50S ribosomal protein L13P - Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)

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P29198 (RL13_HALMA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 97. 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 L13P

Alternative name(s):
Hmal13

Gene names

Name:	rpl13p
Ordered Locus Names:	rrnAC0065

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

General annotation (Comments)

Function	This protein is one of the early assembly proteins of the 50S ribosomal subunit By similarity. Binds to 23S rRNA. HAMAP-Rule MF_01366
Subunit structure	Part of the 50S ribosomal subunit. Interacts weakly with proteins L3 and L6. Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10
Sequence similarities	Belongs to the ribosomal protein L13P 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	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 – 145

145

50S ribosomal protein L13P HAMAP-Rule MF_01366

PRO_0000133758

Secondary structure

145

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P29198 [UniParc].

Last modified December 1, 1992. Version 1.
Checksum: 069CE666662AE3BC
Show »

FASTA

145

16,228

        10         20         30         40         50         60 
MSVAEFDADV IVDARDCIMG RVASQVAEQA LDGETVAVVN AERAVITGRE EQIVEKYEKR 

        70         80         90        100        110        120 
VDIGNDNGYF YPKRPDGIFK RTIRGMLPHK KQRGREAFES VRVYLGNPYD EDGEVLDGTS 

       130        140 
LDRLSNIKFV TLGEISETLG ANKTW

« 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]	"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]	"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.
[7]	"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.
[8]	"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.
[9]	"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.
[10]	"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: AAA73097.1.
AY596297 Genomic DNA. Translation: AAV45145.1.

PIR

B41715.

RefSeq

YP_134851.1. NC_006396.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FFK	X-ray	2.40	G	1-145	[»]
1JJ2	X-ray	2.40	I	1-145	[»]
1K73	X-ray	3.01	K	1-145	[»]
1K8A	X-ray	3.00	K	1-145	[»]
1K9M	X-ray	3.00	K	1-145	[»]
1KC8	X-ray	3.01	K	1-145	[»]
1KD1	X-ray	3.00	K	1-145	[»]
1KQS	X-ray	3.10	I	1-145	[»]
1M1K	X-ray	3.20	K	1-145	[»]
1M90	X-ray	2.80	K	1-145	[»]
1N8R	X-ray	3.00	K	1-145	[»]
1NJI	X-ray	3.00	K	1-145	[»]
1Q7Y	X-ray	3.20	K	1-145	[»]
1Q81	X-ray	2.95	K	1-145	[»]
1Q82	X-ray	2.98	K	1-145	[»]
1Q86	X-ray	3.00	K	1-145	[»]
1QVF	X-ray	3.10	I	1-145	[»]
1QVG	X-ray	2.90	I	1-145	[»]
1S72	X-ray	2.40	J	1-145	[»]
1VQ4	X-ray	2.70	J	1-145	[»]
1VQ5	X-ray	2.60	J	1-145	[»]
1VQ6	X-ray	2.70	J	1-145	[»]
1VQ7	X-ray	2.50	J	1-145	[»]
1VQ8	X-ray	2.20	J	1-145	[»]
1VQ9	X-ray	2.40	J	1-145	[»]
1VQK	X-ray	2.30	J	1-145	[»]
1VQL	X-ray	2.30	J	1-145	[»]
1VQM	X-ray	2.30	J	1-145	[»]
1VQN	X-ray	2.40	J	1-145	[»]
1VQO	X-ray	2.20	J	1-145	[»]
1VQP	X-ray	2.25	J	1-145	[»]
1W2B	X-ray	3.50	I	1-145	[»]
1YHQ	X-ray	2.40	J	1-145	[»]
1YI2	X-ray	2.65	J	1-145	[»]
1YIJ	X-ray	2.60	J	1-145	[»]
1YIT	X-ray	2.80	J	1-145	[»]
1YJ9	X-ray	2.90	J	1-145	[»]
1YJN	X-ray	3.00	J	1-145	[»]
1YJW	X-ray	2.90	J	1-145	[»]
2OTJ	X-ray	2.90	J	1-145	[»]
2OTL	X-ray	2.70	J	1-145	[»]
2QA4	X-ray	3.00	J	1-145	[»]
2QEX	X-ray	2.90	J	1-145	[»]
3CC2	X-ray	2.40	J	1-145	[»]
3CC4	X-ray	2.70	J	1-145	[»]
3CC7	X-ray	2.70	J	1-145	[»]
3CCE	X-ray	2.75	J	1-145	[»]
3CCJ	X-ray	2.70	J	1-145	[»]
3CCL	X-ray	2.90	J	1-145	[»]
3CCM	X-ray	2.55	J	1-145	[»]
3CCQ	X-ray	2.90	J	1-145	[»]
3CCR	X-ray	3.00	J	1-145	[»]
3CCS	X-ray	2.95	J	1-145	[»]
3CCU	X-ray	2.80	J	1-145	[»]
3CCV	X-ray	2.90	J	1-145	[»]
3CD6	X-ray	2.75	J	1-145	[»]
3CMA	X-ray	2.80	J	1-145	[»]
3CME	X-ray	2.95	J	1-145	[»]
3CPW	X-ray	2.70	I	1-145	[»]
3CXC	X-ray	3.00	I	1-145	[»]
3G4S	X-ray	3.20	J	4-145	[»]
3G6E	X-ray	2.70	J	4-145	[»]
3G71	X-ray	2.85	J	4-145	[»]
3I55	X-ray	3.11	J	1-145	[»]
3I56	X-ray	2.90	J	1-145	[»]
3OW2	X-ray	2.70	I	4-145	[»]

ProteinModelPortal

P29198.

SMR

P29198. Positions 4-145.

ModBase

Search...

Protein-protein interaction databases

STRING

272569.rrnAC0065.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAV45145; AAV45145; rrnAC0065.

GeneID

3130528.

KEGG

hma:rrnAC0065.

Organism-specific databases

CMR

Search...

Phylogenomic databases

eggNOG

COG0102.

HOGENOM

HOG000225287.

K02871.

OMA

DWAYAKY.

ProtClustDB

PRK06394.

Enzyme and pathway databases

BioCyc

HMAR272569:GJDH-61-MONOMER.

Family and domain databases

Gene3D

3.90.1180.10. 1 hit.

HAMAP

MF_01366_A. Ribosomal_L13_A.

InterPro

IPR005822. Ribosomal_L13.
IPR023563. Ribosomal_L13_CS.
IPR023564. Ribosomal_L13_dom.
IPR005755. Ribosomal_L13_euk/arc.
[Graphical view]

PANTHER

PTHR11545. PTHR11545. 1 hit.
PTHR11545:SF3. PTHR11545:SF3. 1 hit.

Pfam

PF00572. Ribosomal_L13. 1 hit.
[Graphical view]

PIRSF

PIRSF002181. Ribosomal_L13. 1 hit.

SUPFAM

SSF52161. Ribosomal_L13. 1 hit.

TIGRFAMs

TIGR01077. L13_A_E. 1 hit.

PROSITE

PS00783. RIBOSOMAL_L13. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P29198.

Entry information

Entry name

RL13_HALMA

Accession

Primary (citable) accession number: P29198
Secondary accession number(s): Q5V5Q7

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	December 1, 1992
Last modified:	May 1, 2013
This is version 97 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

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