UniProtKB - P14900 (MURD_ECOLI)

BLAST

>sp|P14900|MURD_ECOLI UDP-N-acetylmuramoylalanine--D-glutamate ligase OS=Escherichia coli (strain K12) OX=83333 GN=murD PE=1 SV=3
MADYQGKNVVIIGLGLTGLSCVDFFLARGVTPRVMDTRMTPPGLDKLPEAVERHTGSLND
EWLMAADLIVASPGIALAHPSLSAAADAGIEIVGDIELFCREAQAPIVAITGSNGKSTVT
TLVGEMAKAAGVNVGVGGNIGLPALMLLDDECELYVLELSSFQLETTSSLQAVAATILNV
TEDHMDRYPFGLQQYRAAKLRIYENAKVCVVNADDALTMPIRGADERCVSFGVNMGDYHL
NHQQGETWLRVKGEKVLNVKEMKLSGQHNYTNALAALALADAAGLPRASSLKALTTFTGL
PHRFEVVLEHNGVRWINDSKATNVGSTEAALNGLHVDGTLHLLLGGDGKSADFSPLARYL
NGDNVRLYCFGRDGAQLAALRPEVAEQTETMEQAMRLLAPRVQPGDMVLLSPACASLDQF
KNFEQRGNEFARLAKELG

Align
Format
Add to basket Added to basket
History
Entry version 189 (07 Nov 2018)
Sequence version 3 (23 Jan 2007)
Previous versions | rss
Other tutorials and videos
Help video
Feedback

Protein

UDP-N-acetylmuramoylalanine--D-glutamate ligase

Gene

murD

Organism

Escherichia coli (strain K12)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).

Catalytic activityⁱ

ATP + UDP-N-acetyl-alpha-D-muramoyl-L-alanine + D-glutamate = ADP + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate.

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.

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Nucleotide bindingⁱ	112 – 118	ATPSequence analysis		7

GO - Molecular functionⁱ

ATP binding Source: UniProtKB-UniRule
identical protein binding
Source: IntAct
Inferred from physical interactionⁱ
- 24561554
UDP-N-acetylmuramoylalanine-D-glutamate ligase activity
Source: EcoCyc
Inferred from direct assayⁱ
- 1765076

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

cell cycle Source: UniProtKB-KW
cell division Source: UniProtKB-KW
cell wall organization Source: UniProtKB-KW
peptidoglycan biosynthetic process
Source: EcoCyc
Inferred from direct assayⁱ
- 24389752
regulation of cell shape Source: UniProtKB-KW

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Ligase
Biological process	Cell cycle, Cell division, Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis
Ligand	ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCycⁱ	EcoCyc:UDP-NACMURALA-GLU-LIG-MONOMER MetaCyc:UDP-NACMURALA-GLU-LIG-MONOMER
BRENDAⁱ	6.3.2.9 2026
SABIO-RKⁱ	P14900
UniPathwayⁱ	UPA00219

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: UDP-N-acetylmuramoylalanine--D-glutamate ligase (EC:6.3.2.9) Alternative name(s): D-glutamic acid-adding enzyme UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase
Gene namesⁱ	Name:murD Ordered Locus Names:b0088, JW0086
Organismⁱ	Escherichia coli (strain K12)
Taxonomic identifierⁱ	83333 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › Escherichia coli
Proteomesⁱ	UP000000318 Componentⁱ: Chromosome UP000000625 Componentⁱ: Chromosome

Organism-specific databases

EcoGeneⁱ	EG10620 murD

EcoGeneⁱ

EG10620 murD

Subcellular locationⁱ

Cytoplasm

GO - Cellular componentⁱ

cytoplasm
Source: EcoliWiki
Inferred from direct assayⁱ
- 1765076

View the complete GO annotation on QuickGO ...

