RL14_HALMA
ID RL14_HALMA Reviewed; 132 AA.
AC P22450; Q5V1T3;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 25-MAY-2022, entry version 141.
DE RecName: Full=50S ribosomal protein L14 {ECO:0000255|HAMAP-Rule:MF_01367};
DE AltName: Full=Hl27;
DE AltName: Full=Hmal14;
GN Name=rpl14 {ECO:0000255|HAMAP-Rule:MF_01367}; OrderedLocusNames=rrnAC1602;
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=2143141; DOI=10.1016/0014-5793(90)80923-7;
RA Arndt E.;
RT "Nucleotide sequence of four genes encoding ribosomal proteins from the
RT 'S10 and spectinomycin' operon equivalent region in the archaebacterium
RT Halobacterium marismortui.";
RL FEBS Lett. 267:193-198(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 X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF THE 50S SUBUNIT.
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=10937989; DOI=10.1126/science.289.5481.905;
RA Ban N., Nissen P., Hansen J., Moore P.B., Steitz T.A.;
RT "The complete atomic structure of the large ribosomal subunit at 2.4 A
RT resolution.";
RL Science 289:905-920(2000).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF THE 50S SUBUNIT.
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=10937990; DOI=10.1126/science.289.5481.920;
RA Nissen P., Hansen J., Ban N., Moore P.B., Steitz T.A.;
RT "The structural basis of ribosome activity in peptide bond synthesis.";
RL Science 289:920-930(2000).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF THE 50S SUBUNIT.
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=11828326; DOI=10.1038/nsb758;
RA Schmeing T.M., Seila A.C., Hansen J.L., Freeborn B., Soukup J.K.,
RA Scaringe S.A., Strobel S.A., Moore P.B., Steitz T.A.;
RT "A pre-translocational intermediate in protein synthesis observed in
RT crystals of enzymatically active 50S subunits.";
RL Nat. Struct. Biol. 9:225-230(2002).
RN [6]
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 [7]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF THE 50S SUBUNIT.
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=11483524; DOI=10.1093/emboj/20.15.4214;
RA Klein D.J., Schmeing T.M., Moore P.B., Steitz T.A.;
RT "The kink-turn: a new RNA secondary structure motif.";
RL EMBO J. 20:4214-4221(2001).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH
RP FOUR MACROLIDE ANTIBIOTICS.
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=12150912; DOI=10.1016/s1097-2765(02)00570-1;
RA Hansen J.L., Ippolito J.A., Ban N., Nissen P., Moore P.B., Steitz T.A.;
RT "The structures of four macrolide antibiotics bound to the large ribosomal
RT subunit.";
RL Mol. Cell 10:117-128(2002).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF THE 50S SUBUNIT.
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=12185246; DOI=10.1073/pnas.172404099;
RA Hansen J.L., Schmeing T.M., Moore P.B., Steitz T.A.;
RT "Structural insights into peptide bond formation.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:11670-11675(2002).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH
RP FIVE ANTIBIOTICS AT THE PEPTIDYL TRANSFERASE CENTER.
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=12860128; DOI=10.1016/s0022-2836(03)00668-5;
RA Hansen J.L., Moore P.B., Steitz T.A.;
RT "Structures of five antibiotics bound at the peptidyl transferase center of
RT the large ribosomal subunit.";
RL J. Mol. Biol. 330:1061-1075(2003).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF THE 50S SUBUNIT WITH TWO DIFFERENT
RP E SITE SUBSTRATES.
RX PubMed=14561884; DOI=10.1261/rna.5120503;
RA Schmeing T.M., Moore P.B., Steitz T.A.;
RT "Structures of deacylated tRNA mimics bound to the E site of the large
RT ribosomal subunit.";
RL RNA 9:1345-1352(2003).
RN [12]
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 two intersubunit bridges in the 70S ribosome
CC (By similarity). Binds to 23S rRNA. {ECO:0000250}.
CC -!- SUBUNIT: The L3/L14/L24e cluster may contact the 16S rRNA in 2
CC intersubunit bridges (By similarity). Part of the 50S ribosomal
CC subunit. Forms a cluster with proteins L3 and L24e. {ECO:0000250,
CC ECO:0000269|PubMed:12150912, ECO:0000269|PubMed:12860128}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL14 family.
CC {ECO:0000255|HAMAP-Rule:MF_01367}.
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DR EMBL; X55311; CAA39018.1; -; Genomic_DNA.
DR EMBL; AY596297; AAV46519.1; -; Genomic_DNA.
DR PIR; S10734; R5HS14.
