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P56029

- RL1_HELPY

UniProt

P56029 - RL1_HELPY

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Protein

50S ribosomal protein L1

Gene

rplA

Organism
Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

Binds directly to 23S rRNA. The L1 stalk is quite mobile in the ribosome, and is involved in E site tRNA release.UniRule annotation
Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA.UniRule annotation
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.

GO - Molecular functioni

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

GO - Biological processi

  1. defense response to bacterium Source: UniProtKB-KW
  2. regulation of translation Source: UniProtKB-KW
  3. translation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial, Repressor, Ribonucleoprotein, Ribosomal protein

Keywords - Biological processi

Translation regulation

Keywords - Ligandi

RNA-binding, rRNA-binding, tRNA-binding

Enzyme and pathway databases

BioCyciHPY:HP1201-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L1UniRule annotation
Gene namesi
Name:rplAUniRule annotation
Ordered Locus Names:HP_1201
OrganismiHelicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Taxonomic identifieri85962 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter
ProteomesiUP000000429: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. large ribosomal subunit Source: InterPro
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi17 – 193QND → WNW: Increases antibacterial and antifungal activities 2-4 fold without an increase in hemolytic activies. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 23423450S ribosomal protein L1PRO_0000125667Add
BLAST

Proteomic databases

PRIDEiP56029.

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit.

Protein-protein interaction databases

STRINGi85962.HP1201.

Structurei

Secondary structure

1
234
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 1813Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OT0NMR-A2-18[»]
1P0GNMR-A2-20[»]
1P0JNMR-A2-18[»]
1P0LNMR-A2-20[»]
1P0ONMR-A2-20[»]
1P5KNMR-A2-20[»]
1P5LNMR-A7-20[»]
ProteinModelPortaliP56029.
SMRiP56029. Positions 7-227.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP56029.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L1P family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0081.
KOiK02863.
OMAiAKITPIA.
OrthoDBiEOG6FBX2G.

Family and domain databases

Gene3Di3.30.190.20. 2 hits.
3.40.50.790. 1 hit.
HAMAPiMF_01318_B. Ribosomal_L1_B.
InterProiIPR005878. 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]
PfamiPF00687. Ribosomal_L1. 1 hit.
[Graphical view]
PIRSFiPIRSF002155. Ribosomal_L1. 1 hit.
SUPFAMiSSF56808. SSF56808. 1 hit.
TIGRFAMsiTIGR01169. rplA_bact. 1 hit.
PROSITEiPS01199. RIBOSOMAL_L1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P56029-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAKKVFKRLE KLFSKIQNDK AYGVEQGVEV VKSLASAKFD ETVEVALRLG
60 70 80 90 100
VDPRHADQMV RGAVVLPHGT GKKVRVAVFA KDIKQDEAKN AGADVVGGDD
110 120 130 140 150
LAEEIKNGRI DFDMVIATPD MMAVVGKVGR ILGPKGLMPN PKTGTVTMDI
160 170 180 190 200
AKAVSNAKSG QVNFRVDKKG NVHAPIGKAS FPEEKIKENM LELVKTINRL
210 220 230
KPSSAKGKYI RNAALSLTMS PSVSLDAQEL MDIK
Length:234
Mass (Da):25,266
Last modified:November 1, 1997 - v1
Checksum:iBC7CECDB6B0B0EA8
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti155 – 1551S → T in strain: Hp921023.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000511 Genomic DNA. Translation: AAD08247.1.
U86609 Genomic DNA. Translation: AAB47277.1.
PIRiA64670.
RefSeqiNP_207992.1. NC_000915.1.
YP_006935121.1. NC_018939.1.

Genome annotation databases

EnsemblBacteriaiAAD08247; AAD08247; HP_1201.
GeneIDi13870401.
899963.
KEGGiheo:C694_06215.
hpy:HP1201.
PATRICi20593761. VBIHelPyl33062_1258.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000511 Genomic DNA. Translation: AAD08247.1 .
U86609 Genomic DNA. Translation: AAB47277.1 .
PIRi A64670.
RefSeqi NP_207992.1. NC_000915.1.
YP_006935121.1. NC_018939.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1OT0 NMR - A 2-18 [» ]
1P0G NMR - A 2-20 [» ]
1P0J NMR - A 2-18 [» ]
1P0L NMR - A 2-20 [» ]
1P0O NMR - A 2-20 [» ]
1P5K NMR - A 2-20 [» ]
1P5L NMR - A 7-20 [» ]
ProteinModelPortali P56029.
SMRi P56029. Positions 7-227.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 85962.HP1201.

Proteomic databases

PRIDEi P56029.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAD08247 ; AAD08247 ; HP_1201 .
GeneIDi 13870401.
899963.
KEGGi heo:C694_06215.
hpy:HP1201.
PATRICi 20593761. VBIHelPyl33062_1258.

Phylogenomic databases

eggNOGi COG0081.
KOi K02863.
OMAi AKITPIA.
OrthoDBi EOG6FBX2G.

Enzyme and pathway databases

BioCyci HPY:HP1201-MONOMER.

Miscellaneous databases

EvolutionaryTracei P56029.

Family and domain databases

Gene3Di 3.30.190.20. 2 hits.
3.40.50.790. 1 hit.
HAMAPi MF_01318_B. Ribosomal_L1_B.
InterProi IPR005878. 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 ]
Pfami PF00687. Ribosomal_L1. 1 hit.
[Graphical view ]
PIRSFi PIRSF002155. Ribosomal_L1. 1 hit.
SUPFAMi SSF56808. SSF56808. 1 hit.
TIGRFAMsi TIGR01169. rplA_bact. 1 hit.
PROSITEi PS01199. RIBOSOMAL_L1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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. 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.

Entry informationi

Entry nameiRL1_HELPY
AccessioniPrimary (citable) accession number: P56029
Secondary accession number(s): P94849
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: October 29, 2014
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Helicobacter pylori
    Helicobacter pylori (strain 26695): entries and gene names
  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