Mur_ligase_C_dom_sf
IPR013221 Mur_ligase_cen
IPR000713 Mur_ligase_N
IPR035911 MurE/MurF_N
IPR005761 UDP-N-AcMur-Glu-dNH2Pim_ligase
PfamiView protein in Pfam
PF01225 Mur_ligase, 1 hit
PF02875 Mur_ligase_C, 1 hit
PF08245 Mur_ligase_M, 1 hit
SUPFAMiSSF53244 SSF53244, 1 hit
SSF53623 SSF53623, 1 hit
SSF63418 SSF63418, 1 hit
TIGRFAMsiTIGR01085 murE, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiMURE_ECOLI
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P22188
Secondary accession number(s): O07101
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: January 23, 2007
Last modified: December 11, 2019
This is version 183 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
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