Reviewed, UniProtKB/Swiss-Prot P27150 (RL1_THETH)

Names and origin

Protein names

Recommended name:
    50S ribosomal protein L1

Gene names

Name:	rplA
Synonyms:	rpl1

Organism

Thermus thermophilus

Taxonomic identifier

274 [NCBI]

Taxonomic lineage

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

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	The L1 stalk is quite mobile in the ribosome, and is involved in E site tRNA release By similarity. Binds directly to 23S rRNA. Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA By similarity.
Subunit structure	Part of the 50S ribosomal subunit. HAMAP MF_01318
Sequence similarities	Belongs to the ribosomal protein L1P family.

Ontologies

Keywords
Biological process	Translation regulation
Ligand	RNA-binding rRNA-binding tRNA-binding
Molecular function	Repressor Ribonucleoprotein Ribosomal protein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	RNA processing Inferred from electronic annotation. Source: InterPro 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 Ref.3

Chain

2 – 229

228

50S ribosomal protein L1 HAMAP MF_01318

PRO_0000125765

Experimental info

Sequence conflict

2

1

P → V AA sequence Ref.3

Sequence conflict

4 – 5

2

HG → TN AA sequence Ref.3

Sequence conflict

14

1

K → F AA sequence Ref.3

Secondary structure

1

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229

Helix Strand Turn

Details...

Turn

9 – 13

5

Helix

23 – 31

9

Beta strand

36 – 38

3

Beta strand

41 – 50

10

Helix

55 – 57

3

Beta strand

60 – 64

5

Beta strand

66 – 68

3

Beta strand

75 – 78

4

Helix

82 – 89

8

Beta strand

93 – 96

4

Helix

98 – 100

3

Helix

101 – 105

5

Beta strand

112 – 116

5

Helix

118 – 120

3

Helix

121 – 135

15

Turn

141 – 144

4

Helix

150 – 158

9

Beta strand

161 – 165

5

Beta strand

170 – 178

9

Helix

183 – 198

16

Beta strand

209 – 216

8

Beta strand

223 – 225

3

Sequences

	Sequence		Length	Mass (Da)
	P27150-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 38C14B2563718175	FASTA	229	24,826
	10 20 30 40 50 60 MPKHGKRYRA LLEKVDPNKI YTIDEAAHLV 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

[1]	"Cloning and overexpression of the ribosomal protein L1 gene from Thermus thermophilus VK1. Crystallization of the recombinant protein L1." Ossina N., Eliseikina I.A., Garber M.B., Jonsson B.-H. Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: VK1.
[2]	"The complete primary structure of ribosomal protein L1 from Thermus thermophilus." Amons R., Muranova T.A., Rykunova A.I., Eliseikina I.A., Sedelnikova S.E. J. Protein Chem. 12:725-734(1993) [PubMed: 8136022] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-229.
[3]	"Ribosomal proteins from Thermus thermophilus for structural investigations." Garber M.B., Agalarov S.C., Eliseikina I.A., Fomenkova N.P., Nikonov S.V., Sedelnikova S.E., Shikaeva O.S., Vasiliev D., Zhdanov A.S., Liljas A., Svensson L.A. Biochimie 74:327-336(1992) [PubMed: 1637860] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-16. Strain: VK1.
[4]	"Interaction of ribosomal L1 proteins from mesophilic and thermophilic Archaea and Bacteria with specific L1-binding sites on 23S rRNA and mRNA." Koehrer C., Mayer C., Neumair O., Groebner P., Piendl W. Eur. J. Biochem. 256:97-105(1998) [PubMed: 9746351] [Abstract] Cited for: BINDING TO METHANOCOCCUS VANNIELII 23S RRNA AND TO M.VANNIELII L1 MRNA. Strain: VK1.
[5]	"Crystal structure of the RNA binding ribosomal protein L1 from Thermus thermophilus." Nikonov S.V., Nevskaya N., Eliseikina I.A., Fomenkova N.P., Nikulin A., Ossina N., Garber M.B., Jonsson B.-H., Briand C., Al-Karadaghi S., Svensson L.A., Aevarsson A., Liljas A. EMBO J. 15:1350-1359(1996) [PubMed: 8635468] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS). Strain: VK1.
[6]	"A mutant form of the ribosomal protein L1 reveals conformational flexibility." Unge J., Al-Karadaghi S., Liljas A., Jonsson B.H., Eliseikina I., Ossina N., Nevskaya N., Fomenkova N., Garber M., Nikonov S. FEBS Lett. 411:53-59(1997) [PubMed: 9247141] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF MUTANT CYS-180.
[7]	"New insights into the interaction of ribosomal protein L1 with RNA." Nevskaya N., Tishchenko S., Volchkov S., Kljashtorny V., Nikonova E., Nikonov O., Nikulin A., Kohrer C., Piendl W., Zimmermann R., Stockley P., Garber M.B., Nikonov S. J. Mol. Biol. 355:747-759(2006) [PubMed: 16330048] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH A M.VANNIELII L1 MRNA FRAGMENT. Strain: VK1.
[8]	"Solution structure of the E. coli 70S ribosome at 11.5 A resolution." Gabashvili I.S., Agrawal R.K., Spahn C.M., Grassucci R.A., Svergun D.I., Frank J., Penczek P. Cell 100:537-549(2000) [PubMed: 10721991] [Abstract] Cited for: STRUCTURE BY ELECTRON MICROSCOPY (11.5 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X81375 Genomic DNA. Translation: CAA57139.1.

PIR

S66577.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AD2	X-ray	1.90	A	2-229	[»]
1EG0	electron microscopy	11.50	N	1-229	[»]
1ZHO	X-ray	2.60	A/C/E/G	2-229	[»]
2HW8	X-ray	2.10	A	2-228	[»]
2OUM	X-ray	2.55	A	2-229	[»]
2OV7	X-ray	2.30	A/B/C	2-229	[»]
2VPL	X-ray	2.30	A/C	2-229	[»]
487D	electron microscopy	7.50	H	6-229	[»]

ModBase

Search...

Family and domain databases

HAMAP

MF_01318.
[Tree]

InterPro

IPR005878. Ribosom_L1_bac-type.
IPR002143. Ribosomal_L1.
IPR016094. Ribosomal_L1_2-a/b-sand.
[Graphical view]

Gene3D

G3DSA:3.30.190.20. Ribosomal_L1_2-a/b-sand. 1 hit.

Pfam

PF00687. Ribosomal_L1. 1 hit.
[Graphical view]

PIRSF

PIRSF002155. Ribosomal_L1. 1 hit.

ProDom

PD001314. Ribosomal_L1. 1 hit.
[Graphical view] [Entries sharing at least one domain]

TIGRFAMs

TIGR01169. rplA_bact. 1 hit.

PROSITE

PS01199. RIBOSOMAL_L1. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

RL1_THETH

Accession

Primary (citable) accession number: P27150

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 76 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)