P14123 (RL18_HALMA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
50S ribosomal protein L18P

Alternative name(s):
Hl12
Hmal18

Gene names

Name:	rpl18p
Ordered Locus Names:	rrnAC1593

Organism

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

Taxonomic identifier

272569 [NCBI]

Taxonomic lineage

cellular organisms › Archaea › Euryarchaeota › Halobacteria › Halobacteriales › Halobacteriaceae › Haloarcula › Haloarcula marismortui

Protein attributes

Sequence length	187 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	This is one of 5 proteins that mediate the attachment of the 5S rRNA onto the large ribosomal subunit, where it forms part of the central protuberance and stabilizes the orientation of adjacent RNA domains. HAMAP-Rule MF_01337_A
Subunit structure	Part of the 50S ribosomal subunit. Interacts with proteins L5 and L21e, and attaches the 5S rRNA to the 23S rRNA. Has been cross-linked to L21e. Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12
Sequence similarities	Belongs to the ribosomal protein L18P 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	5S rRNA binding Inferred from electronic annotation. Source: InterPro 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.3

Chain

2 – 187

186

50S ribosomal protein L18P HAMAP-Rule MF_01337_A

PRO_0000131400

Experimental info

Sequence conflict

18

1

R → A AA sequence Ref.3

Secondary structure

1

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187

Helix Strand Turn

Details...

Beta strand

4 – 6

3

Helix

12 – 15

4

Helix

21 – 28

8

Beta strand

34 – 39

6

Beta strand

44 – 50

7

Beta strand

53 – 55

3

Beta strand

57 – 64

8

Helix

65 – 70

6

Beta strand

76 – 78

3

Helix

79 – 95

17

Beta strand

102 – 104

3

Helix

115 – 125

11

Helix

134 – 136

3

Helix

140 – 144

5

Helix

146 – 153

8

Beta strand

159 – 162

4

Helix

170 – 181

12

Beta strand

182 – 185

4

Sequences

	Sequence		Length	Mass (Da)
	P14123 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 60E9AF3CB64E7CA5	FASTA	187	20,614
	10 20 30 40 50 60 MATGPRYKVP MRRRREARTD YHQRLRLLKS GKPRLVARKS NKHVRAQLVT LGPNGDDTLA 70 80 90 100 110 120 SAHSSDLAEY GWEAPTGNMP SAYLTGLLAG LRAQEAGVEE AVLDIGLNSP TPGSKVFAIQ 130 140 150 160 170 180 EGAIDAGLDI PHNDDVLADW QRTRGAHIAE YDEQLEEPLY SGDFDAADLP EHFDELRETL LDGDIEL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Organization and nucleotide sequence of ten ribosomal protein genes from the region equivalent to the spectinomycin operon in the archaebacterium Halobacterium marismortui." Scholzen T., Arndt E. Mol. Gen. Genet. 228:70-80(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]	"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 2-25.
[4]	"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: CROSS-LINKING TO L21E.
[5]	"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.
[6]	"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.
[7]	"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.
[8]	"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.
[9]	"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.
[10]	"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.
[11]	"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.
[12]	"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

X58395 Genomic DNA. Translation: CAA41290.1.
AY596297 Genomic DNA. Translation: AAV46511.1.

PIR

R5HS18. S16541.

