50S ribosomal protein L30P - Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)

Contribute

Send feedback

Read comments (?) or add your own

P14121 (RL30_HALMA) Reviewed, UniProtKB/Swiss-Prot

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

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

Documents (3) |

Third-party data

text xml rdf/xml gff fasta

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 L30P

Alternative name(s):
Hl16
Hl20
Hmal30

Gene names

Name:	rpl30p
Ordered Locus Names:	rrnAC1591

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	154 AA.
Sequence status	Complete.
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, stabilizing the orientation of adjacent RNA domains. HAMAP-Rule MF_01371
Subunit structure	Part of the 50S ribosomal subunit. Binds 5S rRNA. Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12
Sequence similarities	Belongs to the ribosomal protein L30P 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	large ribosomal subunit Inferred from electronic annotation. Source: InterPro
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

Chain

1 – 154

154

50S ribosomal protein L30P HAMAP-Rule MF_01371

PRO_0000104622

Experimental info

Sequence conflict

W → L Ref.2

Sequence conflict

148

Missing Ref.2

Secondary structure

154

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P14121 [UniParc].

Last modified August 1, 1992. Version 2.
Checksum: ED673F036E974C14
Show »

FASTA

154

17,042

        10         20         30         40         50         60 
MHALVQLRGE VNMHTDIQDT LEMLNIHHVN HCTLVPETDA YRGMVAKVND FVAFGEPSQE 

        70         80         90        100        110        120 
TLETVLATRA EPLEGDADVD DEWVAEHTDY DDISGLAFAL LSEETTLREQ GLSPTLRLHP 

       130        140        150 
PRGGHDGVKH PVKEGGQLGK HDTEGIDDLL EAMR

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Primary structures of five ribosomal proteins from the archaebacterium Halobacterium marismortui and their structural relationships to eubacterial and eukaryotic ribosomal proteins." Hatakeyama T., Kaufmann F., Schroeter B., Hatakeyama T. Eur. J. Biochem. 185:685-693(1989) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE.
[2]	"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].
[3]	"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.
[4]	"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 1-30.
[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: CAA41292.1.
AY596297 Genomic DNA. Translation: AAV46509.1.

PIR

R5HS30. S16543.