Keywords - Cellular componentⁱ

Cytoplasm

Pathology & Biotechⁱ

Chemistry databases

ChEMBLⁱ	CHEMBL4732
Drug and drug target database More...DrugBankⁱ	DB03801 Lysine Nz-Carboxylic Acid DB08112 N-({6-[(4-CYANO-2-FLUOROBENZYL)OXY]NAPHTHALEN-2-YL}SULFONYL)-D-GLUTAMIC ACID DB08108 N-({6-[(4-CYANOBENZYL)OXY]NAPHTHALEN-2-YL}SULFONYL)-D-GLUTAMIC ACID DB08106 N-[(6-BUTOXYNAPHTHALEN-2-YL)SULFONYL]-D-GLUTAMIC ACID DB08105 N-[(6-BUTOXYNAPHTHALEN-2-YL)SULFONYL]-L-GLUTAMIC ACID DB08107 N-{[6-(PENTYLOXY)NAPHTHALEN-2-YL]SULFONYL}-D-GLUTAMIC ACID DB01673 Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine DB02314 Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine-D-Glutamate

ChEMBLⁱ

CHEMBL4732

DrugBankⁱ

DB03801 Lysine Nz-Carboxylic Acid
DB08112 N-({6-[(4-CYANO-2-FLUOROBENZYL)OXY]NAPHTHALEN-2-YL}SULFONYL)-D-GLUTAMIC ACID
DB08108 N-({6-[(4-CYANOBENZYL)OXY]NAPHTHALEN-2-YL}SULFONYL)-D-GLUTAMIC ACID
DB08106 N-[(6-BUTOXYNAPHTHALEN-2-YL)SULFONYL]-D-GLUTAMIC ACID
DB08105 N-[(6-BUTOXYNAPHTHALEN-2-YL)SULFONYL]-L-GLUTAMIC ACID
DB08107 N-{[6-(PENTYLOXY)NAPHTHALEN-2-YL]SULFONYL}-D-GLUTAMIC ACID
DB01673 Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine
DB02314 Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine-D-Glutamate

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Initiator methionineⁱ		Removed1 Publication
ChainⁱPRO_0000109013	2 – 438	UDP-N-acetylmuramoylalanine--D-glutamate ligaseAdd BLAST		437

Proteomic databases

EPDⁱ	P14900
PaxDbⁱ	P14900
PRIDEⁱ	P14900

Interactionⁱ

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
itself		3	EBI-554780,EBI-554780
trxC	P0AGG4	2	EBI-554780,EBI-549392

GO - Molecular functionⁱ

identical protein binding
Source: IntAct
Inferred from physical interactionⁱ
- 24561554

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	4261477, 566 interactors
Database of interacting proteins More...DIPⁱ	DIP-10279N
IntActⁱ	P14900, 8 interactors
STRINGⁱ	316385.ECDH10B_0070

Chemistry databases

BindingDBⁱ

P14900

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	9 – 12	Combined sources	4
Helixⁱ	15 – 26	Combined sources	12
Turnⁱ	27 – 29	Combined sources	3
Beta strandⁱ	33 – 40	Combined sources	8
Helixⁱ	44 – 46	Combined sources	3
Beta strandⁱ	53 – 57	Combined sources	5
Helixⁱ	60 – 64	Combined sources	5
Beta strandⁱ	67 – 71	Combined sources	5
Helixⁱ	75 – 78	Combined sources	4
Helixⁱ	80 – 87	Combined sources	8
Beta strandⁱ	91 – 93	Combined sources	3
Helixⁱ	95 – 102	Combined sources	8
Beta strandⁱ	107 – 111	Combined sources	5
Beta strandⁱ	113 – 115	Combined sources	3
Helixⁱ	116 – 129	Combined sources	14
Beta strandⁱ	134 – 142	Combined sources	9
Helixⁱ	144 – 147	Combined sources	4
Beta strandⁱ	154 – 158	Combined sources	5
Helixⁱ	161 – 165	Combined sources	5
Beta strandⁱ	173 – 177	Combined sources	5
Helixⁱ	185 – 187	Combined sources	3
Helixⁱ	191 – 200	Combined sources	10
Helixⁱ	201 – 203	Combined sources	3
Beta strandⁱ	207 – 212	Combined sources	6
Helixⁱ	216 – 218	Combined sources	3
Beta strandⁱ	221 – 223	Combined sources	3
Beta strandⁱ	229 – 231	Combined sources	3
Beta strandⁱ	233 – 243	Combined sources	11
Beta strandⁱ	246 – 251	Combined sources	6
Beta strandⁱ	254 – 258	Combined sources	5
Helixⁱ	259 – 261	Combined sources	3
Helixⁱ	267 – 282	Combined sources	16
Helixⁱ	287 – 296	Combined sources	10
Beta strandⁱ	303 – 310	Combined sources	8
Beta strandⁱ	313 – 317	Combined sources	5
Helixⁱ	324 – 331	Combined sources	8
Beta strandⁱ	340 – 347	Combined sources	8
Helixⁱ	350 – 352	Combined sources	3
Helixⁱ	354 – 359	Combined sources	6
Beta strandⁱ	362 – 371	Combined sources	10
Helixⁱ	374 – 378	Combined sources	5
Helixⁱ	382 – 384	Combined sources	3
Beta strandⁱ	385 – 387	Combined sources	3
Helixⁱ	391 – 398	Combined sources	8
Helixⁱ	399 – 401	Combined sources	3
Beta strandⁱ	407 – 410	Combined sources	4
Beta strandⁱ	413 – 416	Combined sources	4
Turnⁱ	417 – 419	Combined sources	3
Beta strandⁱ	420 – 422	Combined sources	3
Helixⁱ	423 – 437	Combined sources	15

