50S ribosomal protein L27 - Escherichia coli (strain K12)

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P0A7L8 (RL27_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 86. History...

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

Documents (4) |

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 L27

Gene names

Name:	rpmA
Ordered Locus Names:	b3185, JW3152

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	85 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 23S rRNA. Cross-links to the A and P site tRNAs.
Sequence similarities	Belongs to the ribosomal protein L27P family.
Mass spectrometry	Molecular mass is 8993.5 Da from positions 2 - 85. Determined by MALDI. Ref.9

Ontologies

Keywords
Ligand	RNA-binding rRNA-binding tRNA-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: InterPro
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 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

Removed Ref.4

Chain

2 – 85

50S ribosomal protein L27 HAMAP-Rule MF_00539

PRO_0000181085

Secondary structure

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0A7L8 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: B43AAE180ABC23EA
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FASTA

9,124

        10         20         30         40         50         60 
MAHKKAGGST RNGRDSEAKR LGVKRFGGES VLAGSIIVRQ RGTKFHAGAN VGCGRDHTLF 

        70         80 
AKADGKVKFE VKGPKNRKFI SIEAE

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and nucleotide sequencing of the genes, rpIU and rpmA, for ribosomal proteins L21 and L27 of Escherichia coli." Jeong J.H., Kitakawa M.S., Isono S., Isono K. DNA Seq. 4:59-67(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]	"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.
[3]	"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.
[4]	"The primary structure of protein L27 from the peptidyl-tRNA binding site of Escherichia coli ribosomes." Chen R., Mende L., Arfsten U. FEBS Lett. 59:96-99(1975) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-85. Strain: K12.
[5]	"Protein-rRNA binding features and their structural and functional implications in ribosomes as determined by cross-linking studies." Urlaub H., Kruft V., Bischof O., Mueller E.-C., Wittmann-Liebold B. EMBO J. 14:4578-4588(1995) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 67-78, CROSS-LINKING TO RRNA. Strain: MRE-600.
[6]	"The use of 2-iminothiolane as an RNA-protein cross-linking agent in Escherichia coli ribosomes, and the localisation on 23S RNA of sites cross-linked to proteins L4, L6, L21, L23, L27 and L29." Wower I., Wower J., Meinke M., Brimacombe R. Nucleic Acids Res. 9:4285-4302(1981) [PubMed] [Europe PMC] [Abstract] Cited for: CROSS-LINKING TO 23S RRNA. Strain: MRE-600.
[7]	"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.
[8]	"Escherichia coli proteome analysis using the gene-protein database." VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C. Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY 2D-GEL.
[9]	"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.
[10]	"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.
[11]	"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

D13267 Genomic DNA. Translation: BAA02526.1.
U18997 Genomic DNA. Translation: AAA57986.1.
U00096 Genomic DNA. Translation: AAC76217.1.
AP009048 Genomic DNA. Translation: BAE77229.1.

PIR

R5EC27. JS0767.

RefSeq

NP_417652.1. NC_000913.2.
YP_491370.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1P85	electron microscopy	12.30	U	2-85	[»]
1P86	electron microscopy	11.50	U	2-85	[»]
1VS6	X-ray	3.46	W	1-85	[»]
1VS8	X-ray	3.46	W	1-85	[»]
1VT2	X-ray	3.30	W	1-85	[»]
2AW4	X-ray	3.46	W	2-85	[»]
2AWB	X-ray	3.46	W	2-85	[»]
2GYA	electron microscopy	15.00	U	2-84	[»]
2GYC	electron microscopy	15.00	U	2-85	[»]
2I2T	X-ray	3.22	W	2-84	[»]
2I2V	X-ray	3.22	W	2-84	[»]
2J28	electron microscopy	8.00	W	2-85	[»]
2QAM	X-ray	3.21	W	2-85	[»]
2QAO	X-ray	3.21	W	2-85	[»]
2QBA	X-ray	3.54	W	2-85	[»]
2QBC	X-ray	3.54	W	2-85	[»]
2QBE	X-ray	3.30	W	2-85	[»]
2QBG	X-ray	3.30	W	2-85	[»]
2QBI	X-ray	4.00	W	2-85	[»]
2QBK	X-ray	4.00	W	2-85	[»]
2QOV	X-ray	3.93	W	2-85	[»]
2QOX	X-ray	3.93	W	2-85	[»]
2QOZ	X-ray	3.50	W	2-85	[»]
2QP1	X-ray	3.50	W	2-85	[»]
2RDO	electron microscopy	9.10	W	2-85	[»]
2VHM	X-ray	3.74	W	2-85	[»]
2VHN	X-ray	3.74	W	2-85	[»]
2WWQ	electron microscopy	5.80	Y	7-85	[»]
2Z4L	X-ray	4.45	W	2-85	[»]
2Z4N	X-ray	4.45	W	2-85	[»]
3BBX	electron microscopy	10.00	W	2-85	[»]
3DF2	X-ray	3.50	W	2-84	[»]
3DF4	X-ray	3.50	W	2-84	[»]
3E1B	electron microscopy	-	P	1-85	[»]
3E1D	electron microscopy	-	P	1-85	[»]
3FIK	electron microscopy	6.70	W	7-85	[»]
3I1N	X-ray	3.19	W	1-85	[»]
3I1P	X-ray	3.19	W	1-85	[»]
3I1R	X-ray	3.81	W	1-85	[»]
3I1T	X-ray	3.81	W	1-85	[»]
3I20	X-ray	3.71	W	1-85	[»]
3I22	X-ray	3.71	W	1-85	[»]
3IZT	electron microscopy	-	X	1-85	[»]
3IZU	electron microscopy	-	X	1-85	[»]
3J01	electron microscopy	-	W	2-85	[»]
3J0T	electron microscopy	12.10	Y	2-84	[»]
3J0W	electron microscopy	14.70	Y	2-84	[»]
3J0Y	electron microscopy	13.50	Y	2-84	[»]
3J11	electron microscopy	13.10	Y	2-84	[»]
3J12	electron microscopy	11.50	Y	2-84	[»]
3J14	electron microscopy	11.50	Y	2-84	[»]
3J19	electron microscopy	8.30	W	10-85	[»]
3J37	electron microscopy	9.80	0	2-85	[»]
3KCR	electron microscopy	-	W	1-85	[»]
3OAS	X-ray	3.25	W	7-85	[»]
3OAT	X-ray	3.25	W	7-85	[»]
3OFC	X-ray	3.19	W	7-85	[»]
3OFD	X-ray	3.19	W	7-85	[»]
3OFQ	X-ray	3.10	W	7-85	[»]
3OFR	X-ray	3.10	W	7-85	[»]
3OFZ	X-ray	3.29	W	7-85	[»]
3OG0	X-ray	3.29	W	7-85	[»]
3ORB	X-ray	3.30	W	1-85	[»]
3R8S	X-ray	3.00	W	10-85	[»]
3R8T	X-ray	3.00	W	11-85	[»]
3SGF	X-ray	3.20	0	1-85	[»]
3UOS	X-ray	3.70	0	1-85	[»]
4GAR	X-ray	3.30	W	1-85	[»]
4GAU	X-ray	3.30	W	1-85	[»]

ProteinModelPortal

P0A7L8.

SMR

P0A7L8. Positions 2-85.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-47933N.

IntAct

P0A7L8. 22 interactions.

MINT

MINT-1317488.

STRING

511145.b3185.

Proteomic databases

PaxDb

P0A7L8.

PRIDE

P0A7L8.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76217; AAC76217; b3185.
BAE77229; BAE77229; BAE77229.

GeneID

12932199.
945190.

KEGG

ecj:Y75_p3105.
eco:b3185.

PATRIC

32121790. VBIEscCol129921_3279.

Organism-specific databases

EchoBASE

EB4296.

EcoGene

EG50002. rpmA.

Phylogenomic databases

eggNOG

COG0211.

HOGENOM

HOG000111610.

K02899.

OMA

DGIVKFE.

ProtClustDB

PRK05435.

Enzyme and pathway databases

BioCyc

EcoCyc:EG50002-MONOMER.
ECOL316407:JW3152-MONOMER.

Gene expression databases

Genevestigator

P0A7L8.

Family and domain databases

HAMAP

MF_00539. Ribosomal_L27.

InterPro

IPR001684. Ribosomal_L27.
IPR018261. Ribosomal_L27_CS.
[Graphical view]

PANTHER

PTHR15893. PTHR15893. 1 hit.

Pfam

PF01016. Ribosomal_L27. 1 hit.
[Graphical view]

PRINTS

PR00063. RIBOSOMALL27.

ProDom

PD003114. Ribosomal_L27. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SUPFAM

SSF110324. Ribosomal_L27. 1 hit.

TIGRFAMs

TIGR00062. L27. 1 hit.

PROSITE

PS00831. RIBOSOMAL_L27. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0A7L8.

Entry information

Entry name

RL27_ECOLI

Accession

Primary (citable) accession number: P0A7L8
Secondary accession number(s): P02427, Q2M927

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 86 of the entry and version 2 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

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

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

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents