50S ribosomal protein L18e - Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)

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P12733 (RL18E_HALMA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 107. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
50S ribosomal protein L18e

Alternative name(s):
Hl29
L19

Gene names

Name:	rpl18e
Ordered Locus Names:	rrnAC0064

Organism

Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) (Halobacterium marismortui) [Complete proteome] [HAMAP]

Taxonomic identifier

272569 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Halobacteria › Halobacteriales › Halobacteriaceae › Haloarcula ›

Protein attributes

Sequence length	116 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	Stabilizes the tertiary rRNA structure within the 23S rRNA domain (domain II) to which it binds. HAMAP-Rule MF_00329
Subunit structure	Part of the 50S ribosomal subunit. Interacts weakly with proteins L4 and L15. Has been cross-linked to L4. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14
Sequence similarities	Belongs to the ribosomal protein L18e family.

Ontologies

Keywords
Ligand	RNA-binding rRNA-binding
Molecular function	Ribonucleoprotein Ribosomal protein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological_process	translation Inferred from electronic annotation. Source: HAMAP
Cellular_component	ribosome Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	rRNA binding Inferred from electronic annotation. Source: UniProtKB-KW 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

Removed Ref.3 Ref.5

Chain

2 – 116

115

50S ribosomal protein L18e HAMAP-Rule MF_00329

PRO_0000132787

Secondary structure

116

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P12733 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: BFACD702AE94474D
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FASTA

116

12,422

        10         20         30         40         50         60 
MSKTNPRLSS LIADLKSAAR SSGGAVWGDV AERLEKPRRT HAEVNLGRIE RYAQEDETVV 

        70         80         90        100        110 
VPGKVLGSGV LQKDVTVAAV DFSGTAETKI DQVGEAVSLE QAIENNPEGS HVRVIR

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Halobacterial S9 operon. Three ribosomal protein genes are cotranscribed with genes encoding a tRNA(Leu), the enolase, and a putative membrane protein in the archaebacterium Haloarcula (Halobacterium) marismortui." Kroemer W.J., Arndt E. J. Biol. Chem. 266:24573-24579(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea." Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W., Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E., Hood L., Ng W.V. Genome Res. 14:2221-2234(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
[3]	"Complete amino acid sequences of the ribosomal proteins L25, L29 and L31 from the archaebacterium Halobacterium marismortui." Hatakeyama T., Kimura M. Eur. J. Biochem. 172:703-711(1988) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-116.
[4]	"The alpha-operon equivalent genome region in the extreme halophilic archaebacterium Haloarcula (Halobacterium) marismortui." Scholzen T., Arndt E. J. Biol. Chem. 267:12123-12130(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-72.
[5]	"Extended N-terminal sequencing of proteins of archaebacterial ribosomes blotted from two-dimensional gels onto glass fiber and poly(vinylidene difluoride) membrane." Walsh M.J., McDougall J., Wittmann-Liebold B. Biochemistry 27:6867-6876(1988) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-24.
[6]	"Localization of proteins HL29 and HL31 from Haloarcula marismortui within the 50 S ribosomal subunit by chemical crosslinking." Bergmann U., Wittmann-Liebold B. J. Mol. Biol. 232:693-700(1993) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 4-27; 37-39 AND 65-82, CROSS-LINKING TO L4.
[7]	"The complete atomic structure of the large ribosomal subunit at 2.4 A resolution." Ban N., Nissen P., Hansen J., Moore P.B., Steitz T.A. Science 289:905-920(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF THE 50S SUBUNIT. Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
[8]	"The structural basis of ribosome activity in peptide bond synthesis." Nissen P., Hansen J., Ban N., Moore P.B., Steitz T.A. Science 289:920-930(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF THE 50S SUBUNIT. Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
[9]	"A pre-translocational intermediate in protein synthesis observed in crystals of enzymatically active 50S subunits." Schmeing T.M., Seila A.C., Hansen J.L., Freeborn B., Soukup J.K., Scaringe S.A., Strobel S.A., Moore P.B., Steitz T.A. Nat. Struct. Biol. 9:225-230(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF THE 50S SUBUNIT. Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
[10]	"The kink-turn: a new RNA secondary structure motif." Klein D.J., Schmeing T.M., Moore P.B., Steitz T.A. EMBO J. 20:4214-4221(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF THE 50S SUBUNIT. Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
[11]	"The structures of four macrolide antibiotics bound to the large ribosomal subunit." Hansen J.L., Ippolito J.A., Ban N., Nissen P., Moore P.B., Steitz T.A. Mol. Cell 10:117-128(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH FOUR MACROLIDE ANTIBIOTICS. Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
[12]	"Structural insights into peptide bond formation." Hansen J.L., Schmeing T.M., Moore P.B., Steitz T.A. Proc. Natl. Acad. Sci. U.S.A. 99:11670-11675(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF THE 50S SUBUNIT. Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
[13]	"Structures of five antibiotics bound at the peptidyl transferase center of the large ribosomal subunit." Hansen J.L., Moore P.B., Steitz T.A. J. Mol. Biol. 330:1061-1075(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH FIVE ANTIBIOTICS AT THE PEPTIDYL TRANSFERASE CENTER. Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
[14]	"Structures of deacylated tRNA mimics bound to the E site of the large ribosomal subunit." Schmeing T.M., Moore P.B., Steitz T.A. RNA 9:1345-1352(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF THE 50S SUBUNIT WITH TWO DIFFERENT E SITE SUBSTRATES.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M76567 Genomic DNA. Translation: AAA73096.1.
AY596297 Genomic DNA. Translation: AAV45144.1.
M87833 Genomic DNA. Translation: AAA73213.1.