DR RefSeq; WP_004516961.1; NZ_CP039138.1.
DR PDB; 1C04; X-ray; 5.00 A; D=71-85.
DR PDB; 1FFK; X-ray; 2.40 A; H=1-132.
DR PDB; 1JJ2; X-ray; 2.40 A; J=1-132.
DR PDB; 1K73; X-ray; 3.01 A; L=1-132.
DR PDB; 1K8A; X-ray; 3.00 A; L=1-132.
DR PDB; 1K9M; X-ray; 3.00 A; L=1-132.
DR PDB; 1KC8; X-ray; 3.01 A; L=1-132.
DR PDB; 1KD1; X-ray; 3.00 A; L=1-132.
DR PDB; 1KQS; X-ray; 3.10 A; J=1-132.
DR PDB; 1M1K; X-ray; 3.20 A; L=1-132.
DR PDB; 1M90; X-ray; 2.80 A; L=1-132.
DR PDB; 1N8R; X-ray; 3.00 A; L=1-132.
DR PDB; 1NJI; X-ray; 3.00 A; L=1-132.
DR PDB; 1Q7Y; X-ray; 3.20 A; L=1-132.
DR PDB; 1Q81; X-ray; 2.95 A; L=1-132.
DR PDB; 1Q82; X-ray; 2.98 A; L=1-132.
DR PDB; 1Q86; X-ray; 3.00 A; L=1-132.
DR PDB; 1QVF; X-ray; 3.10 A; J=1-132.
DR PDB; 1QVG; X-ray; 2.90 A; J=1-132.
DR PDB; 1S72; X-ray; 2.40 A; K=1-132.
DR PDB; 1VQ4; X-ray; 2.70 A; K=1-132.
DR PDB; 1VQ5; X-ray; 2.60 A; K=1-132.
DR PDB; 1VQ6; X-ray; 2.70 A; K=1-132.
DR PDB; 1VQ7; X-ray; 2.50 A; K=1-132.
DR PDB; 1VQ8; X-ray; 2.20 A; K=1-132.
DR PDB; 1VQ9; X-ray; 2.40 A; K=1-132.
DR PDB; 1VQK; X-ray; 2.30 A; K=1-132.
DR PDB; 1VQL; X-ray; 2.30 A; K=1-132.
DR PDB; 1VQM; X-ray; 2.30 A; K=1-132.
DR PDB; 1VQN; X-ray; 2.40 A; K=1-132.
DR PDB; 1VQO; X-ray; 2.20 A; K=1-132.
DR PDB; 1VQP; X-ray; 2.25 A; K=1-132.
DR PDB; 1W2B; X-ray; 3.50 A; J=1-132.
DR PDB; 1YHQ; X-ray; 2.40 A; K=1-132.
DR PDB; 1YI2; X-ray; 2.65 A; K=1-132.
DR PDB; 1YIJ; X-ray; 2.60 A; K=1-132.
DR PDB; 1YIT; X-ray; 2.80 A; K=1-132.
DR PDB; 1YJ9; X-ray; 2.90 A; K=1-132.
DR PDB; 1YJN; X-ray; 3.00 A; K=1-132.
DR PDB; 1YJW; X-ray; 2.90 A; K=1-132.
DR PDB; 2OTJ; X-ray; 2.90 A; K=1-132.
DR PDB; 2OTL; X-ray; 2.70 A; K=1-132.
DR PDB; 2QA4; X-ray; 3.00 A; K=1-132.
DR PDB; 2QEX; X-ray; 2.90 A; K=1-132.
DR PDB; 3CC2; X-ray; 2.40 A; K=1-132.
DR PDB; 3CC4; X-ray; 2.70 A; K=1-132.
DR PDB; 3CC7; X-ray; 2.70 A; K=1-132.
DR PDB; 3CCE; X-ray; 2.75 A; K=1-132.
DR PDB; 3CCJ; X-ray; 2.70 A; K=1-132.
DR PDB; 3CCL; X-ray; 2.90 A; K=1-132.
DR PDB; 3CCM; X-ray; 2.55 A; K=1-132.
DR PDB; 3CCQ; X-ray; 2.90 A; K=1-132.
DR PDB; 3CCR; X-ray; 3.00 A; K=1-132.
DR PDB; 3CCS; X-ray; 2.95 A; K=1-132.
DR PDB; 3CCU; X-ray; 2.80 A; K=1-132.
DR PDB; 3CCV; X-ray; 2.90 A; K=1-132.
DR PDB; 3CD6; X-ray; 2.75 A; K=1-132.
