RL11_HALMA
ID RL11_HALMA Reviewed; 162 AA.
AC P14122; Q5V2B0;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 147.
DE RecName: Full=50S ribosomal protein L11 {ECO:0000255|HAMAP-Rule:MF_00736};
DE AltName: Full=Hmal11;
GN Name=rpl11 {ECO:0000255|HAMAP-Rule:MF_00736}; OrderedLocusNames=rrnAC1414;
OS Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS B-1809) (Halobacterium marismortui).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=272569;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2320419; DOI=10.1093/nar/18.5.1285;
RA Arndt E., Weigel C.;
RT "Nucleotide sequence of the genes encoding the L11, L1, L10 and L12
RT equivalent ribosomal proteins from the archaebacterium Halobacterium
RT marismortui.";
RL Nucleic Acids Res. 18:1285-1285(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=15520287; DOI=10.1101/gr.2700304;
RA Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA Hood L., Ng W.V.;
RT "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT Dead Sea.";
RL Genome Res. 14:2221-2234(2004).
RN [3]
RP PROTEIN SEQUENCE OF 2-28.
RX PubMed=3196689; DOI=10.1021/bi00418a032;
RA Walsh M.J., McDougall J., Wittmann-Liebold B.;
RT "Extended N-terminal sequencing of proteins of archaebacterial ribosomes
RT blotted from two-dimensional gels onto glass fiber and poly(vinylidene
RT difluoride) membrane.";
RL Biochemistry 27:6867-6876(1988).
RN [4]
RP 3D-STRUCTURE MODELING.
RX PubMed=10476961; DOI=10.1038/23641;
RA Ban N., Nissen P., Hansen J., Capel M., Moore P.B., Steitz T.A.;
RT "Placement of protein and RNA structures into a 5 A-resolution map of the
RT 50S ribosomal subunit.";
RL Nature 400:841-847(1999).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS), RRNA-BINDING, AND INTERACTION WITH
RP L10.
RX PubMed=17599351; DOI=10.1016/j.jmb.2007.05.091;
RA Kavran J.M., Steitz T.A.;
RT "Structure of the base of the L7/L12 stalk of the Haloarcula marismortui
RT large ribosomal subunit: analysis of L11 movements.";
RL J. Mol. Biol. 371:1047-1059(2007).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF THE 50S SUBUNIT.
RX PubMed=23695244; DOI=10.1107/s0907444913004745;
RA Gabdulkhakov A., Nikonov S., Garber M.;
RT "Revisiting the Haloarcula marismortui 50S ribosomal subunit model.";
RL Acta Crystallogr. D 69:997-1004(2013).
CC -!- FUNCTION: Forms part of the ribosomal stalk which helps the ribosome
CC interact with GTP-bound translation factors.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Forms part of the ribosomal
CC stalk which helps the ribosome interact with GTP-bound translation
CC factors. Forms a heptameric L10(L12)2(L12)2(L12)2 complex, where L10
CC forms an elongated spine to which 3 L12 dimers bind in a sequential
CC fashion (Probable). {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL11 family.
CC {ECO:0000255|HAMAP-Rule:MF_00736}.
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DR EMBL; X51430; CAA35793.1; -; Genomic_DNA.
DR EMBL; AY596297; AAV46342.1; -; Genomic_DNA.
DR PIR; S08420; R5HS11.
DR RefSeq; WP_011223608.1; NZ_CP039138.1.
DR PDB; 1C04; X-ray; 5.00 A; C=79-88.
DR PDB; 1S72; X-ray; 2.40 A; I=1-162.
DR PDB; 1VQ4; X-ray; 2.70 A; I=1-162.
DR PDB; 1VQ5; X-ray; 2.60 A; I=1-162.
DR PDB; 1VQ6; X-ray; 2.70 A; I=1-162.
DR PDB; 1VQ7; X-ray; 2.50 A; I=1-162.
DR PDB; 1VQ8; X-ray; 2.20 A; I=1-162.
DR PDB; 1VQ9; X-ray; 2.40 A; I=1-162.