RefSeq

YP_136217.1. NC_006396.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FFK	X-ray	2.40	K	2-187	[»]
1JJ2	X-ray	2.40	M	2-187	[»]
1K73	X-ray	3.01	O	2-187	[»]
1K8A	X-ray	3.00	O	2-187	[»]
1K9M	X-ray	3.00	O	2-187	[»]
1KC8	X-ray	3.01	O	2-187	[»]
1KD1	X-ray	3.00	O	2-187	[»]
1KQS	X-ray	3.10	M	2-187	[»]
1M1K	X-ray	3.20	O	2-187	[»]
1M90	X-ray	2.80	O	2-187	[»]
1N8R	X-ray	3.00	O	2-187	[»]
1NJI	X-ray	3.00	O	2-187	[»]
1Q7Y	X-ray	3.20	O	2-187	[»]
1Q81	X-ray	2.95	O	2-187	[»]
1Q82	X-ray	2.98	O	2-187	[»]
1Q86	X-ray	3.00	O	2-187	[»]
1QVF	X-ray	3.10	M	2-187	[»]
1QVG	X-ray	2.90	M	2-187	[»]
1S72	X-ray	2.40	N	1-187	[»]
1VQ4	X-ray	2.70	N	1-187	[»]
1VQ5	X-ray	2.60	N	1-187	[»]
1VQ6	X-ray	2.70	N	1-187	[»]
1VQ7	X-ray	2.50	N	1-187	[»]
1VQ8	X-ray	2.20	N	1-187	[»]
1VQ9	X-ray	2.40	N	1-187	[»]
1VQK	X-ray	2.30	N	1-187	[»]
1VQL	X-ray	2.30	N	1-187	[»]
1VQM	X-ray	2.30	N	1-187	[»]
1VQN	X-ray	2.40	N	1-187	[»]
1VQO	X-ray	2.20	N	1-187	[»]
1VQP	X-ray	2.25	N	1-187	[»]
1W2B	X-ray	3.50	M	2-186	[»]
1YHQ	X-ray	2.40	N	1-187	[»]
1YI2	X-ray	2.65	N	1-187	[»]
1YIJ	X-ray	2.60	N	1-187	[»]
1YIT	X-ray	2.80	N	1-187	[»]
1YJ9	X-ray	2.90	N	1-187	[»]
1YJN	X-ray	3.00	N	1-187	[»]
1YJW	X-ray	2.90	N	1-187	[»]
2OTJ	X-ray	2.90	N	1-187	[»]
2OTL	X-ray	2.70	N	1-187	[»]
2QA4	X-ray	3.00	N	1-187	[»]
2QEX	X-ray	2.90	N	1-187	[»]
3CC2	X-ray	2.40	N	1-187	[»]
3CC4	X-ray	2.70	N	1-187	[»]
3CC7	X-ray	2.70	N	1-187	[»]
3CCE	X-ray	2.75	N	1-187	[»]
3CCJ	X-ray	2.70	N	1-187	[»]
3CCL	X-ray	2.90	N	1-187	[»]
3CCM	X-ray	2.55	N	1-187	[»]
3CCQ	X-ray	2.90	N	1-187	[»]
3CCR	X-ray	3.00	N	1-187	[»]
3CCS	X-ray	2.95	N	1-187	[»]
3CCU	X-ray	2.80	N	1-187	[»]
3CCV	X-ray	2.90	N	1-187	[»]
3CD6	X-ray	2.75	N	1-187	[»]
3CMA	X-ray	2.80	N	1-187	[»]
3CME	X-ray	2.95	N	1-187	[»]
3CPW	X-ray	2.70	M	1-187	[»]
3CXC	X-ray	3.00	M	2-186	[»]
3G4S	X-ray	3.20	N	2-187	[»]
3G6E	X-ray	2.70	N	2-187	[»]
3G71	X-ray	2.85	N	2-187	[»]
3I55	X-ray	3.11	N	1-187	[»]
3I56	X-ray	2.90	N	1-187	[»]
3OW2	X-ray	2.70	M	2-187	[»]

ProteinModelPortal

P14123.

SMR

P14123. Positions 2-187.

ModBase

Search...

Protein-protein interaction databases

STRING

272569.rrnAC1593.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAV46511; AAV46511; rrnAC1593.

GeneID

3127918.

KEGG

hma:rrnAC1593.

Organism-specific databases

CMR

Search...

Phylogenomic databases

eggNOG

COG0256.

HOGENOM

HOG000105947.

KO

K02881.

OMA

EYGWEAP.

ProtClustDB

PRK08569.

Enzyme and pathway databases

BioCyc

HMAR272569:GJDH-1449-MONOMER.

Family and domain databases

HAMAP

MF_01337_A. Ribosomal_L18_A.

InterPro

IPR005485. Rbsml_L5_euk/L18_arc.
IPR005484. Ribosomal_L18/L5.
[Graphical view]

PANTHER

PTHR23410. PTHR23410. 1 hit.

Pfam

PF00861. Ribosomal_L18p. 1 hit.
[Graphical view]

PRINTS

PR00058. RIBOSOMALL5.

ProtoNet

Search...

Other

EvolutionaryTrace

P14123.

Entry information

Entry name

RL18_HALMA

Accession

Primary (citable) accession number: P14123
Secondary accession number(s): Q5V1U1

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 108 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program