Show more details

3D structure databases

ProteinModelPortalⁱ	P14900
SMRⁱ	P14900
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P14900

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the MurCDEF family.Curated

Phylogenomic databases

eggNOGⁱ	ENOG4105DMZ Bacteria COG0771 LUCA
HOGENOMⁱ	HOG000049427
InParanoidⁱ	P14900
KEGG Orthology (KO) More...KOⁱ	K01925
PhylomeDBⁱ	P14900

Family and domain databases

Gene3Dⁱ	3.40.1190.10, 1 hit 3.90.190.20, 1 hit
HAMAPⁱ	MF_00639 MurD, 1 hit
InterProⁱ	View protein in InterPro IPR036565 Mur-like_cat_sf IPR004101 Mur_ligase_C IPR036615 Mur_ligase_C_dom_sf IPR013221 Mur_ligase_cen IPR005762 UDP-N-AcMur-Glu_ligase
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF02875 Mur_ligase_C, 1 hit PF08245 Mur_ligase_M, 1 hit
SUPFAMⁱ	SSF53244 SSF53244, 1 hit SSF53623 SSF53623, 1 hit
TIGRFAMsⁱ	TIGR01087 murD, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

P14900-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MADYQGKNVV IIGLGLTGLS CVDFFLARGV TPRVMDTRMT PPGLDKLPEA 
        60         70         80         90        100
VERHTGSLND EWLMAADLIV ASPGIALAHP SLSAAADAGI EIVGDIELFC 
       110        120        130        140        150
REAQAPIVAI TGSNGKSTVT TLVGEMAKAA GVNVGVGGNI GLPALMLLDD 
       160        170        180        190        200
ECELYVLELS SFQLETTSSL QAVAATILNV TEDHMDRYPF GLQQYRAAKL 
       210        220        230        240        250
RIYENAKVCV VNADDALTMP IRGADERCVS FGVNMGDYHL NHQQGETWLR 
       260        270        280        290        300
VKGEKVLNVK EMKLSGQHNY TNALAALALA DAAGLPRASS LKALTTFTGL 
       310        320        330        340        350
PHRFEVVLEH NGVRWINDSK ATNVGSTEAA LNGLHVDGTL HLLLGGDGKS 
       360        370        380        390        400
ADFSPLARYL NGDNVRLYCF GRDGAQLAAL RPEVAEQTET MEQAMRLLAP 
       410        420        430 
RVQPGDMVLL SPACASLDQF KNFEQRGNEF ARLAKELG

Length:438

Mass (Da):46,974

Last modified:January 23, 2007 - v3

Checksum:ⁱ11C64782C098F761

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	28	R → A in CAA35611 (PubMed:2129548).Curated	1
Sequence conflictⁱ	174	A → T in CAA35611 (PubMed:2129548).Curated	1
Sequence conflictⁱ	276 – 277	AL → RV in CAA35611 (PubMed:2129548).Curated	2

