50S ribosomal protein L29P - Haloarcula marismortui

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Reviewed, UniProtKB/Swiss-Prot P10971 (RL29_HALMA)

Last modified November 3, 2009. Version 78. History...

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

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein names

Recommended name:
    50S ribosomal protein L29P
Alternative name(s):
    Hmal29
    Hl33

Gene names

Name:	rpl29p
Ordered Locus Names:	rrnAC1604

Organism

Haloarcula marismortui (Halobacterium marismortui) [Complete proteome] [HAMAP]

Taxonomic identifier

Taxonomic lineage

Archaea › Euryarchaeota › Halobacteria › Halobacteriales › Halobacteriaceae › Haloarcula

Protein attributes

Sequence length	71 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 I) to which it binds. Located at the polypeptide exit tunnel on the outside of the subunit. HAMAP MF_00374
Subunit structure	Part of the 50S ribosomal subunit. Interacts with protein L23. Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12
Sequence similarities	Belongs to the ribosomal protein L29P 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

1

Removed Ref.3

Chain

70

50S ribosomal protein L29P HAMAP MF_00374

PRO_0000130508

Secondary structure

1

.

.

.

.

.

.

.

71

Helix Strand Turn

Sequences

Sequence

Length

Mass (Da)

Tools

P10971-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 31779CA339CC699A
Show »

71

7,879

        10         20         30         40         50         60 
MTVLHVQEIR DMTPAEREAE LDDLKTELLN ARAVQAAGGA PENPGRIKEL RKAIARIKTI 

        70 
QGEEGDLQEN E

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Organization and nucleotide sequence of a gene cluster coding for eight ribosomal proteins in the archaebacterium Halobacterium marismortui." Arndt E., Kroemer W., Hatakeyama T. J. Biol. Chem. 265:3034-3039(1990) [PubMed: 2406244] [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: 15520287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43049 / DSM 3752 / JCM 8966.
[3]	"The primary structures of ribosomal proteins L16, L23 and L33 from the archaebacterium Halobacterium marismortui." Hatakeyama T., Hatakeyama T., Kimura M. FEBS Lett. 240:21-28(1988) [PubMed: 3191994] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-70.
[4]	"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: 2143141] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 60-71.
[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: 10937989] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF THE 50S SUBUNIT. Strain: ATCC 43049 / DSM 3752 / JCM 8966.
[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: 10937990] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF THE 50S SUBUNIT. Strain: ATCC 43049 / DSM 3752 / JCM 8966.
[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: 11828326] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF THE 50S SUBUNIT. Strain: ATCC 43049 / DSM 3752 / JCM 8966.
[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: 11483524] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF THE 50S SUBUNIT. Strain: ATCC 43049 / DSM 3752 / JCM 8966.
[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: 12150912] [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.
[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: 12185246] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF THE 50S SUBUNIT. Strain: ATCC 43049 / DSM 3752 / JCM 8966.
[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: 12860128] [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.
[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: 14561884] [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

J05222 Genomic DNA. Translation: AAA86866.1.
AY596297 Genomic DNA. Translation: AAV46521.1.
X55311 Genomic DNA. Translation: CAA39015.1.

PIR

R5HS29. A35064.
T46794.

