UniProtKB - P0AF16 (MURJ_ECOLI)

BLAST

>sp|P0AF16|MURJ_ECOLI Lipid II flippase MurJ OS=Escherichia coli (strain K12) OX=83333 GN=murJ PE=1 SV=1
MNLLKSLAAVSSMTMFSRVLGFARDAIVARIFGAGMATDAFFVAFKLPNLLRRIFAEGAF
SQAFVPILAEYKSKQGEDATRVFVSYVSGLLTLALAVVTVAGMLAAPWVIMVTAPGFADT
ADKFALTSQLLKITFPYILLISLASLVGAILNTWNRFSIPAFAPTLLNISMIGFALFAAP
YFNPPVLALAWAVTVGGVLQLVYQLPHLKKIGMLVLPRINFHDAGAMRVVKQMGPAILGV
SVSQISLIINTIFASFLASGSVSWMYYADRLMEFPSGVLGVALGTILLPSLSKSFASGNH
DEYNRLMDWGLRLCFLLALPSAVALGILSGPLTVSLFQYGKFTAFDALMTQRALIAYSVG
LIGLIVVKVLAPGFYSRQDIKTPVKIAIVTLILTQLMNLAFIGPLKHAGLSLSIGLAACL
NASLLYWQLRKQKIFTPQPGWMAFLLRLVVAVLVMSGVLLGMLHIMPEWSLGTMPWRLLR
LMAVVLAGIAAYFAALAVLGFKVKEFARRTV

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History
Entry version 95 (07 Nov 2018)
Sequence version 1 (20 Dec 2005)
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Protein

Lipid II flippase MurJ

Gene

murJ

Organism

Escherichia coli (strain K12)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

Involved in peptidoglycan biosynthesis. Transports lipid-linked peptidoglycan precursors from the inner to the outer leaflet of the cytoplasmic membrane.UniRule annotation3 Publications

Miscellaneous

FtsW (AC P0ABG4) is also proposed to act as a lipid II flippase. The identity of the lipid II flippase is controversial with conflicting in vivo and in vitro results.

Pathwayⁱ: peptidoglycan biosynthesis

This protein is involved in the pathway peptidoglycan biosynthesis, which is part of Cell wall biogenesis.UniRule annotation1 Publication
View all proteins of this organism that are known to be involved in the pathway peptidoglycan biosynthesis and in Cell wall biogenesis.

GO - Molecular functionⁱ

lipid-linked peptidoglycan transporter activity
Source: EcoCyc
Inferred from direct assayⁱ
- 25013077

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

cell wall organization Source: UniProtKB-KW
glycolipid translocation
Source: CACAO
Inferred from mutant phenotypeⁱ
- 25013077
lipid-linked peptidoglycan transport
Source: EcoCyc
Inferred from direct assayⁱ
- 25013077
lipid translocation
Source: EcoCyc
Inferred from direct assayⁱ
- 25013077
peptidoglycan biosynthetic process
Source: EcoCyc
Inferred from mutant phenotypeⁱ
- 18708495
regulation of cell shape Source: UniProtKB-KW

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Biological process	Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis, Transport

Biological process

Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis, Transport

Enzyme and pathway databases

BioCycⁱ	EcoCyc:G6561-MONOMER MetaCyc:G6561-MONOMER
UniPathwayⁱ	UPA00219

Protein family/group databases

TCDBⁱ	2.A.66.4.3 the multidrug/oligosaccharidyl-lipid/polysaccharide (mop) flippase superfamily

TCDBⁱ

2.A.66.4.3 the multidrug/oligosaccharidyl-lipid/polysaccharide (mop) flippase superfamily

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Lipid II flippase MurJCurated Alternative name(s): Peptidoglycan biosynthesis protein MurJCurated
Gene namesⁱ	Name:murJ1 PublicationUniRule annotation Synonyms:mviN, yceN Ordered Locus Names:b1069, JW1056
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	EG13880 murJ

