P0A7K2 (RL7_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
50S ribosomal protein L7/L12

Alternative name(s):
L8

Gene names

Name:	rplL
Ordered Locus Names:	b3986, JW3949

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	121 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.14 Ref.16
Subunit structure	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. Ref.14 Ref.15
Post-translational modification	Acetylation of Ser-2 converts L12 to L7. HAMAP-Rule MF_00368 Lys-82 was found to be 50% monomethylated. HAMAP-Rule MF_00368
Sequence similarities	Belongs to the ribosomal protein L7/L12P family.
Mass spectrometry	Molecular mass is 12206.7 Da from positions 2 - 121. Determined by MALDI. Non-methylated. Ref.13 Molecular mass is 66643±13 Da from positions 2 - 121. Determined by ESI. Isolated L10(L12)4. Ref.15 Molecular mass is 12223±1 Da from positions 2 - 121. Determined by ESI. L7, acetylated Ser-2. Ref.15 Molecular mass is 12164±1 Da from positions 2 - 121. Determined by ESI. L12, unacetylated. Ref.15

Ontologies

Keywords
Molecular function	Ribonucleoprotein Ribosomal protein
PTM	Acetylation Methylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	translation Inferred from electronic annotation. Source: UniProtKB-HAMAP
Cellular_component	cytosolic large ribosomal subunit Inferred from direct assay PubMed 4942547. Source: EcoCyc
Molecular_function	structural constituent of ribosome Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.6 Ref.7 Ref.8 Ref.9 Ref.10

Chain

2 – 121

120

50S ribosomal protein L7/L12 HAMAP-Rule MF_00368

PRO_0000157528

Regions

Region

54 – 121

68

Required for recruitment of EF-Tu and EF-G, and for EF-Tu and EF-G-promoted GTP hydrolysis HAMAP-Rule MF_00368

Amino acid modifications

Modified residue

2

1

N-acetylserine; in L7 HAMAP-Rule MF_00368

Modified residue

82

1

N6-methyllysine; partial HAMAP-Rule MF_00368

Experimental info

Mutagenesis

66

1

K → A: EF-Tu-binding and EF-Tu-promoted GTP hydrolysis reduced. Ref.14

Mutagenesis

67

1

V → D: EF-Tu-binding and EF-Tu-promoted GTP hydrolysis reduced. Ref.14

Mutagenesis

70

1

I → A: EF-Tu-binding and EF-Tu-promoted GTP hydrolysis reduced. Ref.14

Mutagenesis

71

1

K → A: EF-Tu-binding and EF-Tu-promoted GTP hydrolysis reduced. Ref.14

Mutagenesis

74

1

R → M: EF-Tu-binding and EF-Tu-promoted GTP hydrolysis reduced. Ref.14

Mutagenesis

85

1

K → A: EF-Tu-binding and EF-Tu-promoted GTP hydrolysis reduced. Ref.14

Sequence conflict

6

1

D → F AA sequence Ref.9

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

121

Helix Strand Turn

Details...

Helix

5 – 7

3

Beta strand

9 – 13

5

Helix

17 – 20

4

Beta strand

23 – 25

3

Helix

26 – 29

4

Helix

33 – 50

18

Beta strand

55 – 61

7

Helix

63 – 65

3

Helix

66 – 77

12

Helix

81 – 89

9

Beta strand

92 – 99

8

Helix

101 – 114

14

Beta strand

117 – 121

5

Sequences

	Sequence		Length	Mass (Da)
	P0A7K2 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 08B051A0CDAA527E	FASTA	121	12,295
	10 20 30 40 50 60 MSITKDQIIE AVAAMSVMDV VELISAMEEK FGVSAAAAVA VAAGPVEAAE EKTEFDVILK 70 80 90 100 110 120 AAGANKVAVI KAVRGATGLG LKEAKDLVES APAALKEGVS KDDAEALKKA LEEAGAEVEV K