RefSeq

YP_136215.1. NC_006396.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FFK	X-ray	2.40	T	1-154	[»]
1JJ2	X-ray	2.40	V	1-154	[»]
1K73	X-ray	3.01	X	1-154	[»]
1K8A	X-ray	3.00	X	1-154	[»]
1K9M	X-ray	3.00	X	1-154	[»]
1KC8	X-ray	3.01	X	1-154	[»]
1KD1	X-ray	3.00	X	1-154	[»]
1KQS	X-ray	3.10	V	1-154	[»]
1M1K	X-ray	3.20	X	1-154	[»]
1M90	X-ray	2.80	X	1-154	[»]
1N8R	X-ray	3.00	X	1-154	[»]
1NJI	X-ray	3.00	X	1-154	[»]
1Q7Y	X-ray	3.20	X	1-154	[»]
1Q81	X-ray	2.95	X	1-154	[»]
1Q82	X-ray	2.98	X	1-154	[»]
1Q86	X-ray	3.00	X	1-154	[»]
1QVF	X-ray	3.10	V	1-154	[»]
1QVG	X-ray	2.90	V	1-154	[»]
1S72	X-ray	2.40	W	1-154	[»]
1VQ4	X-ray	2.70	W	1-154	[»]
1VQ5	X-ray	2.60	W	1-154	[»]
1VQ6	X-ray	2.70	W	1-154	[»]
1VQ7	X-ray	2.50	W	1-154	[»]
1VQ8	X-ray	2.20	W	1-154	[»]
1VQ9	X-ray	2.40	W	1-154	[»]
1VQK	X-ray	2.30	W	1-154	[»]
1VQL	X-ray	2.30	W	1-154	[»]
1VQM	X-ray	2.30	W	1-154	[»]
1VQN	X-ray	2.40	W	1-154	[»]
1VQO	X-ray	2.20	W	1-154	[»]
1VQP	X-ray	2.25	W	1-154	[»]
1W2B	X-ray	3.50	V	1-154	[»]
1YHQ	X-ray	2.40	W	1-154	[»]
1YI2	X-ray	2.65	W	1-154	[»]
1YIJ	X-ray	2.60	W	1-154	[»]
1YIT	X-ray	2.80	W	1-154	[»]
1YJ9	X-ray	2.90	W	1-154	[»]
1YJN	X-ray	3.00	W	1-154	[»]
1YJW	X-ray	2.90	W	1-154	[»]
2OTJ	X-ray	2.90	W	1-154	[»]
2OTL	X-ray	2.70	W	1-154	[»]
2QA4	X-ray	3.00	W	1-154	[»]
2QEX	X-ray	2.90	W	1-154	[»]
3CC2	X-ray	2.40	W	1-154	[»]
3CC4	X-ray	2.70	W	1-154	[»]
3CC7	X-ray	2.70	W	1-154	[»]
3CCE	X-ray	2.75	W	1-154	[»]
3CCJ	X-ray	2.70	W	1-154	[»]
3CCL	X-ray	2.90	W	1-154	[»]
3CCM	X-ray	2.55	W	1-154	[»]
3CCQ	X-ray	2.90	W	1-154	[»]
3CCR	X-ray	3.00	W	1-154	[»]
3CCS	X-ray	2.95	W	1-154	[»]
3CCU	X-ray	2.80	W	1-154	[»]
3CCV	X-ray	2.90	W	1-154	[»]
3CD6	X-ray	2.75	W	1-154	[»]
3CMA	X-ray	2.80	W	1-154	[»]
3CME	X-ray	2.95	W	1-154	[»]
3CPW	X-ray	2.70	V	1-154	[»]
3CXC	X-ray	3.00	V	1-154	[»]
3G4S	X-ray	3.20	W	1-154	[»]
3G6E	X-ray	2.70	W	1-154	[»]
3G71	X-ray	2.85	W	1-154	[»]
3I55	X-ray	3.11	W	1-154	[»]
3I56	X-ray	2.90	W	1-154	[»]
3OW2	X-ray	2.70	V	1-154	[»]

ProteinModelPortal

P14121.

SMR

P14121. Positions 1-154.

ModBase

Search...

Protein-protein interaction databases

STRING

272569.rrnAC1591.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAV46509; AAV46509; rrnAC1591.

GeneID

3127531.

KEGG

hma:rrnAC1591.

Organism-specific databases

CMR

Search...

Phylogenomic databases

eggNOG

COG1841.

HOGENOM

HOG000170918.

K02907.

OMA

HPPRKGH.

ProtClustDB

PRK06049.

Enzyme and pathway databases

BioCyc

HMAR272569:GJDH-1447-MONOMER.

Family and domain databases

Gene3D

1.10.15.30. 1 hit.
3.30.1390.20. 2 hits.

HAMAP

MF_01371_A. Ribosomal_L30_A.

InterPro

IPR005997. Ribosomal_L30_arc.
IPR023106. Ribosomal_L30_central_dom_arc.
IPR018038. Ribosomal_L30_CS.
IPR016082. Ribosomal_L30_ferredoxin-like.
[Graphical view]

Pfam

PF00327. Ribosomal_L30. 1 hit.
[Graphical view]

SUPFAM

SSF55129. Ribosomal_L30. 1 hit.

TIGRFAMs

TIGR01309. L30P_arch. 1 hit.

PROSITE

PS00634. RIBOSOMAL_L30. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P14121.

Entry information

Entry name

RL30_HALMA

Accession

Primary (citable) accession number: P14121
Secondary accession number(s): Q5V1U3

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	August 1, 1992
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

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

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Experimental info

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