EcoGeneⁱ

EG13880 murJ

Subcellular locationⁱ

Cell inner membrane
UniRule annotation
Manual assertion according to rulesⁱ
- HAMAP-Rule:MF_02078
2 Publications
Manual assertion based on experiment inⁱ
- Ref.4
  "Global topology analysis of the Escherichia coli inner membrane proteome."
  Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
  Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract]
  Cited for: SUBCELLULAR LOCATION.
- Ref.7
  "Structure-function analysis of MurJ reveals a solvent-exposed cavity containing residues essential for peptidoglycan biogenesis in Escherichia coli."
  Butler E.K., Davis R.M., Bari V., Nicholson P.A., Ruiz N.
  J. Bacteriol. 195:4639-4649(2013) [PubMed] [Europe PMC] [Abstract]
  Cited for: PROBABLE FUNCTION AS A TRANSPORTER, SUBCELLULAR LOCATION, TOPOLOGY, MUTAGENESIS OF ARG-18; ARG-24; ASP-39; ARG-52 AND ARG-270.
; Multi-pass membrane protein
UniRule annotation
Manual assertion according to rulesⁱ
- HAMAP-Rule:MF_02078
2 Publications
Manual assertion based on experiment inⁱ
- Ref.4
  "Global topology analysis of the Escherichia coli inner membrane proteome."
  Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
  Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract]
  Cited for: SUBCELLULAR LOCATION.
- Ref.7
  "Structure-function analysis of MurJ reveals a solvent-exposed cavity containing residues essential for peptidoglycan biogenesis in Escherichia coli."
  Butler E.K., Davis R.M., Bari V., Nicholson P.A., Ruiz N.
  J. Bacteriol. 195:4639-4649(2013) [PubMed] [Europe PMC] [Abstract]
  Cited for: PROBABLE FUNCTION AS A TRANSPORTER, SUBCELLULAR LOCATION, TOPOLOGY, MUTAGENESIS OF ARG-18; ARG-24; ASP-39; ARG-52 AND ARG-270.

Topology

Feature key	Position(s)	DescriptionActions	Length
Topological domainⁱ	1 – 5	CytoplasmicSequence analysis	5
Transmembraneⁱ	6 – 32	HelicalSequence analysisAdd BLAST	27
Topological domainⁱ	33 – 40	PeriplasmicSequence analysis	8
Transmembraneⁱ	41 – 69	HelicalSequence analysisAdd BLAST	29
Topological domainⁱ	70 – 82	CytoplasmicSequence analysisAdd BLAST	13
Transmembraneⁱ	83 – 109	HelicalSequence analysisAdd BLAST	27
Topological domainⁱ	110 – 123	PeriplasmicSequence analysisAdd BLAST	14
Transmembraneⁱ	124 – 154	HelicalSequence analysisAdd BLAST	31
Topological domainⁱ	155 – 156	CytoplasmicSequence analysis	2
Transmembraneⁱ	157 – 178	HelicalSequence analysisAdd BLAST	22
Topological domainⁱ	179 – 185	PeriplasmicSequence analysis	7
Transmembraneⁱ	186 – 207	HelicalSequence analysisAdd BLAST	22
Topological domainⁱ	208 – 223	CytoplasmicSequence analysisAdd BLAST	16
Transmembraneⁱ	224 – 253	HelicalSequence analysisAdd BLAST	30
Topological domainⁱ	254 – 263	PeriplasmicSequence analysis	10
Transmembraneⁱ	264 – 292	HelicalSequence analysisAdd BLAST	29
Topological domainⁱ	293 – 302	CytoplasmicSequence analysis	10
Transmembraneⁱ	303 – 337	HelicalSequence analysisAdd BLAST	35
Topological domainⁱ	338 – 346	PeriplasmicSequence analysis	9
Transmembraneⁱ	347 – 374	HelicalSequence analysisAdd BLAST	28
Topological domainⁱ	375 – 379	CytoplasmicSequence analysis	5
Transmembraneⁱ	380 – 402	HelicalSequence analysisAdd BLAST	23
Topological domainⁱ	403 – 409	PeriplasmicSequence analysis	7
Transmembraneⁱ	410 – 429	HelicalSequence analysisAdd BLAST	20
Topological domainⁱ	430 – 443	CytoplasmicSequence analysisAdd BLAST	14
Transmembraneⁱ	444 – 463	HelicalSequence analysisAdd BLAST	20
Topological domainⁱ	464 – 477	PeriplasmicSequence analysisAdd BLAST	14
Transmembraneⁱ	478 – 499	HelicalSequence analysisAdd BLAST	22
Topological domainⁱ	500 – 511	CytoplasmicSequence analysisAdd BLAST	12

GO - Cellular componentⁱ

integral component of plasma membrane
Source: EcoCyc
Inferred from direct assayⁱ
- 23935042
plasma membrane
Source: EcoCyc
Inferred from direct assayⁱ
- 15919996

View the complete GO annotation on QuickGO ...