DR PDB; 1VQK; X-ray; 2.30 A; I=1-162.
DR PDB; 1VQL; X-ray; 2.30 A; I=1-162.
DR PDB; 1VQM; X-ray; 2.30 A; I=1-162.
DR PDB; 1VQN; X-ray; 2.40 A; I=1-162.
DR PDB; 1VQO; X-ray; 2.20 A; I=1-162.
DR PDB; 1VQP; X-ray; 2.25 A; I=1-162.
DR PDB; 1YHQ; X-ray; 2.40 A; I=1-162.
DR PDB; 1YI2; X-ray; 2.65 A; I=1-162.
DR PDB; 1YIJ; X-ray; 2.60 A; I=1-162.
DR PDB; 1YIT; X-ray; 2.80 A; I=1-162.
DR PDB; 1YJ9; X-ray; 2.90 A; I=1-162.
DR PDB; 1YJN; X-ray; 3.00 A; I=1-162.
DR PDB; 1YJW; X-ray; 2.90 A; I=1-162.
DR PDB; 2OTJ; X-ray; 2.90 A; I=2-162.
DR PDB; 2OTL; X-ray; 2.70 A; I=1-162.
DR PDB; 2QA4; X-ray; 3.00 A; I=1-162.
DR PDB; 2QEX; X-ray; 2.90 A; I=1-162.
DR PDB; 3CC2; X-ray; 2.40 A; I=1-162.
DR PDB; 3CC4; X-ray; 2.70 A; I=1-162.
DR PDB; 3CC7; X-ray; 2.70 A; I=1-162.
DR PDB; 3CCE; X-ray; 2.75 A; I=1-162.
DR PDB; 3CCJ; X-ray; 2.70 A; I=1-162.
DR PDB; 3CCL; X-ray; 2.90 A; I=1-162.
DR PDB; 3CCM; X-ray; 2.55 A; I=1-162.
DR PDB; 3CCQ; X-ray; 2.90 A; I=1-162.
DR PDB; 3CCR; X-ray; 3.00 A; I=1-162.
DR PDB; 3CCS; X-ray; 2.95 A; I=1-162.
DR PDB; 3CCU; X-ray; 2.80 A; I=1-162.
DR PDB; 3CCV; X-ray; 2.90 A; I=1-162.
DR PDB; 3CD6; X-ray; 2.75 A; I=1-162.
DR PDB; 3CMA; X-ray; 2.80 A; I=1-162.
DR PDB; 3CME; X-ray; 2.95 A; I=1-162.
DR PDB; 3G4S; X-ray; 3.20 A; I=67-136.
DR PDB; 3G6E; X-ray; 2.70 A; I=67-136.
DR PDB; 3G71; X-ray; 2.85 A; I=67-136.
DR PDB; 3I55; X-ray; 3.11 A; I=1-162.
DR PDB; 3I56; X-ray; 2.90 A; I=1-162.
DR PDB; 4V9F; X-ray; 2.40 A; I=1-162.
DR PDBsum; 1C04; -.
DR PDBsum; 1S72; -.
DR PDBsum; 1VQ4; -.
DR PDBsum; 1VQ5; -.
DR PDBsum; 1VQ6; -.
DR PDBsum; 1VQ7; -.
DR PDBsum; 1VQ8; -.
DR PDBsum; 1VQ9; -.
DR PDBsum; 1VQK; -.
DR PDBsum; 1VQL; -.
DR PDBsum; 1VQM; -.
DR PDBsum; 1VQN; -.
DR PDBsum; 1VQO; -.
DR PDBsum; 1VQP; -.
DR PDBsum; 1YHQ; -.
DR PDBsum; 1YI2; -.
DR PDBsum; 1YIJ; -.
DR PDBsum; 1YIT; -.
DR PDBsum; 1YJ9; -.
DR PDBsum; 1YJN; -.
DR PDBsum; 1YJW; -.
DR PDBsum; 2OTJ; -.
DR PDBsum; 2OTL; -.
DR PDBsum; 2QA4; -.
DR PDBsum; 2QEX; -.
