RL13_HALMA
ID RL13_HALMA Reviewed; 145 AA.
AC P29198; Q5V5Q7;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 25-MAY-2022, entry version 143.
DE RecName: Full=50S ribosomal protein L13 {ECO:0000255|HAMAP-Rule:MF_01366};
DE AltName: Full=Hmal13;
GN Name=rpl13 {ECO:0000255|HAMAP-Rule:MF_01366}; OrderedLocusNames=rrnAC0065;
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=1840597; DOI=10.1016/s0021-9258(18)54267-8;
RA Kroemer W.J., Arndt E.;
RT "Halobacterial S9 operon. Three ribosomal protein genes are cotranscribed
RT with genes encoding a tRNA(Leu), the enolase, and a putative membrane
RT protein in the archaebacterium Haloarcula (Halobacterium) marismortui.";
RL J. Biol. Chem. 266:24573-24579(1991).
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 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 [7]
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 [8]
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 [9]
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 [10]
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 [11]
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: This protein is one of the early assembly proteins of the 50S
CC ribosomal subunit (By similarity). Binds to 23S rRNA. {ECO:0000250}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Interacts weakly with
CC proteins L3 and L6. {ECO:0000255|HAMAP-Rule:MF_01366,
CC ECO:0000269|PubMed:12150912, ECO:0000269|PubMed:12860128}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL13 family.
CC {ECO:0000255|HAMAP-Rule:MF_01366}.
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DR EMBL; M76567; AAA73097.1; -; Genomic_DNA.
DR EMBL; AY596297; AAV45145.1; -; Genomic_DNA.
DR PIR; B41715; B41715.
DR RefSeq; WP_004593558.1; NZ_CP039138.1.
DR PDB; 1FFK; X-ray; 2.40 A; G=1-145.
DR PDB; 1JJ2; X-ray; 2.40 A; I=1-145.
DR PDB; 1K73; X-ray; 3.01 A; K=1-145.
DR PDB; 1K8A; X-ray; 3.00 A; K=1-145.
DR PDB; 1K9M; X-ray; 3.00 A; K=1-145.
DR PDB; 1KC8; X-ray; 3.01 A; K=1-145.
DR PDB; 1KD1; X-ray; 3.00 A; K=1-145.
DR PDB; 1KQS; X-ray; 3.10 A; I=1-145.
DR PDB; 1M1K; X-ray; 3.20 A; K=1-145.
DR PDB; 1M90; X-ray; 2.80 A; K=1-145.
DR PDB; 1ML5; EM; 14.00 A; m=1-145.
DR PDB; 1N8R; X-ray; 3.00 A; K=1-145.
DR PDB; 1NJI; X-ray; 3.00 A; K=1-145.
DR PDB; 1Q7Y; X-ray; 3.20 A; K=1-145.
DR PDB; 1Q81; X-ray; 2.95 A; K=1-145.
DR PDB; 1Q82; X-ray; 2.98 A; K=1-145.
DR PDB; 1Q86; X-ray; 3.00 A; K=1-145.
DR PDB; 1QVF; X-ray; 3.10 A; I=1-145.
DR PDB; 1QVG; X-ray; 2.90 A; I=1-145.
DR PDB; 1S72; X-ray; 2.40 A; J=1-145.
DR PDB; 1VQ4; X-ray; 2.70 A; J=1-145.
DR PDB; 1VQ5; X-ray; 2.60 A; J=1-145.
DR PDB; 1VQ6; X-ray; 2.70 A; J=1-145.
DR PDB; 1VQ7; X-ray; 2.50 A; J=1-145.
DR PDB; 1VQ8; X-ray; 2.20 A; J=1-145.
DR PDB; 1VQ9; X-ray; 2.40 A; J=1-145.
DR PDB; 1VQK; X-ray; 2.30 A; J=1-145.
DR PDB; 1VQL; X-ray; 2.30 A; J=1-145.
DR PDB; 1VQM; X-ray; 2.30 A; J=1-145.
DR PDB; 1VQN; X-ray; 2.40 A; J=1-145.
DR PDB; 1VQO; X-ray; 2.20 A; J=1-145.
DR PDB; 1VQP; X-ray; 2.25 A; J=1-145.
DR PDB; 1W2B; X-ray; 3.50 A; I=1-145.
DR PDB; 1YHQ; X-ray; 2.40 A; J=1-145.
DR PDB; 1YI2; X-ray; 2.65 A; J=1-145.