Keywords - Cellular componentⁱ

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	18	R → A or C: Lack of activity. 1 Publication	1
Mutagenesisⁱ	24	R → A or C: Lack of activity. 1 Publication	1
Mutagenesisⁱ	39	D → A or C: Lack of activity. 1 Publication	1
Mutagenesisⁱ	52	R → A: Decrease in activity. 1 Publication	1
Mutagenesisⁱ	52	R → C: Lack of activity. 1 Publication	1
Mutagenesisⁱ	270	R → A or C: Lack of activity. 1 Publication	1

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000182006	1 – 511	Lipid II flippase MurJAdd BLAST		511

Proteomic databases

PaxDbⁱ	P0AF16
PRIDEⁱ	P0AF16

Interactionⁱ

Protein-protein interaction databases

BioGridⁱ	4260079, 316 interactors
IntActⁱ	P0AF16, 1 interactor
STRINGⁱ	316385.ECDH10B_1140

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	7 – 11	Combined sources	5
Helixⁱ	15 – 32	Combined sources	18
Helixⁱ	36 – 55	Combined sources	20
Helixⁱ	58 – 73	Combined sources	16
Helixⁱ	77 – 104	Combined sources	28
Helixⁱ	106 – 113	Combined sources	8
Helixⁱ	115 – 119	Combined sources	5
Beta strandⁱ	120 – 122	Combined sources	3
Helixⁱ	123 – 134	Combined sources	12
Helixⁱ	137 – 154	Combined sources	18
Helixⁱ	158 – 178	Combined sources	21
Turnⁱ	179 – 181	Combined sources	3
Beta strandⁱ	182 – 184	Combined sources	3
Helixⁱ	186 – 210	Combined sources	25
Helixⁱ	224 – 255	Combined sources	32
Helixⁱ	261 – 286	Combined sources	26
Helixⁱ	288 – 296	Combined sources	9
Helixⁱ	300 – 327	Combined sources	28
Helixⁱ	329 – 337	Combined sources	9
Helixⁱ	344 – 358	Combined sources	15
Helixⁱ	360 – 376	Combined sources	17
Helixⁱ	383 – 405	Combined sources	23
Helixⁱ	407 – 431	Combined sources	25
Helixⁱ	441 – 465	Combined sources	25
Helixⁱ	474 – 498	Combined sources	25

Show more details

3D structure databases

ProteinModelPortalⁱ	P0AF16
SMRⁱ	P0AF16
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the MurJ/MviN family.UniRule annotationCurated

Keywords - Domainⁱ

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGⁱ	ENOG4105CJR Bacteria COG0728 LUCA
HOGENOMⁱ	HOG000263812
InParanoidⁱ	P0AF16
KEGG Orthology (KO) More...KOⁱ	K03980
PhylomeDBⁱ	P0AF16

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd13123 MATE_MurJ_like, 1 hit
HAMAPⁱ	MF_02078 MurJ_MviN, 1 hit
InterProⁱ	View protein in InterPro IPR004268 MurJ
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF03023 MVIN, 1 hit
PIRSFⁱ	PIRSF002869 MviN, 1 hit
PRINTSⁱ	PR01806 VIRFACTRMVIN
TIGRFAMsⁱ	TIGR01695 murJ_mviN, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

P0AF16-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MNLLKSLAAV SSMTMFSRVL GFARDAIVAR IFGAGMATDA FFVAFKLPNL 
        60         70         80         90        100
LRRIFAEGAF SQAFVPILAE YKSKQGEDAT RVFVSYVSGL LTLALAVVTV 
       110        120        130        140        150
AGMLAAPWVI MVTAPGFADT ADKFALTSQL LKITFPYILL ISLASLVGAI 
       160        170        180        190        200
LNTWNRFSIP AFAPTLLNIS MIGFALFAAP YFNPPVLALA WAVTVGGVLQ 
       210        220        230        240        250
LVYQLPHLKK IGMLVLPRIN FHDAGAMRVV KQMGPAILGV SVSQISLIIN 
       260        270        280        290        300
TIFASFLASG SVSWMYYADR LMEFPSGVLG VALGTILLPS LSKSFASGNH 
       310        320        330        340        350
DEYNRLMDWG LRLCFLLALP SAVALGILSG PLTVSLFQYG KFTAFDALMT 
       360        370        380        390        400
QRALIAYSVG LIGLIVVKVL APGFYSRQDI KTPVKIAIVT LILTQLMNLA 
       410        420        430        440        450
FIGPLKHAGL SLSIGLAACL NASLLYWQLR KQKIFTPQPG WMAFLLRLVV 
       460        470        480        490        500
AVLVMSGVLL GMLHIMPEWS LGTMPWRLLR LMAVVLAGIA AYFAALAVLG 
       510 
FKVKEFARRT V

Length:511

Mass (Da):55,267

Last modified:December 20, 2005 - v1

Checksum:ⁱCB20FE3CFC9419C2

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U00096 Genomic DNA Translation: AAC74153.1 AP009048 Genomic DNA Translation: BAA35877.1
PIRⁱ	B64850
NCBI Reference Sequences More...RefSeqⁱ	NP_415587.1, NC_000913.3 WP_001050683.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaⁱ	AAC74153; AAC74153; b1069 BAA35877; BAA35877; BAA35877
GeneIDⁱ	945487
KEGGⁱ	ecj:JW1056 eco:b1069
PATRICⁱ	fig\|1411691.4.peg.1199

