rplL

Functionⁱ

The binding site for several of the GTPase factors involved in protein synthesis (IF-2, EF-Tu, EF-G and RF3). Is thus essential for accurate translation. Deletion of 1 of the L12 dimers from the ribosome (by deleting the binding site on L10) leads to decreased IF-2 association with the 70S ribosome and decreased stimulation of the GTPase activity of EF-G.2 Publications

Miscellaneous

Ribosomal protein L8 appears to be an aggregate of ribosomal proteins L7/L12 and L10.1 Publication

GO - Molecular functionⁱ

protein homodimerization activity
Source: CAFA
Inferred from direct assayⁱ
- 10747797
ribosome binding
Source: CAFA
Inferred from direct assayⁱ
- 10747797
structural constituent of ribosome Source: InterPro

Complete GO annotation...

GO - Biological processⁱ

translation
Source: CAFA
Inferred from mutant phenotypeⁱ
- 10747797

Complete GO annotation...

Keywordsⁱ

Molecular function	Ribonucleoprotein, Ribosomal protein

Molecular function

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCycⁱ	EcoCyc:EG10873-MONOMER. MetaCyc:EG10873-MONOMER.

BioCycⁱ

EcoCyc:EG10873-MONOMER.
MetaCyc:EG10873-MONOMER.

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: 50S ribosomal protein L7/L12UniRule annotation Alternative name(s): L8 Large ribosomal subunit protein bL121 Publication
Gene namesⁱ	Name:rplLUniRule annotation Ordered Locus Names:b3986, JW3949
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	EG10873. rplL.

EcoGeneⁱ

EG10873. rplL.

Subcellular locationⁱ

GO - Cellular componentⁱ

cytosol
Source: EcoCyc
Inferred from direct assayⁱ
- 15911532
- 18304323
cytosolic large ribosomal subunit
Source: EcoliWiki
Inferred from direct assayⁱ
- 4587209
large ribosomal subunit
Source: CAFA
Inferred from direct assayⁱ
- 10747797

Complete GO annotation...

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	66	K → A: EF-Tu-binding and EF-Tu-promoted GTP hydrolysis reduced. 1 Publication	1
Mutagenesisⁱ	67	V → D: EF-Tu-binding and EF-Tu-promoted GTP hydrolysis reduced. 1 Publication	1
Mutagenesisⁱ	70	I → A: EF-Tu-binding and EF-Tu-promoted GTP hydrolysis reduced. 1 Publication	1
Mutagenesisⁱ	71	K → A: EF-Tu-binding and EF-Tu-promoted GTP hydrolysis reduced. 1 Publication	1
Mutagenesisⁱ	74	R → M: EF-Tu-binding and EF-Tu-promoted GTP hydrolysis reduced. 1 Publication	1
Mutagenesisⁱ	85	K → A: EF-Tu-binding and EF-Tu-promoted GTP hydrolysis reduced. 1 Publication	1

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Initiator methionineⁱ		Removed5 Publications
ChainⁱPRO_0000157528	2 – 121	50S ribosomal protein L7/L12Add BLAST		120

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Modified residueⁱ	2	N-acetylserine; in L71 Publication		1
Modified residueⁱ	82	N6-methyllysine; partial1 Publication		1

Post-translational modificationⁱ

Acetylation of Ser-2 converts L12 to L7.

Lys-82 was found to be 50% monomethylated.1 Publication

Keywords - PTMⁱ

Acetylation, Methylation

Proteomic databases

EPDⁱ	P0A7K2.
PaxDbⁱ	P0A7K2.
PRIDEⁱ	P0A7K2.

2D gel databases

SWISS-2DPAGEⁱ	P0A7K2.

SWISS-2DPAGEⁱ

P0A7K2.

