50S ribosomal protein L14P - Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)

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P22450 (RL14_HALMA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 96. 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 L14P

Alternative name(s):
Hl27
Hmal14

Gene names

Name:	rpl14p
Ordered Locus Names:	rrnAC1602

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	132 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Forms part of two intersubunit bridges in the 70S ribosome By similarity. Binds to 23S rRNA. HAMAP-Rule MF_01367
Subunit structure	The L3/L14/L24e cluster may contact the 16S rRNA in 2 intersubunit bridges By similarity. Part of the 50S ribosomal subunit. Forms a cluster with proteins L3 and L24e. Ref.3 Ref.4 Ref.5 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11
Sequence similarities	Belongs to the ribosomal protein L14P family.

Ontologies

Keywords
Ligand	RNA-binding rRNA-binding
Molecular function	Ribonucleoprotein Ribosomal protein
Technical term	3D-structure Complete proteome
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: HAMAP 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 – 132

132

50S ribosomal protein L14P HAMAP-Rule MF_01367

PRO_0000128571

Secondary structure

132

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P22450 [UniParc].

Last modified August 1, 1991. Version 1.
Checksum: 536F9C4461B7EA87
Show »

FASTA

132

14,193

        10         20         30         40         50         60 
MEALGADVTQ GLEKGSLITC ADNTGARELK VISVHGYSGT KNRHPKAGLG DKITVSVTKG 

        70         80         90        100        110        120 
TPEMRRQVLE AVVVRQRKPI RRPDGTRVKF EDNAAVIVDE NEDPRGTELK GPIAREVAQR 

       130 
FGSVASAATM IV

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of four genes encoding ribosomal proteins from the 'S10 and spectinomycin' operon equivalent region in the archaebacterium Halobacterium marismortui." Arndt E. FEBS Lett. 267:193-198(1990) [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]	"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.
[4]	"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.
[5]	"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.
[6]	"Placement of protein and RNA structures into a 5 A-resolution map of the 50S ribosomal subunit." Ban N., Nissen P., Hansen J., Capel M., Moore P.B., Steitz T.A. Nature 400:841-847(1999) [PubMed] [Europe PMC] [Abstract] Cited for: 3D-STRUCTURE MODELING.
[7]	"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.
[8]	"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.
[9]	"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.
[10]	"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.
[11]	"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

X55311 Genomic DNA. Translation: CAA39018.1.
AY596297 Genomic DNA. Translation: AAV46519.1.

PIR

R5HS14. S10734.

