P0A7N9 (RL33_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
50S ribosomal protein L33

Gene names

Name:	rpmG
Ordered Locus Names:	b3636, JW3611

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	55 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)

Subunit structure	Part of the 50S ribosomal subunit. Cross-links to the P and E site tRNAs.
Miscellaneous	Surface exposed on the 50S subunit. HAMAP-Rule MF_00294
Sequence similarities	Belongs to the ribosomal protein L33P family.
Mass spectrometry	Molecular mass is 6254.1 Da from positions 2 - 55. Determined by MALDI. Ref.7

Ontologies

Keywords
Ligand	RNA-binding tRNA-binding
Molecular function	Ribonucleoprotein Ribosomal protein
PTM	Methylation
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	ribosome Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	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.5

Chain

2 – 55

54

50S ribosomal protein L33 HAMAP-Rule MF_00294

PRO_0000170158

Amino acid modifications

Modified residue

2

1

N-methylalanine HAMAP-Rule MF_00294

Experimental info

Sequence conflict

48 – 49

2

IY → YI AA sequence Ref.5

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

55

Helix Strand Turn

Details...

Beta strand

7 – 17

11

Beta strand

20 – 25

6

Helix

27 – 29

3

Beta strand

36 – 40

5

Turn

41 – 44

4

Beta strand

45 – 50

6

Sequences

	Sequence		Length	Mass (Da)
	P0A7N9 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 31681CC3DAC0C5D6	FASTA	55	6,372
	10 20 30 40 50 MAKGIREKIK LVSSAGTGHF YTTTKNKRTK PEKLELKKFD PVVRQHVIYK EAKIK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and the nucleotide sequence of the genes for Escherichia coli ribosomal proteins L28 (rpmB) and L33 (rpmG)." Lee J.S., An G., Friesen J.D., Isono K. Mol. Gen. Genet. 184:218-223(1981) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication." Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R. Genomics 16:551-561(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Primary structure of protein L33 from the large subunit of the Escherichia coli ribosome." Wittmann-Liebold B., Pannenbecker R. FEBS Lett. 68:115-118(1976) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-55. Strain: K.
[6]	"The ribosomal neighbourhood of the central fold of tRNA: cross-links from position 47 of tRNA located at the A, P or E site." Osswald M., Doering T., Brimacombe R. Nucleic Acids Res. 23:4635-4641(1995) [PubMed] [Europe PMC] [Abstract] Cited for: CROSS-LINKING TO THE TRNA CENTRAL FOLD. Strain: MRE-600.
[7]	"Observation of Escherichia coli ribosomal proteins and their posttranslational modifications by mass spectrometry." Arnold R.J., Reilly J.P. Anal. Biochem. 269:105-112(1999) [PubMed] [Europe PMC] [Abstract] Cited for: MASS SPECTROMETRY. Strain: K12 / ATCC 25404 / DSM 5698 / NCIMB 11290.
[8]	"Study of the structural dynamics of the E. coli 70S ribosome using real-space refinement." Gao H., Sengupta J., Valle M., Korostelev A., Eswar N., Stagg S.M., Van Roey P., Agrawal R.K., Harvey S.C., Sali A., Chapman M.S., Frank J. Cell 113:789-801(2003) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY ELECTRON MICROSCOPY (11.50 ANGSTROMS). Strain: MRE-600.
[9]	"Structures of the bacterial ribosome at 3.5 A resolution." Schuwirth B.S., Borovinskaya M.A., Hau C.W., Zhang W., Vila-Sanjurjo A., Holton J.M., Cate J.H.D. Science 310:827-834(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES. Strain: MRE-600.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J01677 Genomic DNA. Translation: AAA74100.1.
L10328 Genomic DNA. Translation: AAA61989.1.
U00096 Genomic DNA. Translation: AAC76660.1.
AP009048 Genomic DNA. Translation: BAE77656.1.

PIR

R5EC33. S42444.

