RL1_HELPY
ID RL1_HELPY Reviewed; 234 AA.
AC P56029; P94849;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 127.
DE RecName: Full=50S ribosomal protein L1 {ECO:0000255|HAMAP-Rule:MF_01318};
GN Name=rplA {ECO:0000255|HAMAP-Rule:MF_01318}; OrderedLocusNames=HP_1201;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 57-234.
RC STRAIN=Hp921023;
RX PubMed=10456921; DOI=10.1128/iai.67.9.4713-4719.1999;
RA Hocking D., Webb E., Radcliff F., Rothel L., Taylor S., Pinczower G.,
RA Kapouleas C., Braley H., Lee A., Doidge C.;
RT "Isolation of recombinant protective Helicobacter pylori antigens.";
RL Infect. Immun. 67:4713-4719(1999).
RN [3]
RP SYNTHESIS, AND ANTIBACTERIAL ACTIVITY OF 2-20 AND 22-38.
RX PubMed=10227288; DOI=10.1038/19439;
RA Putsep K., Branden C.I., Boman H.G., Normark S.;
RT "Antibacterial peptide from H. pylori.";
RL Nature 398:671-672(1999).
RN [4]
RP STRUCTURE BY NMR OF 2-20.
RA Lee K.H., Lee D.G., Park Y., Hahm K.-S., Kim Y.;
RT "Structure of antimicrobial peptide, HP (2-20) and its analogues derived
RT from Helicobacter pylori, as determined by 1H NMR spectroscopy.";
RL Submitted (SEP-2004) to the PDB data bank.
RN [5]
RP STRUCTURE BY NMR OF 2-20, ANTIFUNGAL ACTIVITY, LYSIS MECHANISM, AND
RP MUTAGENESIS OF 17-GLN--ASP-19.
RX PubMed=16255716; DOI=10.1042/bj20051574;
RA Lee K.H., Lee D.G., Park Y., Kang D.-I., Shin S.Y., Hahm K.-S., Kim Y.;
RT "Interactions between the plasma membrane and the antimicrobial peptide HP
RT (2-20) and its analogues derived from Helicobacter pylori.";
RL Biochem. J. 394:105-114(2006).
CC -!- FUNCTION: Binds directly to 23S rRNA. The L1 stalk is quite mobile in
CC the ribosome, and is involved in E site tRNA release.
CC {ECO:0000255|HAMAP-Rule:MF_01318}.
CC -!- FUNCTION: Protein L1 is also a translational repressor protein, it
CC controls the translation of the L11 operon by binding to its mRNA.
CC {ECO:0000255|HAMAP-Rule:MF_01318}.
CC -!- FUNCTION: Peptides originating from the N-terminal end of L1 have
CC antibacterial activity against bacteria such as E.coli and B.megaterium
CC and modest antifungal activities. Has no effect on H.pylori itself.
CC Peptides are not hemolytic against mammalian cells. These peptides may
CC be released in the stomach during altruistic lysis to kill other fast
CC growing bacteria.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit.
CC -!- MISCELLANEOUS: The antimicrobial peptide HP (2-20) forms a short alpha-
CC helix. Increasing the amphiphilicity of the helix increases its
CC antimicrobial activities.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL1 family.
CC {ECO:0000255|HAMAP-Rule:MF_01318}.
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DR EMBL; AE000511; AAD08247.1; -; Genomic_DNA.
DR EMBL; U86609; AAB47277.1; -; Genomic_DNA.
DR PIR; A64670; A64670.
DR RefSeq; NP_207992.1; NC_000915.1.
DR RefSeq; WP_001085839.1; NC_018939.1.
DR PDB; 1OT0; NMR; -; A=2-18.
DR PDB; 1P0G; NMR; -; A=2-20.
DR PDB; 1P0J; NMR; -; A=2-18.
DR PDB; 1P0L; NMR; -; A=2-20.
DR PDB; 1P0O; NMR; -; A=2-20.
DR PDB; 1P5K; NMR; -; A=2-20.
DR PDB; 1P5L; NMR; -; A=7-20.
DR PDBsum; 1OT0; -.
DR PDBsum; 1P0G; -.
DR PDBsum; 1P0J; -.
DR PDBsum; 1P0L; -.
DR PDBsum; 1P0O; -.
DR PDBsum; 1P5K; -.
DR PDBsum; 1P5L; -.
DR AlphaFoldDB; P56029; -.
DR SMR; P56029; -.
DR STRING; 85962.C694_06215; -.
DR PaxDb; P56029; -.
DR EnsemblBacteria; AAD08247; AAD08247; HP_1201.
DR KEGG; hpy:HP_1201; -.
DR PATRIC; fig|85962.47.peg.1291; -.
DR eggNOG; COG0081; Bacteria.
DR OMA; GWTDVDV; -.
DR PhylomeDB; P56029; -.
DR EvolutionaryTrace; P56029; -.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0015934; C:large ribosomal subunit; IEA:InterPro.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR CDD; cd00403; Ribosomal_L1; 1.
DR Gene3D; 3.40.50.790; -; 1.
DR HAMAP; MF_01318_B; Ribosomal_L1_B; 1.
DR InterPro; IPR005878; Ribosom_L1_bac-type.
DR InterPro; IPR002143; Ribosomal_L1.
DR InterPro; IPR023674; Ribosomal_L1-like.
DR InterPro; IPR028364; Ribosomal_L1/biogenesis.
DR InterPro; IPR016095; Ribosomal_L1_3-a/b-sand.
DR InterPro; IPR023673; Ribosomal_L1_CS.
DR Pfam; PF00687; Ribosomal_L1; 1.
DR PIRSF; PIRSF002155; Ribosomal_L1; 1.
DR SUPFAM; SSF56808; SSF56808; 1.
DR TIGRFAMs; TIGR01169; rplA_bact; 1.
DR PROSITE; PS01199; RIBOSOMAL_L1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial; Reference proteome; Repressor;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding;
KW Translation regulation; tRNA-binding.
FT CHAIN 1..234
FT /note="50S ribosomal protein L1"
FT /id="PRO_0000125667"
FT VARIANT 155
FT /note="S -> T (in strain: Hp921023)"
FT MUTAGEN 17..19
FT /note="QND->WNW: Increases antibacterial and antifungal
FT activities 2-4 fold without an increase in hemolytic
FT activities."
FT /evidence="ECO:0000269|PubMed:16255716"
FT HELIX 6..19
FT /evidence="ECO:0007829|PDB:1OT0"
SQ SEQUENCE 234 AA; 25266 MW; BC7CECDB6B0B0EA8 CRC64;
MAKKVFKRLE KLFSKIQNDK AYGVEQGVEV VKSLASAKFD ETVEVALRLG VDPRHADQMV
RGAVVLPHGT GKKVRVAVFA KDIKQDEAKN AGADVVGGDD LAEEIKNGRI DFDMVIATPD
MMAVVGKVGR ILGPKGLMPN PKTGTVTMDI AKAVSNAKSG QVNFRVDKKG NVHAPIGKAS
FPEEKIKENM LELVKTINRL KPSSAKGKYI RNAALSLTMS PSVSLDAQEL MDIK