Protein	Similar proteins		Species	Score	Length	Source
P0AF16	Probable lipid II flippase MurJ		ECO57		511	UniRef100_P0AF16
Lipid II flippase MurJ		Shigella sp.		511
Probable lipid II flippase MurJ		Escherichia coli O145 str. RM9872		511
Probable lipid II flippase MurJ		Klebsiella pneumoniae IS22		511
Probable lipid II flippase MurJ		KLEPN		511
+52

Protein	Similar proteins		Species	Score	Length	Source
P0AF16	Probable lipid II flippase MurJ		ECO57		511	UniRef90_P0AF16
Probable lipid II flippase MurJ		SALTY		524
Lipid II flippase MurJ		Shigella sp.		511
Probable lipid II flippase MurJ		Escherichia coli O145 str. RM9872		511
Probable lipid II flippase MurJ		Klebsiella pneumoniae IS22		511
+1173

Protein	Similar proteins		Species	Score	Length	Source
P0AF16	Probable lipid II flippase MurJ		ECO57		511	UniRef50_P0AF16
Probable lipid II flippase MurJ		SALTY		524
Lipid II flippase MurJ		Shigella sp.		511
Probable lipid II flippase MurJ		Escherichia coli O145 str. RM9872		511
Probable lipid II flippase MurJ		Klebsiella pneumoniae IS22		511
+2436

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U00096 Genomic DNA Translation: AAC74153.1 AP009048 Genomic DNA Translation: BAA35877.1
PIRⁱ	B64850
RefSeqⁱ	NP_415587.1, NC_000913.3 WP_001050683.1, 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
	6CC4	X-ray	3.50	A	4-511	[»]
ProteinModelPortalⁱ	P0AF16
SMRⁱ	P0AF16
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	4260079, 316 interactors
IntActⁱ	P0AF16, 1 interactor
STRINGⁱ	316385.ECDH10B_1140

Protein family/group databases

TCDBⁱ	2.A.66.4.3 the multidrug/oligosaccharidyl-lipid/polysaccharide (mop) flippase superfamily

TCDBⁱ

2.A.66.4.3 the multidrug/oligosaccharidyl-lipid/polysaccharide (mop) flippase superfamily

Proteomic databases

PaxDbⁱ	P0AF16
PRIDEⁱ	P0AF16

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	AAC74153; AAC74153; b1069 BAA35877; BAA35877; BAA35877
GeneIDⁱ	945487
KEGGⁱ	ecj:JW1056 eco:b1069
PATRICⁱ	fig\|1411691.4.peg.1199

Organism-specific databases

EchoBASEⁱ	EB3639
EcoGeneⁱ	EG13880 murJ

Phylogenomic databases

eggNOGⁱ	ENOG4105CJR Bacteria COG0728 LUCA
HOGENOMⁱ	HOG000263812
InParanoidⁱ	P0AF16
KOⁱ	K03980
PhylomeDBⁱ	P0AF16

Enzyme and pathway databases

UniPathwayⁱ	UPA00219
BioCycⁱ	EcoCyc:G6561-MONOMER MetaCyc:G6561-MONOMER

Miscellaneous databases

Protein Ontology More...PROⁱ	PR:P0AF16

PROⁱ

PR:P0AF16

Family and domain databases

CDDⁱ	cd13123 MATE_MurJ_like, 1 hit
HAMAPⁱ	MF_02078 MurJ_MviN, 1 hit
InterProⁱ	View protein in InterPro IPR004268 MurJ
Pfamⁱ	View protein in Pfam PF03023 MVIN, 1 hit
PIRSFⁱ	PIRSF002869 MviN, 1 hit
PRINTSⁱ	PR01806 VIRFACTRMVIN
TIGRFAMsⁱ	TIGR01695 murJ_mviN, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	MURJ_ECOLI
Accessionⁱ	P0AF16Primary (citable) accession number: P0AF16 Secondary accession number(s): P75932
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
	Last sequence update:	December 20, 2005
	Last modified:	November 7, 2018
	This is version 95 of the entry and version 1 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, 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 - P0AF16 (MURJ_ECOLI)

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Lipid II flippase MurJ

murJ

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

Miscellaneous

<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

<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

Protein family/group 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

Topology

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

Mutagenesis

<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

Protein-protein interaction 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

<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

Keywords - Domaini

Phylogenomic databases

Family and domain databases

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

Protein family/group 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

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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

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