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Protein

50S ribosomal protein L27

Gene

rpmA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  1. rRNA binding Source: UniProtKB-KW
  2. structural constituent of ribosome Source: InterPro
  3. tRNA binding Source: UniProtKB-KW

GO - Biological processi

  1. translation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding, tRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG50002-MONOMER.
ECOL316407:JW3152-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L27
Gene namesi
Name:rpmA
Ordered Locus Names:b3185, JW3152
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG50002. rpmA.

Subcellular locationi

GO - Cellular componenti

  1. cytosolic large ribosomal subunit Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 858450S ribosomal protein L27PRO_0000181085Add
BLAST

Proteomic databases

PaxDbiP0A7L8.
PRIDEiP0A7L8.

Expressioni

Gene expression databases

GenevestigatoriP0A7L8.

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit, cross-links to the 23S rRNA. Cross-links to the A and P site tRNAs.

Binary interactionsi

WithEntry#Exp.IntActNotes
mqsAQ468642EBI-546875,EBI-1120353

Protein-protein interaction databases

BioGridi849576. 1 interaction.
DIPiDIP-47933N.
IntActiP0A7L8. 26 interactions.
MINTiMINT-1317488.
STRINGi511145.b3185.

Structurei

Secondary structure

1
85
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi22 – 254Combined sources
Beta strandi36 – 394Combined sources
Beta strandi44 – 474Combined sources
Helixi48 – 503Combined sources
Beta strandi51 – 533Combined sources
Beta strandi55 – 573Combined sources
Beta strandi59 – 7214Combined sources
Turni73 – 764Combined sources
Beta strandi77 – 837Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2J28electron microscopy8.00W2-85[»]
2RDOelectron microscopy9.10W2-85[»]
3BBXelectron microscopy10.00W2-85[»]
3J5Lelectron microscopy6.60W7-85[»]
3J7Zelectron microscopy3.90W1-85[»]
4CSUelectron microscopy5.50Y2-85[»]
4U1UX-ray2.95W10-85[»]
4U1VX-ray3.00W10-85[»]
4U20X-ray2.90W10-85[»]
4U24X-ray2.90W10-85[»]
4U25X-ray2.90W10-85[»]
4U26X-ray2.80W10-85[»]
4U27X-ray2.80W10-85[»]
4V47electron microscopy12.30U2-85[»]
4V48electron microscopy11.50U2-85[»]
4V4HX-ray3.46W1-85[»]
4V4QX-ray3.46W2-85[»]
4V4Velectron microscopy15.00U2-85[»]
4V4Welectron microscopy15.00U2-85[»]
4V50X-ray3.22W2-85[»]
4V52X-ray3.21W2-85[»]
4V53X-ray3.54W2-85[»]
4V54X-ray3.30W2-85[»]
4V55X-ray4.00W2-85[»]
4V56X-ray3.93W2-85[»]
4V57X-ray3.50W2-85[»]
4V5BX-ray3.74W2-85[»]
4V5Helectron microscopy5.80Y7-85[»]
4V5YX-ray4.45W2-85[»]
4V64X-ray3.50W2-84[»]
4V65electron microscopy-P1-85[»]
4V66electron microscopy-P1-85[»]
4V69electron microscopy6.70W7-85[»]
4V6CX-ray3.19W1-85[»]
4V6DX-ray3.81W1-85[»]
4V6EX-ray3.71W1-85[»]
4V6Kelectron microscopy-X1-85[»]
4V6Lelectron microscopy-X1-85[»]
4V6Melectron microscopy-W2-85[»]
4V6Nelectron microscopy12.10Y2-85[»]
4V6Oelectron microscopy14.70Y2-85[»]
4V6Pelectron microscopy13.50Y2-85[»]
4V6Qelectron microscopy11.50Y2-85[»]
4V6Relectron microscopy11.50Y2-85[»]
4V6Selectron microscopy13.10Y2-85[»]
4V6Telectron microscopy8.30W10-85[»]
4V6Velectron microscopy9.8002-85[»]
4V6Yelectron microscopy12.00W7-85[»]
4V6Zelectron microscopy12.00W7-85[»]
4V70electron microscopy17.00W7-85[»]
4V71electron microscopy20.00W7-85[»]
4V72electron microscopy13.00W7-85[»]
4V73electron microscopy15.00W7-85[»]
4V74electron microscopy17.00W7-85[»]
4V75electron microscopy12.00W7-85[»]
4V76electron microscopy17.00W7-85[»]
4V77electron microscopy17.00W7-85[»]
4V78electron microscopy20.00W7-85[»]
4V79electron microscopy15.00W7-85[»]
4V7Aelectron microscopy9.00W7-85[»]
4V7Belectron microscopy6.80W1-85[»]
4V7Celectron microscopy7.60Y2-85[»]
4V7Delectron microscopy7.60Z2-85[»]
4V7Ielectron microscopy-W1-85[»]
4V7SX-ray3.25W7-85[»]
4V7TX-ray3.19W7-85[»]
4V7UX-ray3.10W7-85[»]
4V7VX-ray3.29W7-85[»]
4V85X-ray3.2001-85[»]
4V89X-ray3.7001-85[»]
4V9CX-ray3.30W1-85[»]
4V9DX-ray3.00W11-85[»]
4V9OX-ray2.90W1-85[»]
4V9PX-ray2.90W1-85[»]
4WF1X-ray3.09W10-85[»]
4WWWX-ray3.30W1-85[»]
DisProtiDP00140.
ProteinModelPortaliP0A7L8.
SMRiP0A7L8. Positions 2-85.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7L8.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L27P family.Curated