PIR

R5HSH9. A41715.

RefSeq

YP_134850.1. NC_006396.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FFK	X-ray	2.40	L	2-116	[»]
1JJ2	X-ray	2.40	N	2-116	[»]
1K73	X-ray	3.01	P	2-116	[»]
1K8A	X-ray	3.00	P	2-116	[»]
1K9M	X-ray	3.00	P	2-116	[»]
1KC8	X-ray	3.01	P	2-116	[»]
1KD1	X-ray	3.00	P	2-116	[»]
1KQS	X-ray	3.10	N	2-116	[»]
1M1K	X-ray	3.20	P	2-116	[»]
1M90	X-ray	2.80	P	2-116	[»]
1N8R	X-ray	3.00	P	2-116	[»]
1NJI	X-ray	3.00	P	2-116	[»]
1Q7Y	X-ray	3.20	P	2-116	[»]
1Q81	X-ray	2.95	P	2-116	[»]
1Q82	X-ray	2.98	P	2-116	[»]
1Q86	X-ray	3.00	P	2-116	[»]
1QVF	X-ray	3.10	N	2-116	[»]
1QVG	X-ray	2.90	N	2-116	[»]
1S72	X-ray	2.40	O	1-116	[»]
1VQ4	X-ray	2.70	O	1-116	[»]
1VQ5	X-ray	2.60	O	1-116	[»]
1VQ6	X-ray	2.70	O	1-116	[»]
1VQ7	X-ray	2.50	O	1-116	[»]
1VQ8	X-ray	2.20	O	1-116	[»]
1VQ9	X-ray	2.40	O	1-116	[»]
1VQK	X-ray	2.30	O	1-116	[»]
1VQL	X-ray	2.30	O	1-116	[»]
1VQM	X-ray	2.30	O	1-116	[»]
1VQN	X-ray	2.40	O	1-116	[»]
1VQO	X-ray	2.20	O	1-116	[»]
1VQP	X-ray	2.25	O	1-116	[»]
1W2B	X-ray	3.50	N	2-115	[»]
1YHQ	X-ray	2.40	O	1-116	[»]
1YI2	X-ray	2.65	O	1-116	[»]
1YIJ	X-ray	2.60	O	1-116	[»]
1YIT	X-ray	2.80	O	1-116	[»]
1YJ9	X-ray	2.90	O	1-116	[»]
1YJN	X-ray	3.00	O	1-116	[»]
1YJW	X-ray	2.90	O	1-116	[»]
2OTJ	X-ray	2.90	O	1-116	[»]
2OTL	X-ray	2.70	O	1-116	[»]
2QA4	X-ray	3.00	O	1-116	[»]
2QEX	X-ray	2.90	O	1-116	[»]
3CC2	X-ray	2.40	O	1-116	[»]
3CC4	X-ray	2.70	O	1-116	[»]
3CC7	X-ray	2.70	O	1-116	[»]
3CCE	X-ray	2.75	O	1-116	[»]
3CCJ	X-ray	2.70	O	1-116	[»]
3CCL	X-ray	2.90	O	1-116	[»]
3CCM	X-ray	2.55	O	1-116	[»]
3CCQ	X-ray	2.90	O	1-116	[»]
3CCR	X-ray	3.00	O	1-116	[»]
3CCS	X-ray	2.95	O	1-116	[»]
3CCU	X-ray	2.80	O	1-116	[»]
3CCV	X-ray	2.90	O	1-116	[»]
3CD6	X-ray	2.75	O	1-116	[»]
3CMA	X-ray	2.80	O	1-116	[»]
3CME	X-ray	2.95	O	1-116	[»]
3CPW	X-ray	2.70	N	1-116	[»]
3CXC	X-ray	3.00	N	2-115	[»]
3G4S	X-ray	3.20	O	2-116	[»]
3G6E	X-ray	2.70	O	2-116	[»]
3G71	X-ray	2.85	O	2-116	[»]
3I55	X-ray	3.11	O	1-116	[»]
3I56	X-ray	2.90	O	1-116	[»]
3OW2	X-ray	2.70	N	2-116	[»]

ProteinModelPortal

P12733.

SMR

P12733. Positions 2-116.

ModBase

Search...

Protein-protein interaction databases

STRING

272569.rrnAC0064.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAV45144; AAV45144; rrnAC0064.

GeneID

3130533.

KEGG

hma:rrnAC0064.

Organism-specific databases

CMR

Search...

Phylogenomic databases

eggNOG

COG1727.

HOGENOM

HOG000225300.

K02883.

OMA

SKINRYT.

ProtClustDB

PRK04005.

Enzyme and pathway databases

BioCyc

HMAR272569:GJDH-60-MONOMER.

Family and domain databases

HAMAP

MF_00329. Ribosomal_L18e.

InterPro

IPR001196. Ribosomal_L15_CS.
IPR021131. Ribosomal_L18e/L15P.
IPR022947. Ribosomal_L18e_arc.
IPR021132. Ribosomal_L18e_CS.
[Graphical view]

Pfam

PF00828. Ribosomal_L18e. 1 hit.
[Graphical view]

SUPFAM

SSF52080. Ribosomal_L18e/L15. 1 hit.

PROSITE

PS01106. RIBOSOMAL_L18E. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P12733.

Entry information

Entry name

RL18E_HALMA

Accession

Primary (citable) accession number: P12733
Secondary accession number(s): Q5V5Q8

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 107 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Ribosomal proteins

Ribosomal proteins families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Other

Entry information

Relevant documents