RefSeq

YP_136225.1. NC_006396.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1C04	X-ray	5.00	D	31-107	[»]
1FFK	X-ray	2.40	H	1-132	[»]
1JJ2	X-ray	2.40	J	1-132	[»]
1K73	X-ray	3.01	L	1-132	[»]
1K8A	X-ray	3.00	L	1-132	[»]
1K9M	X-ray	3.00	L	1-132	[»]
1KC8	X-ray	3.01	L	1-132	[»]
1KD1	X-ray	3.00	L	1-132	[»]
1KQS	X-ray	3.10	J	1-132	[»]
1M1K	X-ray	3.20	L	1-132	[»]
1M90	X-ray	2.80	L	1-132	[»]
1N8R	X-ray	3.00	L	1-132	[»]
1NJI	X-ray	3.00	L	1-132	[»]
1Q7Y	X-ray	3.20	L	1-132	[»]
1Q81	X-ray	2.95	L	1-132	[»]
1Q82	X-ray	2.98	L	1-132	[»]
1Q86	X-ray	3.00	L	1-132	[»]
1QVF	X-ray	3.10	J	1-132	[»]
1QVG	X-ray	2.90	J	1-132	[»]
1S72	X-ray	2.40	K	1-132	[»]
1VQ4	X-ray	2.70	K	1-132	[»]
1VQ5	X-ray	2.60	K	1-132	[»]
1VQ6	X-ray	2.70	K	1-132	[»]
1VQ7	X-ray	2.50	K	1-132	[»]
1VQ8	X-ray	2.20	K	1-132	[»]
1VQ9	X-ray	2.40	K	1-132	[»]
1VQK	X-ray	2.30	K	1-132	[»]
1VQL	X-ray	2.30	K	1-132	[»]
1VQM	X-ray	2.30	K	1-132	[»]
1VQN	X-ray	2.40	K	1-132	[»]
1VQO	X-ray	2.20	K	1-132	[»]
1VQP	X-ray	2.25	K	1-132	[»]
1W2B	X-ray	3.50	J	1-132	[»]
1YHQ	X-ray	2.40	K	1-132	[»]
1YI2	X-ray	2.65	K	1-132	[»]
1YIJ	X-ray	2.60	K	1-132	[»]
1YIT	X-ray	2.80	K	1-132	[»]
1YJ9	X-ray	2.90	K	1-132	[»]
1YJN	X-ray	3.00	K	1-132	[»]
1YJW	X-ray	2.90	K	1-132	[»]
2OTJ	X-ray	2.90	K	1-132	[»]
2OTL	X-ray	2.70	K	1-132	[»]
2QA4	X-ray	3.00	K	1-132	[»]
2QEX	X-ray	2.90	K	1-132	[»]
3CC2	X-ray	2.40	K	1-132	[»]
3CC4	X-ray	2.70	K	1-132	[»]
3CC7	X-ray	2.70	K	1-132	[»]
3CCE	X-ray	2.75	K	1-132	[»]
3CCJ	X-ray	2.70	K	1-132	[»]
3CCL	X-ray	2.90	K	1-132	[»]
3CCM	X-ray	2.55	K	1-132	[»]
3CCQ	X-ray	2.90	K	1-132	[»]
3CCR	X-ray	3.00	K	1-132	[»]
3CCS	X-ray	2.95	K	1-132	[»]
3CCU	X-ray	2.80	K	1-132	[»]
3CCV	X-ray	2.90	K	1-132	[»]
3CD6	X-ray	2.75	K	1-132	[»]
3CMA	X-ray	2.80	K	1-132	[»]
3CME	X-ray	2.95	K	1-132	[»]
3CPW	X-ray	2.70	J	1-132	[»]
3CXC	X-ray	3.00	J	1-132	[»]
3G4S	X-ray	3.20	K	1-132	[»]
3G6E	X-ray	2.70	K	1-132	[»]
3G71	X-ray	2.85	K	1-132	[»]
3I55	X-ray	3.11	K	1-132	[»]
3I56	X-ray	2.90	K	1-132	[»]
3OW2	X-ray	2.70	J	1-132	[»]

ProteinModelPortal

P22450.

SMR

P22450. Positions 1-132.

ModBase

Search...

Protein-protein interaction databases

STRING

272569.rrnAC1602.

Proteomic databases

PRIDE

P22450.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAV46519; AAV46519; rrnAC1602.

GeneID

3128380.

KEGG

hma:rrnAC1602.

Organism-specific databases

CMR

Search...

Phylogenomic databases

eggNOG

COG0093.

HOGENOM

HOG000183703.

K02874.

OMA

QRKEYRR.

ProtClustDB

PRK08571.

Enzyme and pathway databases

BioCyc

HMAR272569:GJDH-1458-MONOMER.

Family and domain databases

Gene3D

2.40.150.20. 1 hit.

HAMAP

MF_01367_A. Ribosomal_L14_A.

InterPro

IPR019972. Ribosomal_L14_CS.
IPR023571. Ribosomal_L14_dom.
IPR000218. Ribosomal_L14b/L23e.
IPR019971. Ribosomal_L14P_arc.
[Graphical view]

PANTHER

PTHR11761. PTHR11761. 1 hit.

Pfam

PF00238. Ribosomal_L14. 1 hit.
[Graphical view]

SUPFAM

SSF50193. Ribosomal_L14. 1 hit.

TIGRFAMs

TIGR03673. rpl14p_arch. 1 hit.

PROSITE

PS00049. RIBOSOMAL_L14. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P22450.

Entry information

Entry name

RL14_HALMA

Accession

Primary (citable) accession number: P22450
Secondary accession number(s): Q5V1T3

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	August 1, 1991
Last modified:	May 1, 2013
This is version 96 of the entry and version 1 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

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic 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