Phylogenomic databases

eggNOGiCOG0211.
HOGENOMiHOG000111610.
InParanoidiP0A7L8.
KOiK02899.
OMAiKDHTLHA.
OrthoDBiEOG6N94H6.
PhylomeDBiP0A7L8.

Family and domain databases

HAMAPiMF_00539. Ribosomal_L27.
InterProiIPR001684. Ribosomal_L27.
IPR018261. Ribosomal_L27_CS.
[Graphical view]
PANTHERiPTHR15893. PTHR15893. 1 hit.
PfamiPF01016. Ribosomal_L27. 1 hit.
[Graphical view]
PRINTSiPR00063. RIBOSOMALL27.
ProDomiPD003114. Ribosomal_L27. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsiTIGR00062. L27. 1 hit.
PROSITEiPS00831. RIBOSOMAL_L27. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0A7L8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAHKKAGGST RNGRDSEAKR LGVKRFGGES VLAGSIIVRQ RGTKFHAGAN
60 70 80
VGCGRDHTLF AKADGKVKFE VKGPKNRKFI SIEAE
Length:85
Mass (Da):9,124
Last modified:January 23, 2007 - v2
Checksum:iB43AAE180ABC23EA
GO

Mass spectrometryi

Molecular mass is 8993.5 Da from positions 2 - 85. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13267 Genomic DNA. Translation: BAA02526.1.
U18997 Genomic DNA. Translation: AAA57986.1.
U00096 Genomic DNA. Translation: AAC76217.1.
AP009048 Genomic DNA. Translation: BAE77229.1.
PIRiJS0767. R5EC27.
RefSeqiNP_417652.1. NC_000913.3.
YP_491370.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76217; AAC76217; b3185.
BAE77229; BAE77229; BAE77229.
GeneIDi12932199.
945190.
KEGGiecj:Y75_p3105.
eco:b3185.
PATRICi32121790. VBIEscCol129921_3279.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13267 Genomic DNA. Translation: BAA02526.1.
U18997 Genomic DNA. Translation: AAA57986.1.
U00096 Genomic DNA. Translation: AAC76217.1.
AP009048 Genomic DNA. Translation: BAE77229.1.
PIRiJS0767. R5EC27.
RefSeqiNP_417652.1. NC_000913.3.
YP_491370.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2J28electron microscopy8.00W2-85[»]
2RDOelectron microscopy9.10W2-85[»]
3BBXelectron microscopy10.00W2-85[»]
3J5Lelectron microscopy6.60W7-85[»]
3J7Zelectron microscopy3.90W1-85[»]
4CSUelectron microscopy5.50Y2-85[»]
4U1UX-ray2.95W10-85[»]
4U1VX-ray3.00W10-85[»]
4U20X-ray2.90W10-85[»]
4U24X-ray2.90W10-85[»]
4U25X-ray2.90W10-85[»]
4U26X-ray2.80W10-85[»]
4U27X-ray2.80W10-85[»]
4V47electron microscopy12.30U2-85[»]
4V48electron microscopy11.50U2-85[»]
4V4HX-ray3.46W1-85[»]
4V4QX-ray3.46W2-85[»]
4V4Velectron microscopy15.00U2-85[»]
4V4Welectron microscopy15.00U2-85[»]
4V50X-ray3.22W2-85[»]
4V52X-ray3.21W2-85[»]
4V53X-ray3.54W2-85[»]
4V54X-ray3.30W2-85[»]
4V55X-ray4.00W2-85[»]
4V56X-ray3.93W2-85[»]
4V57X-ray3.50W2-85[»]
4V5BX-ray3.74W2-85[»]
4V5Helectron microscopy5.80Y7-85[»]
4V5YX-ray4.45W2-85[»]
4V64X-ray3.50W2-84[»]
4V65electron microscopy-P1-85[»]
4V66electron microscopy-P1-85[»]
4V69electron microscopy6.70W7-85[»]
4V6CX-ray3.19W1-85[»]
4V6DX-ray3.81W1-85[»]
4V6EX-ray3.71W1-85[»]
4V6Kelectron microscopy-X1-85[»]
4V6Lelectron microscopy-X1-85[»]
4V6Melectron microscopy-W2-85[»]
4V6Nelectron microscopy12.10Y2-85[»]