RefSeq

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FFK	X-ray	2.40	S	2-71	[»]
1JJ2	X-ray	2.40	U	2-71	[»]
1K73	X-ray	3.01	W	2-71	[»]
1K8A	X-ray	3.00	W	2-71	[»]
1K9M	X-ray	3.00	W	2-71	[»]
1KC8	X-ray	3.01	W	2-71	[»]
1KD1	X-ray	3.00	W	2-71	[»]
1KQS	X-ray	3.10	U	2-71	[»]
1M1K	X-ray	3.20	W	2-71	[»]
1M90	X-ray	2.80	W	2-71	[»]
1N8R	X-ray	3.00	W	2-71	[»]
1NJI	X-ray	3.00	W	2-71	[»]
1Q7Y	X-ray	3.20	W	2-71	[»]
1Q81	X-ray	2.95	W	2-71	[»]
1Q82	X-ray	2.98	W	2-71	[»]
1Q86	X-ray	3.00	W	2-71	[»]
1QVF	X-ray	3.10	U	2-71	[»]
1QVG	X-ray	2.90	U	2-71	[»]
1S72	X-ray	2.40	V	1-71	[»]
1VQ4	X-ray	2.70	V	1-71	[»]
1VQ5	X-ray	2.60	V	1-71	[»]
1VQ6	X-ray	2.70	V	1-71	[»]
1VQ7	X-ray	2.50	V	1-71	[»]
1VQ8	X-ray	2.20	V	1-71	[»]
1VQ9	X-ray	2.40	V	1-71	[»]
1VQK	X-ray	2.30	V	1-71	[»]
1VQL	X-ray	2.30	V	1-71	[»]
1VQM	X-ray	2.30	V	1-71	[»]
1VQN	X-ray	2.40	V	1-71	[»]
1VQO	X-ray	2.20	V	1-71	[»]
1VQP	X-ray	2.25	V	1-71	[»]
1W2B	X-ray	3.50	U	2-70	[»]
1YHQ	X-ray	2.40	V	1-71	[»]
1YI2	X-ray	2.65	V	1-71	[»]
1YIJ	X-ray	2.60	V	1-71	[»]
1YIT	X-ray	2.80	V	1-71	[»]
1YJ9	X-ray	2.90	V	1-71	[»]
1YJN	X-ray	3.00	V	1-71	[»]
1YJW	X-ray	2.90	V	1-71	[»]
2B66	X-ray	5.90	2	2-71	[»]
2B9N	X-ray	6.76	2	2-71	[»]
2B9P	X-ray	6.46	2	2-71	[»]
2OTJ	X-ray	2.90	V	1-71	[»]
2OTL	X-ray	2.70	V	1-71	[»]
2QA4	X-ray	3.00	V	1-71	[»]
2QEX	X-ray	2.90	V	1-71	[»]
3CC2	X-ray	2.40	V	1-71	[»]
3CC4	X-ray	2.70	V	1-71	[»]
3CC7	X-ray	2.70	V	1-71	[»]
3CCE	X-ray	2.75	V	1-71	[»]
3CCJ	X-ray	2.70	V	1-71	[»]
3CCL	X-ray	2.90	V	1-71	[»]
3CCM	X-ray	2.55	V	1-71	[»]
3CCQ	X-ray	2.90	V	1-71	[»]
3CCR	X-ray	3.00	V	1-71	[»]
3CCS	X-ray	2.95	V	1-71	[»]
3CCU	X-ray	2.80	V	1-71	[»]
3CCV	X-ray	2.90	V	1-71	[»]
3CD6	X-ray	2.75	V	1-71	[»]
3CMA	X-ray	2.80	V	1-71	[»]
3CME	X-ray	2.95	V	1-71	[»]
3CPW	X-ray	2.70	U	1-71	[»]
3CXC	X-ray	3.00	U	2-70	[»]
3G4S	X-ray	3.20	V	2-66	[»]
3G6E	X-ray	2.70	V	2-66	[»]
3G71	X-ray	2.85	V	2-66	[»]

ModBase

Genome annotation databases

GeneID

GenomeReviews

Gene locus rrnAC1604 in contig AY596297_GR.

KEGG

NMPDR

fig|272569.1.peg.1495.

Organism-specific databases

CMR

Phylogenomic databases

HOGENOM

OMA

Enzyme and pathway databases

BioCyc

HMAR272569:RRNAC1604-MON.

Family and domain databases

HAMAP

MF_00374.
[Tree]

InterPro

IPR001854. Ribosomal_L29.
IPR018254. Ribosomal_L29_CS.
[Graphical view]

Pfam

PF00831. Ribosomal_L29. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00012. L29. 1 hit.

PROSITE

PS00579. RIBOSOMAL_L29. 1 hit.
[Graphical view]

ProtoNet

Entry information

Entry name

RL29_HALMA

Accession

Primary (citable) accession number: P10971
Secondary accession number(s): P22526, Q5V1T1

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	January 23, 2007
Last modified:	November 3, 2009
This is version 78 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Ribosomal proteins

Ribosomal proteins families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents