Q5SLP7 (RL1_THET8) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
50S ribosomal protein L1

Gene names

Name:	rplA
Ordered Locus Names:	TTHA0246

Organism

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

Taxonomic identifier

300852 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus › Thermus thermophilus

Protein attributes

Sequence length	229 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	Directly binds to 23S rRNA. Forms what is known as the L1 stalk, which protrudes beyond the 70S ribosome surface. The stalk is preferentially stabilized in 70S versus 50S crystals. Interacts with the E site tRNA, blocking the exit path. This blockage implies that this section of the ribosome must be able to move to release the deacetylated tRNA. HAMAP-Rule MF_01318_B Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA By similarity. HAMAP-Rule MF_01318_B
Subunit structure	Part of the 50S ribosomal subunit.
Sequence similarities	Belongs to the ribosomal protein L1P family.
Mass spectrometry	Molecular mass is 24698 Da from positions 2 - 229. Determined by MALDI. Ref.4

Ontologies

Keywords
Biological process	Translation regulation
Ligand	RNA-binding rRNA-binding tRNA-binding
Molecular function	Repressor Ribonucleoprotein Ribosomal protein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	regulation of translation Inferred from electronic annotation. Source: UniProtKB-KW 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 tRNA binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.2

Chain

2 – 229

228

50S ribosomal protein L1 HAMAP-Rule MF_01318_B

PRO_0000125764

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

229

Helix Strand Turn

Details...

Helix

6 – 9

4

Helix

11 – 13

3

Beta strand

17 – 19

3

Turn

20 – 22

3

Helix

23 – 32

10

Beta strand

36 – 38

3

Beta strand

41 – 50

10

Beta strand

52 – 54

3

Helix

55 – 57

3

Beta strand

60 – 64

5

Helix

70 – 72

3

Beta strand

75 – 78

4

Beta strand

79 – 81

3

Helix

82 – 89

8

Beta strand

93 – 96

4

Helix

98 – 100

3

Helix

101 – 105

5

Turn

108 – 110

3

Beta strand

112 – 116

5

Helix

118 – 120

3

Helix

121 – 132

12

Turn

133 – 136

4

Helix

141 – 143

3

Beta strand

146 – 148

3

Helix

150 – 157

8

Beta strand

161 – 165

5

Beta strand

170 – 178

9

Beta strand

179 – 181

3

Helix

183 – 199

17

Beta strand

204 – 206

3

Beta strand

209 – 217

9

Beta strand

218 – 220

3

Beta strand

222 – 225

4

Sequences

	Sequence		Length	Mass (Da)
	Q5SLP7 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 99EE7BE00801B1B4	FASTA	229	24,831
	10 20 30 40 50 60 MPKHGKRYRA LLEKVDPNKV YTIDEAARLV KELATAKFDE TVEVHAKLGI DPRRSDQNVR 70 80 90 100 110 120 GTVSLPHGLG KQVRVLAIAK GEKIKEAEEA GADYVGGEEI IQKILDGWMD FDAVVATPDV 130 140 150 160 170 180 MGAVGSKLGR ILGPRGLLPN PKAGTVGFNI GEIIREIKAG RIEFRNDKTG AIHAPVGKAS 190 200 210 220 FPPEKLADNI RAFIRALEAH KPEGAKGTFL RSVYVTTTMG PSVRINPHS

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 2-26.
[3]	"Identification of the gene encoding transcription factor NusG of Thermus thermophilus." Heinrich T., Schroeder W., Erdmann V.A., Hartmann R.K. J. Bacteriol. 174:7859-7863(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 94-181.
[4]	"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.
[5]	"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.
[6]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AP008226 Genomic DNA. Translation: BAD70069.1.