Interactionⁱ

Subunit structureⁱ

Homodimer. Part of the 50S ribosomal subunit; present in 4 copies per ribosome. L7/L12 forms dimers with an elongated shape. Two dimers associate with a copy of L10 to form part of the ribosomal stalk (called L8). The ribosomal stalk helps the ribosome interact with GTP-bound translation factors. Forms a pentameric L10(L12)2(L12)2 complex, where L10 forms an elongated spine to which 2 L12 dimers bind in a sequential fashion.2 Publications

GO - Molecular functionⁱ

protein homodimerization activity
Source: CAFA
Inferred from direct assayⁱ
- 10747797

Complete GO annotation...

Protein-protein interaction databases

BioGridⁱ	852783. 1 interactor.
Database of interacting proteins More...DIPⁱ	DIP-36009N.
IntActⁱ	P0A7K2. 127 interactors.
Molecular INTeraction database More...MINTⁱ	MINT-1277405.
STRINGⁱ	511145.b3986.

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Show more details

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	5 – 12	Combined sources	8
Helixⁱ	17 – 30	Combined sources	14
Helixⁱ	33 – 50	Combined sources	18
Beta strandⁱ	55 – 61	Combined sources	7
Helixⁱ	63 – 65	Combined sources	3
Helixⁱ	66 – 77	Combined sources	12
Helixⁱ	81 – 89	Combined sources	9
Beta strandⁱ	92 – 99	Combined sources	8
Helixⁱ	101 – 114	Combined sources	14
Beta strandⁱ	117 – 121	Combined sources	5

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
	1CTF	X-ray	1.70	A	48-121	[»]
	1RQS	NMR	-	A	48-121	[»]
	1RQT	NMR	-	A/B	2-38	[»]
	1RQU	NMR	-	A/B	2-121	[»]
	1RQV	NMR	-	A/B	2-121	[»]
	2BCW	electron microscopy	11.20	B	54-121	[»]
	3J7Z	electron microscopy	3.90	6	1-121	[»]
	4UY8	electron microscopy	3.80	6	2-31	[»]
	4V4V	electron microscopy	15.00	B3/B5	3-121	[»]
	4V4W	electron microscopy	15.00	B3/B5	3-121	[»]
	4V5M	electron microscopy	7.80	BL	1-121	[»]
	4V5N	electron microscopy	7.60	BL	1-121	[»]
	4V7B	electron microscopy	6.80	B6	1-121	[»]
	4V7D	electron microscopy	7.60	AL	2-121	[»]
	4V85	X-ray	3.20	J/K/L/M	1-121	[»]
	4V89	X-ray	3.70	BJ/BK/BL/BM	1-121	[»]
	4V9O	X-ray	2.90	A6	1-121	[»]
	5KCS	electron microscopy	3.90	1L	1-121	[»]
ProteinModelPortalⁱ	P0A7K2.
SMRⁱ	P0A7K2.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P0A7K2.

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	54 – 121	Required for recruitment of EF-Tu and EF-G, and for EF-Tu and EF-G-promoted GTP hydrolysisAdd BLAST		68

Sequence similaritiesⁱ

Belongs to the bacterial ribosomal protein bL12 family.UniRule annotation

Phylogenomic databases

eggNOGⁱ	ENOG4105KBC. Bacteria. COG0222. LUCA.
HOGENOMⁱ	HOG000248813.
InParanoidⁱ	P0A7K2.
KEGG Orthology (KO) More...KOⁱ	K02935.
PhylomeDBⁱ	P0A7K2.

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd00387. Ribosomal_L7_L12. 1 hit.
Gene3Dⁱ	3.30.1390.10. 1 hit.
HAMAPⁱ	MF_00368. Ribosomal_L7_L12. 1 hit.
InterProⁱ	View protein in InterPro IPR000206. Ribosomal_L7/12. IPR014719. Ribosomal_L7/12_C/ClpS-like. IPR013823. Ribosomal_L7/L12_C. IPR008932. Ribosomal_L7/L12_oligo.
PANTHERⁱ	PTHR24089:SF404. PTHR24089:SF404. 1 hit.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00542. Ribosomal_L12. 1 hit. PF16320. Ribosomal_L12_N. 1 hit.
ProDomⁱ	View protein in ProDom or Entries sharing at least one domain PD001326. Ribosomal_L7/L12_C. 1 hit.
SUPFAMⁱ	SSF48300. SSF48300. 1 hit. SSF54736. SSF54736. 1 hit.
TIGRFAMsⁱ	TIGR00855. L12. 1 hit.

Sequenceⁱ

Sequence statusⁱ: Complete.

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

P0A7K2-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MSITKDQIIE AVAAMSVMDV VELISAMEEK FGVSAAAAVA VAAGPVEAAE 
        60         70         80         90        100
EKTEFDVILK AAGANKVAVI KAVRGATGLG LKEAKDLVES APAALKEGVS 
       110        120 
KDDAEALKKA LEEAGAEVEV K

Length:121

Mass (Da):12,295

Last modified:January 23, 2007 - v2

Checksum:ⁱ08B051A0CDAA527E

GO

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	6	D → F AA sequence (PubMed:9868784).Curated		1

Mass spectrometryⁱ

Molecular mass is 12206.7 Da from positions 2 - 121. Determined by MALDI. Non-methylated.1 Publication

Molecular mass is 66643±13 Da from positions 2 - 121. Determined by ESI. Isolated L10(L12)4.1 Publication

Molecular mass is 12223±1 Da from positions 2 - 121. Determined by ESI. L7, acetylated Ser-2.1 Publication

Molecular mass is 12164±1 Da from positions 2 - 121. Determined by ESI. L12, unacetylated.1 Publication

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	V00339 Genomic DNA. Translation: CAA23624.1. M38301 Genomic DNA. Translation: AAA24573.1. U00006 Genomic DNA. Translation: AAC43084.1. U00096 Genomic DNA. Translation: AAC76960.1. AP009048 Genomic DNA. Translation: BAE77334.1.
PIRⁱ	S12575. R5EC7.
NCBI Reference Sequences More...RefSeqⁱ	NP_418413.1. NC_000913.3. WP_000028878.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaⁱ	AAC76960; AAC76960; b3986. BAE77334; BAE77334; BAE77334.
GeneIDⁱ	948489.
KEGGⁱ	ecj:JW3949. eco:b3986.
PATRICⁱ	fig\|1411691.4.peg.2726.

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	V00339 Genomic DNA. Translation: CAA23624.1. M38301 Genomic DNA. Translation: AAA24573.1. U00006 Genomic DNA. Translation: AAC43084.1. U00096 Genomic DNA. Translation: AAC76960.1. AP009048 Genomic DNA. Translation: BAE77334.1.
PIRⁱ	S12575. R5EC7.
NCBI Reference Sequences More...RefSeqⁱ	NP_418413.1. NC_000913.3. WP_000028878.1. 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
	1CTF	X-ray	1.70	A	48-121	[»]
	1RQS	NMR	-	A	48-121	[»]
	1RQT	NMR	-	A/B	2-38	[»]
	1RQU	NMR	-	A/B	2-121	[»]
	1RQV	NMR	-	A/B	2-121	[»]
	2BCW	electron microscopy	11.20	B	54-121	[»]
	3J7Z	electron microscopy	3.90	6	1-121	[»]
	4UY8	electron microscopy	3.80	6	2-31	[»]
	4V4V	electron microscopy	15.00	B3/B5	3-121	[»]
	4V4W	electron microscopy	15.00	B3/B5	3-121	[»]
	4V5M	electron microscopy	7.80	BL	1-121	[»]
	4V5N	electron microscopy	7.60	BL	1-121	[»]
	4V7B	electron microscopy	6.80	B6	1-121	[»]
	4V7D	electron microscopy	7.60	AL	2-121	[»]
	4V85	X-ray	3.20	J/K/L/M	1-121	[»]
	4V89	X-ray	3.70	BJ/BK/BL/BM	1-121	[»]
	4V9O	X-ray	2.90	A6	1-121	[»]
	5KCS	electron microscopy	3.90	1L	1-121	[»]
ProteinModelPortalⁱ	P0A7K2.
SMRⁱ	P0A7K2.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	852783. 1 interactor.
Database of interacting proteins More...DIPⁱ	DIP-36009N.
IntActⁱ	P0A7K2. 127 interactors.
Molecular INTeraction database More...MINTⁱ	MINT-1277405.
STRINGⁱ	511145.b3986.

2D gel databases

SWISS-2DPAGEⁱ	P0A7K2.

SWISS-2DPAGEⁱ

P0A7K2.

Proteomic databases

EPDⁱ	P0A7K2.
PaxDbⁱ	P0A7K2.
PRIDEⁱ	P0A7K2.

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	AAC76960; AAC76960; b3986. BAE77334; BAE77334; BAE77334.
GeneIDⁱ	948489.
KEGGⁱ	ecj:JW3949. eco:b3986.
PATRICⁱ	fig\|1411691.4.peg.2726.

Organism-specific databases

EchoBASEⁱ	EB0866.
EcoGeneⁱ	EG10873. rplL.

Phylogenomic databases

eggNOGⁱ	ENOG4105KBC. Bacteria. COG0222. LUCA.
HOGENOMⁱ	HOG000248813.
InParanoidⁱ	P0A7K2.
KEGG Orthology (KO) More...KOⁱ	K02935.
PhylomeDBⁱ	P0A7K2.

Enzyme and pathway databases

BioCycⁱ	EcoCyc:EG10873-MONOMER. MetaCyc:EG10873-MONOMER.

BioCycⁱ

EcoCyc:EG10873-MONOMER.
MetaCyc:EG10873-MONOMER.

Miscellaneous databases

EvolutionaryTraceⁱ	P0A7K2.
Protein Ontology More...PROⁱ	PR:P0A7K2.

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd00387. Ribosomal_L7_L12. 1 hit.
Gene3Dⁱ	3.30.1390.10. 1 hit.
HAMAPⁱ	MF_00368. Ribosomal_L7_L12. 1 hit.
InterProⁱ	View protein in InterPro IPR000206. Ribosomal_L7/12. IPR014719. Ribosomal_L7/12_C/ClpS-like. IPR013823. Ribosomal_L7/L12_C. IPR008932. Ribosomal_L7/L12_oligo.
PANTHERⁱ	PTHR24089:SF404. PTHR24089:SF404. 1 hit.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00542. Ribosomal_L12. 1 hit. PF16320. Ribosomal_L12_N. 1 hit.
ProDomⁱ	View protein in ProDom or Entries sharing at least one domain PD001326. Ribosomal_L7/L12_C. 1 hit.
SUPFAMⁱ	SSF48300. SSF48300. 1 hit. SSF54736. SSF54736. 1 hit.
TIGRFAMsⁱ	TIGR00855. L12. 1 hit.
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	RL7_ECOLI
Accessionⁱ	P0A7K2Primary (citable) accession number: P0A7K2 Secondary accession number(s): P02392, Q2M8S2
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
	Last sequence update:	January 23, 2007
	Last modified:	June 7, 2017
	This is version 118 of the entry and version 2 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

Escherichia coli
Escherichia coli (strain K12): entries and cross-references to EcoGene
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
Ribosomal proteins
Ribosomal proteins families and list of entries
SIMILARITY comments
Index of protein domains and families

Similar proteinsⁱ

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:

100%	UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%	UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%	UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P0A7K2 (RL7_ECOLI)

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50S ribosomal protein L7/L12

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>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

<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 - 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

<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 - 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

Amino acid modifications

Proteomic databases

2D gel 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

<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

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

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

Region

<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

<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 length and molecular weight.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

Experimental Info

<p>This subsection of the ‘Sequence’ section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

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

2D gel 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

Documents

Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequenceⁱ

Mass spectrometryⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