RefSeq

NP_418093.1. NC_000913.2.
YP_491797.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1P85	electron microscopy	12.30	1	2-55	[»]
1P86	electron microscopy	11.50	1	2-55	[»]
1VS6	X-ray	3.46	1	1-55	[»]
1VS8	X-ray	3.46	1	1-55	[»]
1VT2	X-ray	3.30	1	1-55	[»]
2AW4	X-ray	3.46	1	2-55	[»]
2AWB	X-ray	3.46	1	2-55	[»]
2GYA	electron microscopy	15.00	1	2-52	[»]
2GYC	electron microscopy	15.00	1	2-53	[»]
2I2T	X-ray	3.22	1	2-54	[»]
2I2V	X-ray	3.22	1	2-54	[»]
2J28	electron microscopy	8.00	1	2-55	[»]
2QAM	X-ray	3.21	1	2-55	[»]
2QAO	X-ray	3.21	1	2-55	[»]
2QBA	X-ray	3.54	1	2-55	[»]
2QBC	X-ray	3.54	1	2-55	[»]
2QBE	X-ray	3.30	1	2-55	[»]
2QBG	X-ray	3.30	1	2-55	[»]
2QBI	X-ray	4.00	1	2-55	[»]
2QBK	X-ray	4.00	1	2-55	[»]
2QOV	X-ray	3.93	1	2-55	[»]
2QOX	X-ray	3.93	1	2-55	[»]
2QOZ	X-ray	3.50	1	2-55	[»]
2QP1	X-ray	3.50	1	2-55	[»]
2RDO	electron microscopy	9.10	1	2-55	[»]
2VHM	X-ray	3.74	1	2-55	[»]
2VHN	X-ray	3.74	1	2-55	[»]
2WWQ	electron microscopy	5.80	4	4-53	[»]
2Z4L	X-ray	4.45	1	2-55	[»]
2Z4N	X-ray	4.45	1	2-55	[»]
3BBX	electron microscopy	10.00	1	2-55	[»]
3DF2	X-ray	3.50	1	2-54	[»]
3DF4	X-ray	3.50	1	2-54	[»]
3E1B	electron microscopy	-	U	2-55	[»]
3E1D	electron microscopy	-	U	2-55	[»]
3FIK	electron microscopy	6.70	1	4-53	[»]
3I1N	X-ray	3.19	1	1-55	[»]
3I1P	X-ray	3.19	1	1-55	[»]
3I1R	X-ray	3.81	1	1-55	[»]
3I1T	X-ray	3.81	1	1-55	[»]
3I20	X-ray	3.71	1	1-55	[»]
3I22	X-ray	3.71	1	1-55	[»]
3IZT	electron microscopy	-	d	1-55	[»]
3IZU	electron microscopy	-	d	1-55	[»]
3J01	electron microscopy	-	1	2-55	[»]
3J0T	electron microscopy	12.10	4	2-54	[»]
3J0W	electron microscopy	14.70	4	2-54	[»]
3J0Y	electron microscopy	13.50	4	2-54	[»]
3J11	electron microscopy	13.10	4	2-54	[»]
3J12	electron microscopy	11.50	4	2-54	[»]
3J14	electron microscopy	11.50	4	2-54	[»]
3J19	electron microscopy	8.30	1	4-53	[»]
3KCR	electron microscopy	-	1	1-55	[»]
3OAS	X-ray	3.25	1	4-53	[»]
3OAT	X-ray	3.25	1	4-53	[»]
3OFC	X-ray	3.19	1	4-53	[»]
3OFD	X-ray	3.19	1	4-53	[»]
3OFQ	X-ray	3.10	1	4-53	[»]
3OFR	X-ray	3.10	1	4-53	[»]
3OFZ	X-ray	3.29	1	4-53	[»]
3OG0	X-ray	3.29	1	4-53	[»]
3ORB	X-ray	3.30	1	1-55	[»]
3R8S	X-ray	3.00	1	4-53	[»]
3R8T	X-ray	3.00	1	4-53	[»]
3SGF	X-ray	3.20	5	1-55	[»]
3UOS	X-ray	3.70	5	1-55	[»]
4GAR	X-ray	3.30	1	1-55	[»]
4GAU	X-ray	3.30	1	1-55	[»]

ProteinModelPortal

P0A7N9.

SMR

P0A7N9. Positions 2-53.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-35968N.

IntAct

P0A7N9. 53 interactions.

MINT

MINT-1234559.

STRING

511145.b3636.

Proteomic databases

PaxDb

P0A7N9.

PRIDE

P0A7N9.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76660; AAC76660; b3636.
BAE77656; BAE77656; BAE77656.

GeneID

12931828.
946318.

KEGG

ecj:Y75_p3538.
eco:b3636.

PATRIC

32122759. VBIEscCol129921_3756.

Organism-specific databases

EchoBASE

EB0884.

EcoGene

EG10891. rpmG.

Phylogenomic databases

eggNOG

COG0267.

HOGENOM

HOG000004839.

KO

K02913.

OMA

MYKETKL.

ProtClustDB

PRK00595.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10891-MONOMER.
ECOL316407:JW3611-MONOMER.

Gene expression databases

Genevestigator

P0A7N9.

Family and domain databases

HAMAP

MF_00294. Ribosomal_L33.

InterPro

IPR001705. Ribosomal_L33.
IPR018264. Ribosomal_L33_CS.
IPR011332. Ribosomal_zn-bd_dom.
[Graphical view]

Pfam

PF00471. Ribosomal_L33. 1 hit.
[Graphical view]

SUPFAM

SSF57829. Ribosomal_zn-bd. 1 hit.

TIGRFAMs

TIGR01023. rpmG_bact. 1 hit.

PROSITE

PS00582. RIBOSOMAL_L33. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0A7N9.

Entry information

Entry name

RL33_ECOLI

Accession

Primary (citable) accession number: P0A7N9
Secondary accession number(s): P02436, Q2M7V0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 84 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program