RefSeq

YP_143512.1. NC_006461.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GIY	X-ray	5.50	C	2-229	[»]
1YL3	X-ray	5.50	C	2-229	[»]
2HGJ	X-ray	5.00	C	1-229	[»]
2HGQ	X-ray	5.50	C	1-229	[»]
2HGU	X-ray	4.51	C	1-229	[»]
2J01	X-ray	2.80	C	1-229	[»]
2J03	X-ray	2.80	C	1-229	[»]
2OM7	electron microscopy	7.30	K	1-229	[»]
2V47	X-ray	3.80	C	2-228	[»]
2V49	X-ray	3.80	C	2-228	[»]
2WDI	X-ray	3.30	C	1-229	[»]
2WDJ	X-ray	3.30	C	1-229	[»]
2WDL	X-ray	3.50	C	1-229	[»]
2WDN	X-ray	3.50	C	1-229	[»]
2WH2	X-ray	3.45	C	1-229	[»]
2WH4	X-ray	3.45	C	1-229	[»]
2WRJ	X-ray	3.60	C	1-229	[»]
2WRL	X-ray	3.60	C	1-229	[»]
2WRO	X-ray	3.60	C	1-229	[»]
2WRR	X-ray	3.60	C	1-229	[»]
2X9S	X-ray	3.10	C	1-229	[»]
2X9U	X-ray	3.10	C	1-229	[»]
2XG0	X-ray	3.20	C	1-229	[»]
2XG2	X-ray	3.20	C	1-229	[»]
2XQE	X-ray	3.10	C	1-229	[»]
2XTG	electron microscopy	7.80	C	1-229	[»]
2XUX	electron microscopy	7.60	C	1-229	[»]
2Y0V	X-ray	3.10	C	1-229	[»]
2Y0X	X-ray	3.10	C	1-229	[»]
2Y0Z	X-ray	3.10	C	1-229	[»]
2Y11	X-ray	3.10	C	1-229	[»]
2Y13	X-ray	3.10	C	1-229	[»]
2Y15	X-ray	3.10	C	1-229	[»]
2Y17	X-ray	3.10	C	1-229	[»]
2Y19	X-ray	3.10	C	1-229	[»]
3FIN	electron microscopy	6.40	C	35-225	[»]
3HUX	X-ray	3.10	C	1-229	[»]
3HUZ	X-ray	3.10	C	1-229	[»]
3KIR	X-ray	3.30	C	1-229	[»]
3KIT	X-ray	3.30	C	1-229	[»]
3KIW	X-ray	3.60	C	1-229	[»]
3KIY	X-ray	3.60	C	1-229	[»]
3KNI	X-ray	3.00	C	1-229	[»]
3KNK	X-ray	3.00	C	1-229	[»]
3KNM	X-ray	3.45	C	1-229	[»]
3KNO	X-ray	3.45	C	1-229	[»]
3TG8	X-ray	1.95	A	1-229	[»]
3ZVP	X-ray	3.80	C	1-229	[»]
4ABS	X-ray	3.10	C	1-229	[»]

ProteinModelPortal

Q5SLP7.

SMR

Q5SLP7. Positions 2-229.

ModBase

Search...

Protein-protein interaction databases

STRING

300852.TTHA0246.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

BAD70069; BAD70069; BAD70069.

GeneID

3168861.

KEGG

ttj:TTHA0246.

PATRIC

23955439. VBITheThe93045_0246.

Phylogenomic databases

eggNOG

COG0081.

HOGENOM

HOG000207015.

KO

K02863.

OMA

AKGRYVK.

ProtClustDB

PRK05424.

Family and domain databases

Gene3D

3.30.190.20. 2 hits.
3.40.50.790. 1 hit.

HAMAP

MF_01318_B. Ribosomal_L1_B.

InterPro

IPR005878. Ribosom_L1_bac-type.
IPR002143. Ribosomal_L1.
IPR016094. Ribosomal_L1_2-a/b-sand.
IPR016095. Ribosomal_L1_3-a/b-sand.
IPR023673. Ribosomal_L1_CS.
IPR023674. Ribosomal_L1_SF.
[Graphical view]

Pfam

PF00687. Ribosomal_L1. 1 hit.
[Graphical view]

PIRSF

PIRSF002155. Ribosomal_L1. 1 hit.

SUPFAM

SSF56808. Ribosomal_L1. 1 hit.

TIGRFAMs

TIGR01169. rplA_bact. 1 hit.

PROSITE

PS01199. RIBOSOMAL_L1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q5SLP7.

Entry information

Entry name

RL1_THET8

Accession

Primary (citable) accession number: Q5SLP7

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 29, 2005
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 79 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program