50S ribosomal protein L14 - Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)

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Q5SHP8 (RL14_THET8) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 78. 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 L14

Gene names

Name:	rplN
Ordered Locus Names:	TTHA1682

Organism

Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) [Reference proteome] [HAMAP]

Taxonomic identifier

300852 [NCBI]

Taxonomic lineage

Bacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus ›

Protein attributes

Sequence length	122 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	This protein binds directly to 23S ribosomal RNA By similarity. HAMAP-Rule MF_01367 Contacts the 16S rRNA of the 30S subunit in two different positions helping to form bridges B5 and B8. HAMAP-Rule MF_01367
Subunit structure	Part of the 50S ribosomal subunit. Contacts protein L19. Forms a bridge to the 30S subunit in the 70S ribosome, contacting the 16S rRNA. Ref.5
Sequence similarities	Belongs to the ribosomal protein L14P family.
Mass spectrometry	Molecular mass is 13304 Da from positions 1 - 122. Determined by MALDI. Ref.3

Ontologies

Keywords
Ligand	RNA-binding rRNA-binding
Molecular function	Ribonucleoprotein Ribosomal protein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference 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: 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 – 122

122

50S ribosomal protein L14 HAMAP-Rule MF_01367

PRO_0000128566

Secondary structure

122

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q5SHP8 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 9305B92EBAAB9B6C
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FASTA

122

13,303

        10         20         30         40         50         60 
MIQPQTYLEV ADNTGARKIM CIRVLKGSNA KYATVGDVIV ASVKEAIPRG AVKEGDVVKA 

        70         80         90        100        110        120 
VVVRTKKEIK RPDGSAIRFD DNAAVIINNQ LEPRGTRVFG PVARELREKG FMKIVSLAPE 


VL

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete genome sequence of Thermus thermophilus HB8." Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S. Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: HB8 / ATCC 27634 / DSM 579.
[2]	"Identification of the 50S ribosomal proteins from the eubacterium Thermus thermophilus." Katsani K.R., Tsiboli P., Anagnostopoulos K., Urlaub H., Choli-Papadopoulou T. Biol. Chem. 381:1079-1087(2000) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-15.
[3]	"Extending ribosomal protein identifications to unsequenced bacterial strains using matrix-assisted laser desorption/ionization mass spectrometry." Suh M.-J., Hamburg D.M., Gregory S.T., Dahlberg A.E., Limbach P.A. Proteomics 5:4818-4831(2005) [PubMed] [Europe PMC] [Abstract] Cited for: MASS SPECTROMETRY.
[4]	"The path of messenger RNA through the ribosome." Yusupova G.Z., Yusupov M.M., Cate J.H.D., Noller H.F. Cell 106:233-241(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (5.0 ANGSTROMS) OF THE RIBOSOME.
[5]	"Crystal structure of the ribosome at 5.5 A resolution." Yusupov M.M., Yusupova G.Z., Baucom A., Lieberman K., Earnest T.N., Cate J.H.D., Noller H.F. Science 292:883-896(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (5.5 ANGSTROMS) OF THE RIBOSOME, INTERSUBUNIT BRIDGE FORMATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AP008226 Genomic DNA. Translation: BAD71505.1.