4V6Oelectron microscopy14.70Y2-85[»]
4V6Pelectron microscopy13.50Y2-85[»]
4V6Qelectron microscopy11.50Y2-85[»]
4V6Relectron microscopy11.50Y2-85[»]
4V6Selectron microscopy13.10Y2-85[»]
4V6Telectron microscopy8.30W10-85[»]
4V6Velectron microscopy9.8002-85[»]
4V6Yelectron microscopy12.00W7-85[»]
4V6Zelectron microscopy12.00W7-85[»]
4V70electron microscopy17.00W7-85[»]
4V71electron microscopy20.00W7-85[»]
4V72electron microscopy13.00W7-85[»]
4V73electron microscopy15.00W7-85[»]
4V74electron microscopy17.00W7-85[»]
4V75electron microscopy12.00W7-85[»]
4V76electron microscopy17.00W7-85[»]
4V77electron microscopy17.00W7-85[»]
4V78electron microscopy20.00W7-85[»]
4V79electron microscopy15.00W7-85[»]
4V7Aelectron microscopy9.00W7-85[»]
4V7Belectron microscopy6.80W1-85[»]
4V7Celectron microscopy7.60Y2-85[»]
4V7Delectron microscopy7.60Z2-85[»]
4V7Ielectron microscopy-W1-85[»]
4V7SX-ray3.25W7-85[»]
4V7TX-ray3.19W7-85[»]
4V7UX-ray3.10W7-85[»]
4V7VX-ray3.29W7-85[»]
4V85X-ray3.2001-85[»]
4V89X-ray3.7001-85[»]
4V9CX-ray3.30W1-85[»]
4V9DX-ray3.00W11-85[»]
4V9OX-ray2.90W1-85[»]
4V9PX-ray2.90W1-85[»]
4WF1X-ray3.09W10-85[»]
4WWWX-ray3.30W1-85[»]
DisProtiDP00140.
ProteinModelPortaliP0A7L8.
SMRiP0A7L8. Positions 2-85.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi849576. 1 interaction.
DIPiDIP-47933N.
IntActiP0A7L8. 26 interactions.
MINTiMINT-1317488.
STRINGi511145.b3185.

Chemistry

ChEMBLiCHEMBL2363135.

Proteomic databases

PaxDbiP0A7L8.
PRIDEiP0A7L8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76217; AAC76217; b3185.
BAE77229; BAE77229; BAE77229.
GeneIDi12932199.
945190.
KEGGiecj:Y75_p3105.
eco:b3185.
PATRICi32121790. VBIEscCol129921_3279.

Organism-specific databases

EchoBASEiEB4296.
EcoGeneiEG50002. rpmA.

Phylogenomic databases

eggNOGiCOG0211.
HOGENOMiHOG000111610.
InParanoidiP0A7L8.
KOiK02899.
OMAiKDHTLHA.
OrthoDBiEOG6N94H6.
PhylomeDBiP0A7L8.

Enzyme and pathway databases

BioCyciEcoCyc:EG50002-MONOMER.
ECOL316407:JW3152-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A7L8.
PROiP0A7L8.

Gene expression databases

GenevestigatoriP0A7L8.

Family and domain databases

HAMAPiMF_00539. Ribosomal_L27.
InterProiIPR001684. Ribosomal_L27.
IPR018261. Ribosomal_L27_CS.
[Graphical view]
PANTHERiPTHR15893. PTHR15893. 1 hit.
PfamiPF01016. Ribosomal_L27. 1 hit.
[Graphical view]
PRINTSiPR00063. RIBOSOMALL27.
ProDomiPD003114. Ribosomal_L27. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsiTIGR00062. L27. 1 hit.
PROSITEiPS00831. RIBOSOMAL_L27. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
    Strain: MRE-600.

Entry informationi

Entry nameiRL27_ECOLI
AccessioniPrimary (citable) accession number: P0A7L8
Secondary accession number(s): P02427, Q2M927
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: March 4, 2015
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Ribosomal proteins
    Ribosomal proteins families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.