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of the ribosomal protein gene cluster adjacent to the gene for RNA polymerase subunit beta in Escherichia coli." Post L.E., Strycharz G.D., Nomura M., Lewis H., Dennis P.P. Proc. Natl. Acad. Sci. U.S.A. 76:1697-1701(1979) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Sequence determination in 3'-end proximalely labelled DNA." Gurevich A.I., Avakov A.E. Bioorg. Khim. 5:301-304(1979) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes." Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L. Nucleic Acids Res. 21:5408-5417(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"The primary structure of an acidic protein from 50-S ribosomes of Escherichia coli which is involved in GTP hydrolysis dependent on elongation factors G and T." Terhorst C., Moeller W., Laursen R., Wittmann-Liebold B. Eur. J. Biochem. 34:138-152(1973) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-121. Strain: MRE-600.
[7]	"The ribosomal protein L8 is a complex L7/L12 and L10." Pettersson I., Hardy S.J.S., Liljas A. FEBS Lett. 64:135-138(1976) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-121. Strain: MRE-600.
[8]	"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Link A.J., Robison K., Church G.M. Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-13. Strain: K12 / EMG2.
[9]	"Small genes/gene-products in Escherichia coli K-12." Wasinger V.C., Humphery-Smith I. FEMS Microbiol. Lett. 169:375-382(1998) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-11. Strain: K12.
[10]	"Protein identification with N and C-terminal sequence tags in proteome projects." Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C., Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L., Hochstrasser D.F. J. Mol. Biol. 278:599-608(1998) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-5. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[11]	"The nucleotide sequence at the proximal end of rpoB gene of Escherichia coli." Gurevich A.I., Avakov A.E., Kolosov M.N. Bioorg. Khim. 5:1735-1739(1979) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 54-121.
[12]	"Escherichia coli proteome analysis using the gene-protein database." VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C. Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY 2D-GEL.
[13]	"Observation of Escherichia coli ribosomal proteins and their posttranslational modifications by mass spectrometry." Arnold R.J., Reilly J.P. Anal. Biochem. 269:105-112(1999) [PubMed] [Europe PMC] [Abstract] Cited for: MASS SPECTROMETRY. Strain: K12 / ATCC 25404 / DSM 5698 / NCIMB 11290.
[14]	"Structural basis for the function of the ribosomal L7/12 stalk in factor binding and GTPase activation." Diaconu M., Kothe U., Schlunzen F., Fischer N., Harms J.M., Tonevitsky A.G., Stark H., Rodnina M.V., Wahl M.C. Cell 121:991-1004(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, BINDING OF EF-TU AND EF-G, SUBUNIT, MUTAGENESIS OF LYS-66; VAL-67; ILE-70; LYS-71; ARG-74 AND LYS-85.
[15]	"Heptameric (L12)6/L10 rather than canonical pentameric complexes are found by tandem MS of intact ribosomes from thermophilic bacteria." Ilag L.L., Videler H., McKay A.R., Sobott F., Fucini P., Nierhaus K.H., Robinson C.V. Proc. Natl. Acad. Sci. U.S.A. 102:8192-8197(2005) [PubMed] [Europe PMC] [Abstract] Cited for: SUBUNIT, STOICHIOMETRY, MASS SPECTROMETRY.
[16]	"Bacterial ribosome requires multiple L12 dimers for efficient initiation and elongation of protein synthesis involving IF2 and EF-G." Mandava C.S., Peisker K., Ederth J., Kumar R., Ge X., Szaflarski W., Sanyal S. Nucleic Acids Res. 40:2054-2064(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN IF-2 (INFB) AND EF-G (FUSA) ASSOCIATION WITH RIBOSOME. Strain: K12 / MG1655 / ATCC 47076.
[17]	"Structure of the C-terminal domain of the ribosomal protein L7/L12 from Escherichia coli at 1.7 A." Leijonmarck M., Liljas A. J. Mol. Biol. 195:555-580(1987) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
[18]	"Topology of the secondary structure elements of ribosomal protein L7/L12 from E. coli in solution." Bocharov E.V., Gudkov A.T., Arseniev A.S. FEBS Lett. 379:291-294(1996) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR.
[19]	"Conformational independence of N- and C-domains in ribosomal protein L7/L12 and in the complex with protein L10." Bocharov E.V., Gudkov A.T., Budovskaya E.V., Arseniev A.S. FEBS Lett. 423:347-350(1998) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

PIR

R5EC7. S12575.

RefSeq

NP_418413.1. NC_000913.3.
YP_491475.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj

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	[»]
2GYA	electron microscopy	15.00	3/5	3-121	[»]
2GYC	electron microscopy	15.00	3/5	3-121	[»]
2XTG	electron microscopy	7.80	L	1-121	[»]
2XUX	electron microscopy	7.60	L	1-121	[»]
3J5O	electron microscopy	6.80	6	1-121	[»]
3J5W	electron microscopy	7.60	L	2-121	[»]
3SGF	X-ray	3.20	J/K/L/M	1-121	[»]
3UOS	X-ray	3.70	J/K/L/M	1-121	[»]
4KIX	X-ray	2.90	6	1-121	[»]

ProteinModelPortal

P0A7K2.

SMR

P0A7K2. Positions 3-121.

ModBase

Search...

MobiDB

Search...

Protein-protein interaction databases

BioGrid

852783. 1 interaction.

DIP

DIP-36009N.

IntAct

P0A7K2. 127 interactions.

MINT

MINT-1277405.

STRING

511145.b3986.

Chemistry

ChEMBL

CHEMBL2363135.

PTM databases

PhosSite

P0810430.

2D gel databases

SWISS-2DPAGE

P0A7K2.

Proteomic databases

PaxDb

P0A7K2.

PRIDE

P0A7K2.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76960; AAC76960; b3986.
BAE77334; BAE77334; BAE77334.

GeneID

12930512.
948489.

KEGG

ecj:Y75_p3211.
eco:b3986.

PATRIC

32123493. VBIEscCol129921_4099.

Organism-specific databases

EchoBASE

EB0866.

EcoGene

EG10873. rplL.

Phylogenomic databases

eggNOG

COG0222.

HOGENOM

HOG000248813.

KO

K02935.

OMA

ASMSVME.

OrthoDB

EOG6WMJ69.

PhylomeDB

P0A7K2.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10873-MONOMER.
ECOL316407:JW3949-MONOMER.

Gene expression databases

Genevestigator

P0A7K2.

Family and domain databases

Gene3D

3.30.1390.10. 1 hit.

HAMAP

MF_00368. Ribosomal_L7_L12.

InterPro

IPR000206. Ribosomal_L7/12.
IPR014719. Ribosomal_L7/12_C/ClpS-like.
IPR013823. Ribosomal_L7/L12_C.
IPR008932. Ribosomal_L7/L12_oligo.
[Graphical view]

PANTHER

PTHR11809. PTHR11809. 1 hit.

Pfam

PF00542. Ribosomal_L12. 1 hit.
[Graphical view]

ProDom

PD001326. Ribosomal_L7/L12_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SUPFAM

SSF48300. SSF48300. 1 hit.
SSF54736. SSF54736. 1 hit.

TIGRFAMs

TIGR00855. L12. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P0A7K2.

PRO

P0A7K2.

Entry information

Entry name

RL7_ECOLI

Accession

Primary (citable) accession number: P0A7K2
Secondary accession number(s): P02392, Q2M8S2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	July 9, 2014
This is version 95 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program