RefSeq

YP_144948.1. NC_006461.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GIY	X-ray	5.50	N	1-122	[»]
1YL3	X-ray	5.50	N	10-121	[»]
2HGJ	X-ray	5.00	N	1-122	[»]
2HGQ	X-ray	5.50	N	1-122	[»]
2HGU	X-ray	4.51	N	1-122	[»]
2J01	X-ray	2.80	O	1-122	[»]
2J03	X-ray	2.80	O	1-122	[»]
2V47	X-ray	3.80	O	1-122	[»]
2V49	X-ray	3.80	O	1-122	[»]
2WDI	X-ray	3.30	O	1-122	[»]
2WDJ	X-ray	3.30	O	1-122	[»]
2WDL	X-ray	3.50	O	1-122	[»]
2WDN	X-ray	3.50	O	1-122	[»]
2WH2	X-ray	3.45	O	1-122	[»]
2WH4	X-ray	3.45	O	1-122	[»]
2WRJ	X-ray	3.60	O	1-122	[»]
2WRL	X-ray	3.60	O	1-122	[»]
2WRO	X-ray	3.60	O	1-122	[»]
2WRR	X-ray	3.60	O	1-122	[»]
2X9S	X-ray	3.10	O	1-122	[»]
2X9U	X-ray	3.10	O	1-122	[»]
2XG0	X-ray	3.20	O	1-122	[»]
2XG2	X-ray	3.20	O	1-122	[»]
2XQE	X-ray	3.10	O	1-122	[»]
2XTG	electron microscopy	7.80	O	1-122	[»]
2XUX	electron microscopy	7.60	O	1-122	[»]
2Y0V	X-ray	3.10	O	1-122	[»]
2Y0X	X-ray	3.10	O	1-122	[»]
2Y0Z	X-ray	3.10	O	1-122	[»]
2Y11	X-ray	3.10	O	1-122	[»]
2Y13	X-ray	3.10	O	1-122	[»]
2Y15	X-ray	3.10	O	1-122	[»]
2Y17	X-ray	3.10	O	1-122	[»]
2Y19	X-ray	3.10	O	1-122	[»]
3FIN	electron microscopy	6.40	O	1-122	[»]
3HUX	X-ray	3.10	O	1-122	[»]
3HUZ	X-ray	3.10	O	1-122	[»]
3I8F	X-ray	3.10	N	1-122	[»]
3I8I	X-ray	3.10	N	1-122	[»]
3I9C	X-ray	3.50	N	1-122	[»]
3I9E	X-ray	3.50	N	1-122	[»]
3KIR	X-ray	3.30	O	1-122	[»]
3KIT	X-ray	3.30	O	1-122	[»]
3KIW	X-ray	3.60	O	1-122	[»]
3KIY	X-ray	3.60	O	1-122	[»]
3KNI	X-ray	3.00	O	1-122	[»]
3KNK	X-ray	3.00	O	1-122	[»]
3KNM	X-ray	3.45	O	1-122	[»]
3KNO	X-ray	3.45	O	1-122	[»]
3TVE	X-ray	3.10	N	1-122	[»]
3TVH	X-ray	3.10	N	1-122	[»]
3UXQ	X-ray	3.20	O	1-122	[»]
3UXR	X-ray	3.20	O	1-122	[»]
3UYE	X-ray	3.00	N	1-122	[»]
3UYG	X-ray	3.00	N	1-122	[»]
3UZ1	X-ray	3.30	N	1-122	[»]
3UZ2	X-ray	3.30	N	1-122	[»]
3UZ8	X-ray	3.00	N	1-122	[»]
3UZ9	X-ray	3.00	N	1-122	[»]
3UZF	X-ray	3.30	N	1-122	[»]
3UZH	X-ray	3.30	N	1-122	[»]
3UZK	X-ray	3.30	N	1-122	[»]
3UZN	X-ray	3.30	N	1-122	[»]
3V23	X-ray	3.00	O	1-122	[»]
3V25	X-ray	3.00	O	1-122	[»]
3V27	X-ray	3.10	O	1-122	[»]
3V29	X-ray	3.10	O	1-122	[»]
3V2D	X-ray	2.70	O	1-122	[»]
3V2F	X-ray	2.70	O	1-122	[»]
3ZVP	X-ray	3.80	O	1-122	[»]
4ABS	X-ray	3.10	O	1-122	[»]
4DHA	X-ray	3.20	O	1-122	[»]
4DHC	X-ray	3.20	O	1-122	[»]
4G5L	X-ray	3.30	N	1-122	[»]
4G5N	X-ray	3.30	N	1-122	[»]
4G5U	X-ray	3.10	N	1-122	[»]
4G5W	X-ray	3.10	N	1-122	[»]

ProteinModelPortal

Q5SHP8.

SMR

Q5SHP8. Positions 1-122.

ModBase

Search...

Protein-protein interaction databases

STRING

300852.TTHA1682.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

BAD71505; BAD71505; BAD71505.

GeneID

3168727.

KEGG

ttj:TTHA1682.

PATRIC

23958319. VBITheThe93045_1652.

Phylogenomic databases

eggNOG

COG0093.

HOGENOM

HOG000183702.

K02874.

OMA

MPVKKSD.

ProtClustDB

PRK05483.

Family and domain databases

Gene3D

2.40.150.20. 1 hit.

HAMAP

MF_01367_B. Ribosomal_L14_B.

InterPro

IPR005745. Ribosomal_L14_bac-type.
IPR019972. Ribosomal_L14_CS.
IPR023571. Ribosomal_L14_dom.
IPR000218. Ribosomal_L14b/L23e.
[Graphical view]

PANTHER

PTHR11761. PTHR11761. 1 hit.
PTHR11761:SF3. PTHR11761:SF3. 1 hit.

Pfam

PF00238. Ribosomal_L14. 1 hit.
[Graphical view]

SUPFAM

SSF50193. Ribosomal_L14. 1 hit.

TIGRFAMs

TIGR01067. rplN_bact. 1 hit.

PROSITE

PS00049. RIBOSOMAL_L14. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q5SHP8.

Entry information

Entry name

RL14_THET8

Accession

Primary (citable) accession number: Q5SHP8

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 29, 2005
Last sequence update:	December 21, 2004
Last modified:	May 1, 2013
This is version 78 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

Phylogenomic databases

Family and domain databases

Other

Entry information

Relevant documents