DR PDBsum; 3CC2; -.
DR PDBsum; 3CC4; -.
DR PDBsum; 3CC7; -.
DR PDBsum; 3CCE; -.
DR PDBsum; 3CCJ; -.
DR PDBsum; 3CCL; -.
DR PDBsum; 3CCM; -.
DR PDBsum; 3CCQ; -.
DR PDBsum; 3CCR; -.
DR PDBsum; 3CCS; -.
DR PDBsum; 3CCU; -.
DR PDBsum; 3CCV; -.
DR PDBsum; 3CD6; -.
DR PDBsum; 3CMA; -.
DR PDBsum; 3CME; -.
DR PDBsum; 3G4S; -.
DR PDBsum; 3G6E; -.
DR PDBsum; 3G71; -.
DR PDBsum; 3I55; -.
DR PDBsum; 3I56; -.
DR PDBsum; 4V9F; -.
DR AlphaFoldDB; P14122; -.
DR SMR; P14122; -.
DR IntAct; P14122; 1.
DR STRING; 272569.rrnAC1414; -.
DR EnsemblBacteria; AAV46342; AAV46342; rrnAC1414.
DR GeneID; 40152382; -.
DR KEGG; hma:rrnAC1414; -.
DR PATRIC; fig|272569.17.peg.2109; -.
DR eggNOG; arCOG04372; Archaea.
DR HOGENOM; CLU_074237_4_0_2; -.
DR OMA; CKQFNAK; -.
DR EvolutionaryTrace; P14122; -.
DR Proteomes; UP000001169; Chromosome I.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0070180; F:large ribosomal subunit rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR CDD; cd00349; Ribosomal_L11; 1.
DR Gene3D; 1.10.10.250; -; 1.
DR Gene3D; 3.30.1550.10; -; 1.
DR HAMAP; MF_00736; Ribosomal_L11; 1.
DR InterPro; IPR000911; Ribosomal_L11/L12.
DR InterPro; IPR036796; Ribosomal_L11/L12_N_sf.
DR InterPro; IPR020783; Ribosomal_L11_C.
DR InterPro; IPR036769; Ribosomal_L11_C_sf.
DR InterPro; IPR020785; Ribosomal_L11_CS.
DR InterPro; IPR020784; Ribosomal_L11_N.
DR PANTHER; PTHR11661; PTHR11661; 1.
DR Pfam; PF00298; Ribosomal_L11; 1.
DR Pfam; PF03946; Ribosomal_L11_N; 1.
DR SMART; SM00649; RL11; 1.
DR SUPFAM; SSF46906; SSF46906; 1.
DR SUPFAM; SSF54747; SSF54747; 1.
DR PROSITE; PS00359; RIBOSOMAL_L11; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3196689"
FT CHAIN 2..162
FT /note="50S ribosomal protein L11"
FT /id="PRO_0000104431"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT TURN 17..20
FT /evidence="ECO:0007829|PDB:2QA4"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:2QA4"
FT HELIX 35..41
FT /evidence="ECO:0007829|PDB:2QA4"
FT STRAND 50..56
FT /evidence="ECO:0007829|PDB:2QA4"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:2QA4"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:2QA4"
FT HELIX 71..77
FT /evidence="ECO:0007829|PDB:1VQ8"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 98..107
FT /evidence="ECO:0007829|PDB:1VQ8"
FT TURN 108..111
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 117..127
FT /evidence="ECO:0007829|PDB:1VQ8"
FT TURN 128..132
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 133..136
FT /evidence="ECO:0007829|PDB:1VQ8"
SQ SEQUENCE 162 AA; 17089 MW; E64E6802B49208B8 CRC64;
MAGTIEVLVP GGEANPGPPL GPELGPTPVD VQAVVQEIND QTAAFDGTEV PVTVKYDDDG
SFEIEVGVPP TAELIKDEAG FETGSGEPQE DFVADLSVDQ VKQIAEQKHP DLLSYDLTNA
AKEVVGTCTS LGVTIEGENP REFKERIDAG EYDDVFAAEA QA