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X51584 Genomic DNA Translation: CAA35933.1 X17609 Genomic DNA Translation: CAA35611.1 X55034 Genomic DNA Translation: CAA38865.1 M30807 Genomic DNA Translation: AAA83858.1 U00096 Genomic DNA Translation: AAC73199.1 AP009048 Genomic DNA Translation: BAB96656.1
PIRⁱ	S08396 CEECME
NCBI Reference Sequences More...RefSeqⁱ	NP_414630.1, NC_000913.3 WP_000796481.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaⁱ	AAC73199; AAC73199; b0088 BAB96656; BAB96656; BAB96656
GeneIDⁱ	944818
KEGGⁱ	ecj:JW0086 eco:b0088
PATRICⁱ	fig\|1411691.4.peg.2192

Protein	Similar proteins		Species	Score	Length	Source
P14900	Multifunctional fusion protein		ECOLX		800	UniRef100_P14900
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase		SHIFL		177
UDP-N-acetylmuramoyl-L-alanine--D-glutamate ligase		Shigella sp.		438
UDP-N-acetylmuramoylalanine--D-glutamate ligase		Klebsiella pneumoniae IS22		438
UDP-N-acetylmuramoylalanine--D-glutamate ligase		Escherichia coli D6-113.11		438
+54

Protein	Similar proteins		Species	Score	Length	Source
P14900	Multifunctional fusion protein		ECOLX		800	UniRef90_P14900
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase		SHIFL		177
UDP-N-acetylmuramoyl-L-alanine--D-glutamate ligase		Shigella sp.		438
UDP-N-acetylmuramoylalanine--D-glutamate ligase		Klebsiella pneumoniae IS22		438
UDP-N-acetylmuramoylalanine--D-glutamate ligase		Escherichia coli D6-113.11		438
+67

Protein	Similar proteins		Species	Score	Length	Source
P14900	Multifunctional fusion protein		ECOLX		800	UniRef50_P14900
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase		SHIFL		177
UDP-N-acetylmuramoyl-L-alanine--D-glutamate ligase		Shigella sp.		438
UDP-N-acetylmuramoylalanine--D-glutamate ligase		Klebsiella pneumoniae IS22		438
UDP-N-acetylmuramoylalanine--D-glutamate ligase		Escherichia coli D6-113.11		438
+67

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X51584 Genomic DNA Translation: CAA35933.1 X17609 Genomic DNA Translation: CAA35611.1 X55034 Genomic DNA Translation: CAA38865.1 M30807 Genomic DNA Translation: AAA83858.1 U00096 Genomic DNA Translation: AAC73199.1 AP009048 Genomic DNA Translation: BAB96656.1
PIRⁱ	S08396 CEECME
RefSeqⁱ	NP_414630.1, NC_000913.3 WP_000796481.1, 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 entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1E0D	X-ray	2.40	A	2-438	[»]
	1EEH	X-ray	1.90	A	2-438	[»]
	1UAG	X-ray	1.95	A	2-438	[»]
	2JFF	X-ray	1.89	A	2-438	[»]
	2JFG	X-ray	1.52	A	2-438	[»]
	2JFH	X-ray	1.97	A	2-438	[»]
	2UAG	X-ray	1.70	A	2-438	[»]
	2UUO	X-ray	2.50	A	2-438	[»]
	2UUP	X-ray	1.88	A	2-438	[»]
	2VTD	X-ray	1.94	A	1-438	[»]
	2VTE	X-ray	2.20	A	1-438	[»]
	2WJP	X-ray	1.60	A	2-438	[»]
	2X5O	X-ray	1.46	A	2-438	[»]
	2XPC	X-ray	1.49	A	2-438	[»]
	2Y1O	X-ray	1.49	A	1-438	[»]
	2Y66	X-ray	1.49	A	1-438	[»]
	2Y67	X-ray	1.85	A	1-438	[»]
	2Y68	X-ray	1.49	A	1-438	[»]
	3UAG	X-ray	1.77	A	2-438	[»]
	4UAG	X-ray	1.66	A	2-438	[»]
	5A5E	X-ray	1.84	A	2-438	[»]
	5A5F	X-ray	1.90	A	2-438	[»]
ProteinModelPortalⁱ	P14900
SMRⁱ	P14900
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	4261477, 566 interactors
DIPⁱ	DIP-10279N
IntActⁱ	P14900, 8 interactors
STRINGⁱ	316385.ECDH10B_0070

