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P56029 (RL1_HELPY) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
50S ribosomal protein L1
Gene names
Name:rplA
Ordered Locus Names:HP_1201
OrganismHelicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori) [Reference proteome] [HAMAP]
Taxonomic identifier85962 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter

Protein attributes

Sequence length234 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds directly to 23S rRNA. The L1 stalk is quite mobile in the ribosome, and is involved in E site tRNA release By similarity. HAMAP-Rule MF_01318

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

Peptides originating from the N-terminal end of L1 have antibacterial activity against bacteria such as E.coli and B.megaterium and modest antifungal activities. Has no effect on H.pylori itself. Peptides are not hemolytic against mammalian cells. These peptides may be released in the stomach during altruistic lysis to kill other fast growing bacteria. HAMAP-Rule MF_01318

Subunit structure

Part of the 50S ribosomal subunit.

Miscellaneous

The antimicrobial peptide HP (2-20) forms a short alpha-helix. Increasing the amphiphilicity of the helix increases its antimicrobial activities.

Sequence similarities

Belongs to the ribosomal protein L1P family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 23423450S ribosomal protein L1 HAMAP-Rule MF_01318
PRO_0000125667

Natural variations

Natural variant1551S → T in strain: Hp921023.

Experimental info

Mutagenesis17 – 193QND → WNW: Increases antibacterial and antifungal activities 2-4 fold without an increase in hemolytic activies. Ref.5

Secondary structure

... 234
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P56029 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: BC7CECDB6B0B0EA8

FASTA23425,266
        10         20         30         40         50         60 
MAKKVFKRLE KLFSKIQNDK AYGVEQGVEV VKSLASAKFD ETVEVALRLG VDPRHADQMV 

        70         80         90        100        110        120 
RGAVVLPHGT GKKVRVAVFA KDIKQDEAKN AGADVVGGDD LAEEIKNGRI DFDMVIATPD 

       130        140        150        160        170        180 
MMAVVGKVGR ILGPKGLMPN PKTGTVTMDI AKAVSNAKSG QVNFRVDKKG NVHAPIGKAS 

       190        200        210        220        230 
FPEEKIKENM LELVKTINRL KPSSAKGKYI RNAALSLTMS PSVSLDAQEL MDIK 

« Hide

References

« Hide 'large scale' references
[1]"The complete genome sequence of the gastric pathogen Helicobacter pylori."
Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G., Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A., Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N., Loftus B.J., Richardson D.L., Dodson R.J. expand/collapse author list , Khalak H.G., Glodek A., McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E., Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D., Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S., Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.
Nature 388:539-547(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700392 / 26695.
[2]"Isolation of recombinant protective Helicobacter pylori antigens."
Hocking D., Webb E., Radcliff F., Rothel L., Taylor S., Pinczower G., Kapouleas C., Braley H., Lee A., Doidge C.
Infect. Immun. 67:4713-4719(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 57-234.
Strain: Hp921023.
[3]"Antibacterial peptide from H. pylori."
Putsep K., Branden C.I., Boman H.G., Normark S.
Nature 398:671-672(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: SYNTHESIS, ANTIBACTERIAL ACTIVITY OF 2-20 AND 22-38.
[4]"Structure of antimicrobial peptide, HP (2-20) and its analogues derived from Helicobacter pylori, as determined by 1H NMR spectroscopy."
Lee K.H., Lee D.G., Park Y., Hahm K.-S., Kim Y.
Submitted (SEP-2004) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 2-20.
[5]"Interactions between the plasma membrane and the antimicrobial peptide HP (2-20) and its analogues derived from Helicobacter pylori."
Lee K.H., Lee D.G., Park Y., Kang D.-I., Shin S.Y., Hahm K.-S., Kim Y.
Biochem. J. 394:105-114(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 2-20, ANTIFUNGAL ACTIVITY, LYSIS MECHANISM, MUTAGENESIS OF 17-GLN--ASP-19.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000511 Genomic DNA. Translation: AAD08247.1.
U86609 Genomic DNA. Translation: AAB47277.1.
PIRA64670.
RefSeqNP_207992.1. NC_000915.1.
YP_006935121.1. NC_018939.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1OT0NMR-A2-18[»]
1P0GNMR-A2-20[»]
1P0JNMR-A2-18[»]
1P0LNMR-A2-20[»]
1P0ONMR-A2-20[»]
1P5KNMR-A2-20[»]
1P5LNMR-A7-20[»]
ProteinModelPortalP56029.
SMRP56029. Positions 7-227.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING85962.HP1201.

Proteomic databases

PRIDEP56029.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAD08247; AAD08247; HP_1201.
GeneID899963.
KEGGheo:C694_06215.
hpy:HP1201.
PATRIC20593761. VBIHelPyl33062_1258.

Phylogenomic databases

eggNOGCOG0081.
KOK02863.
OMAAKITPIA.
OrthoDBEOG6FBX2G.

Enzyme and pathway databases

BioCycHPY:HP1201-MONOMER.

Family and domain databases

Gene3D3.30.190.20. 2 hits.
3.40.50.790. 1 hit.
HAMAPMF_01318_B. Ribosomal_L1_B.
InterProIPR005878. Ribosom_L1_bac-type.
IPR002143. Ribosomal_L1.
IPR023674. Ribosomal_L1-like.
IPR028364. Ribosomal_L1/biogenesis.
IPR016094. Ribosomal_L1_2-a/b-sand.
IPR016095. Ribosomal_L1_3-a/b-sand.
IPR023673. Ribosomal_L1_CS.
[Graphical view]
PfamPF00687. Ribosomal_L1. 1 hit.
[Graphical view]
PIRSFPIRSF002155. Ribosomal_L1. 1 hit.
SUPFAMSSF56808. SSF56808. 1 hit.
TIGRFAMsTIGR01169. rplA_bact. 1 hit.
PROSITEPS01199. RIBOSOMAL_L1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP56029.

Entry information

Entry nameRL1_HELPY
AccessionPrimary (citable) accession number: P56029
Secondary accession number(s): P94849
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: July 9, 2014
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Ribosomal proteins

Ribosomal proteins families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Helicobacter pylori

Helicobacter pylori (strain 26695): entries and gene names