DR PDB; 3CMA; X-ray; 2.80 A; K=1-132.
DR PDB; 3CME; X-ray; 2.95 A; K=1-132.
DR PDB; 3CPW; X-ray; 2.70 A; J=1-132.
DR PDB; 3CXC; X-ray; 3.00 A; J=1-132.
DR PDB; 3G4S; X-ray; 3.20 A; K=1-132.
DR PDB; 3G6E; X-ray; 2.70 A; K=1-132.
DR PDB; 3G71; X-ray; 2.85 A; K=1-132.
DR PDB; 3I55; X-ray; 3.11 A; K=1-132.
DR PDB; 3I56; X-ray; 2.90 A; K=1-132.
DR PDB; 3OW2; X-ray; 2.70 A; J=1-132.
DR PDB; 4ADX; EM; 6.60 A; K=1-132.
DR PDB; 4V9F; X-ray; 2.40 A; K=1-132.
DR PDBsum; 1C04; -.
DR PDBsum; 1FFK; -.
DR PDBsum; 1JJ2; -.
DR PDBsum; 1K73; -.
DR PDBsum; 1K8A; -.
DR PDBsum; 1K9M; -.
DR PDBsum; 1KC8; -.
DR PDBsum; 1KD1; -.
DR PDBsum; 1KQS; -.
DR PDBsum; 1M1K; -.
DR PDBsum; 1M90; -.
DR PDBsum; 1N8R; -.
DR PDBsum; 1NJI; -.
DR PDBsum; 1Q7Y; -.
DR PDBsum; 1Q81; -.
DR PDBsum; 1Q82; -.
DR PDBsum; 1Q86; -.
DR PDBsum; 1QVF; -.
DR PDBsum; 1QVG; -.
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; 1W2B; -.
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; 3CPW; -.
DR PDBsum; 3CXC; -.
DR PDBsum; 3G4S; -.
DR PDBsum; 3G6E; -.
DR PDBsum; 3G71; -.
DR PDBsum; 3I55; -.
DR PDBsum; 3I56; -.
DR PDBsum; 3OW2; -.
DR PDBsum; 4ADX; -.
DR PDBsum; 4V9F; -.
DR AlphaFoldDB; P22450; -.
DR SMR; P22450; -.
DR IntAct; P22450; 2.
DR STRING; 272569.rrnAC1602; -.
DR EnsemblBacteria; AAV46519; AAV46519; rrnAC1602.
DR GeneID; 40152567; -.
DR GeneID; 64821825; -.
DR KEGG; hma:rrnAC1602; -.
DR PATRIC; fig|272569.17.peg.2291; -.
DR eggNOG; arCOG04095; Archaea.
DR HOGENOM; CLU_095071_3_0_2; -.
DR OMA; AKEVLCI; -.
DR EvolutionaryTrace; P22450; -.
DR Proteomes; UP000001169; Chromosome I.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0019843; F: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 Gene3D; 2.40.150.20; -; 1.
DR HAMAP; MF_01367; Ribosomal_L14; 1.
DR InterPro; IPR036853; Ribosomal_L14_sf.
DR InterPro; IPR000218; Ribosomal_L14P.
DR InterPro; IPR019971; Ribosomal_L14P_arc.
DR InterPro; IPR019972; Ribosomal_L14P_CS.
DR PANTHER; PTHR11761; PTHR11761; 1.
DR Pfam; PF00238; Ribosomal_L14; 1.
DR SMART; SM01374; Ribosomal_L14; 1.
DR SUPFAM; SSF50193; SSF50193; 1.
DR TIGRFAMs; TIGR03673; uL14_arch; 1.
DR PROSITE; PS00049; RIBOSOMAL_L14; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding; rRNA-binding.
FT CHAIN 1..132
FT /note="50S ribosomal protein L14"
FT /id="PRO_0000128571"
FT STRAND 5..8
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 17..20
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 22..34
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 52..60
FT /evidence="ECO:0007829|PDB:1VQ8"
FT TURN 62..66
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 68..75
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:3CME"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 115..120
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 122..125
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:1VQ8"
SQ SEQUENCE 132 AA; 14193 MW; 536F9C4461B7EA87 CRC64;
MEALGADVTQ GLEKGSLITC ADNTGARELK VISVHGYSGT KNRHPKAGLG DKITVSVTKG
TPEMRRQVLE AVVVRQRKPI RRPDGTRVKF EDNAAVIVDE NEDPRGTELK GPIAREVAQR
FGSVASAATM IV