Chemistry databases

BindingDBⁱ	P14900
ChEMBLⁱ	CHEMBL4732
DrugBankⁱ	DB03801 Lysine Nz-Carboxylic Acid DB08112 N-({6-[(4-CYANO-2-FLUOROBENZYL)OXY]NAPHTHALEN-2-YL}SULFONYL)-D-GLUTAMIC ACID DB08108 N-({6-[(4-CYANOBENZYL)OXY]NAPHTHALEN-2-YL}SULFONYL)-D-GLUTAMIC ACID DB08106 N-[(6-BUTOXYNAPHTHALEN-2-YL)SULFONYL]-D-GLUTAMIC ACID DB08105 N-[(6-BUTOXYNAPHTHALEN-2-YL)SULFONYL]-L-GLUTAMIC ACID DB08107 N-{[6-(PENTYLOXY)NAPHTHALEN-2-YL]SULFONYL}-D-GLUTAMIC ACID DB01673 Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine DB02314 Uridine-5'-Diphosphate-N-Acetylmuramoyl-L-Alanine-D-Glutamate

Proteomic databases

EPDⁱ	P14900
PaxDbⁱ	P14900
PRIDEⁱ	P14900

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	AAC73199; AAC73199; b0088 BAB96656; BAB96656; BAB96656
GeneIDⁱ	944818
KEGGⁱ	ecj:JW0086 eco:b0088
PATRICⁱ	fig\|1411691.4.peg.2192

Organism-specific databases

EchoBASEⁱ	EB0615
EcoGeneⁱ	EG10620 murD

Phylogenomic databases

eggNOGⁱ	ENOG4105DMZ Bacteria COG0771 LUCA
HOGENOMⁱ	HOG000049427
InParanoidⁱ	P14900
KOⁱ	K01925
PhylomeDBⁱ	P14900

Enzyme and pathway databases

UniPathwayⁱ	UPA00219
BioCycⁱ	EcoCyc:UDP-NACMURALA-GLU-LIG-MONOMER MetaCyc:UDP-NACMURALA-GLU-LIG-MONOMER
BRENDAⁱ	6.3.2.9 2026
SABIO-RKⁱ	P14900

Miscellaneous databases

EvolutionaryTraceⁱ	P14900
Protein Ontology More...PROⁱ	PR:P14900

Family and domain databases

Gene3Dⁱ	3.40.1190.10, 1 hit 3.90.190.20, 1 hit
HAMAPⁱ	MF_00639 MurD, 1 hit
InterProⁱ	View protein in InterPro IPR036565 Mur-like_cat_sf IPR004101 Mur_ligase_C IPR036615 Mur_ligase_C_dom_sf IPR013221 Mur_ligase_cen IPR005762 UDP-N-AcMur-Glu_ligase
Pfamⁱ	View protein in Pfam PF02875 Mur_ligase_C, 1 hit PF08245 Mur_ligase_M, 1 hit
SUPFAMⁱ	SSF53244 SSF53244, 1 hit SSF53623 SSF53623, 1 hit
TIGRFAMsⁱ	TIGR01087 murD, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	MURD_ECOLI
Accessionⁱ	P14900Primary (citable) accession number: P14900
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
	Last sequence update:	January 23, 2007
	Last modified:	November 7, 2018
	This is version 189 of the entry and version 3 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
PATHWAY comments
Index of metabolic and biosynthesis pathways
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
Escherichia coli
Escherichia coli (strain K12): entries and cross-references to EcoGene

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P14900 (MURD_ECOLI)

Your basket is currently empty. i <p>When browsing through different UniProt proteins, you can use the ‘basket’ to save them, so that you can back to find or analyse them later.<p><a href='/help/basket' target='_top'>More...</a></p>

UDP-N-acetylmuramoylalanine--D-glutamate ligase

murD

Select a section on the left to see content.

<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

<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

Regions

<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

Enzyme and pathway databases

<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

Organism-specific databases

<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

<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

<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

Proteomic databases

<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

GO - Molecular functioni

Protein-protein interaction databases

Chemistry databases

<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

3D structure databases

Miscellaneous databases

<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

<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

Phylogenomic databases

Family and domain databases

Experimental Info

Sequence databases

Genome annotation databases

<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

3D structure databases

Protein-protein interaction databases

Chemistry databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<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 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

Documents

UniProt is an ELIXIR core data resource

Your basket is currently empty. ⁱ

Functionⁱ

Pathwayⁱ: peptidoglycan biosynthesis

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