DR PDB; 1YIJ; X-ray; 2.60 A; J=1-145.
DR PDB; 1YIT; X-ray; 2.80 A; J=1-145.
DR PDB; 1YJ9; X-ray; 2.90 A; J=1-145.
DR PDB; 1YJN; X-ray; 3.00 A; J=1-145.
DR PDB; 1YJW; X-ray; 2.90 A; J=1-145.
DR PDB; 2OTJ; X-ray; 2.90 A; J=1-145.
DR PDB; 2OTL; X-ray; 2.70 A; J=1-145.
DR PDB; 2QA4; X-ray; 3.00 A; J=1-145.
DR PDB; 2QEX; X-ray; 2.90 A; J=1-145.
DR PDB; 3CC2; X-ray; 2.40 A; J=1-145.
DR PDB; 3CC4; X-ray; 2.70 A; J=1-145.
DR PDB; 3CC7; X-ray; 2.70 A; J=1-145.
DR PDB; 3CCE; X-ray; 2.75 A; J=1-145.
DR PDB; 3CCJ; X-ray; 2.70 A; J=1-145.
DR PDB; 3CCL; X-ray; 2.90 A; J=1-145.
DR PDB; 3CCM; X-ray; 2.55 A; J=1-145.
DR PDB; 3CCQ; X-ray; 2.90 A; J=1-145.
DR PDB; 3CCR; X-ray; 3.00 A; J=1-145.
DR PDB; 3CCS; X-ray; 2.95 A; J=1-145.
DR PDB; 3CCU; X-ray; 2.80 A; J=1-145.
DR PDB; 3CCV; X-ray; 2.90 A; J=1-145.
DR PDB; 3CD6; X-ray; 2.75 A; J=1-145.
DR PDB; 3CMA; X-ray; 2.80 A; J=1-145.
DR PDB; 3CME; X-ray; 2.95 A; J=1-145.
DR PDB; 3CPW; X-ray; 2.70 A; I=1-145.
DR PDB; 3CXC; X-ray; 3.00 A; I=1-145.
DR PDB; 3G4S; X-ray; 3.20 A; J=4-145.
DR PDB; 3G6E; X-ray; 2.70 A; J=4-145.
DR PDB; 3G71; X-ray; 2.85 A; J=4-145.
DR PDB; 3I55; X-ray; 3.11 A; J=1-145.
DR PDB; 3I56; X-ray; 2.90 A; J=1-145.
DR PDB; 3OW2; X-ray; 2.70 A; I=4-145.
DR PDB; 4V42; X-ray; 5.50 A; BM=1-145.
DR PDB; 4V4R; X-ray; 5.90 A; N=1-145.
DR PDB; 4V4S; X-ray; 6.76 A; N=1-145.
DR PDB; 4V4T; X-ray; 6.46 A; BN=1-145.
DR PDB; 4V9F; X-ray; 2.40 A; J=1-145.
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; 1ML5; -.
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; 4V42; -.
DR PDBsum; 4V4R; -.
DR PDBsum; 4V4S; -.
DR PDBsum; 4V4T; -.
DR PDBsum; 4V9F; -.
DR AlphaFoldDB; P29198; -.
DR SMR; P29198; -.
DR IntAct; P29198; 3.
DR STRING; 272569.rrnAC0065; -.
DR EnsemblBacteria; AAV45145; AAV45145; rrnAC0065.
DR GeneID; 40154380; -.
DR GeneID; 64823168; -.
DR KEGG; hma:rrnAC0065; -.
DR PATRIC; fig|272569.17.peg.873; -.
DR eggNOG; arCOG04242; Archaea.
DR HOGENOM; CLU_076922_1_0_2; -.
DR OMA; GMLPWKT; -.
DR EvolutionaryTrace; P29198; -.
DR Proteomes; UP000001169; Chromosome I.
DR GO; GO:0015934; C:large ribosomal subunit; IEA:InterPro.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR CDD; cd00392; Ribosomal_L13; 1.
DR Gene3D; 3.90.1180.10; -; 1.
DR HAMAP; MF_01366; Ribosomal_L13; 1.
DR InterPro; IPR005822; Ribosomal_L13.
DR InterPro; IPR023563; Ribosomal_L13_CS.
DR InterPro; IPR005755; Ribosomal_L13_euk/arc.
DR InterPro; IPR036899; Ribosomal_L13_sf.
DR PANTHER; PTHR11545; PTHR11545; 1.
DR PANTHER; PTHR11545:SF3; PTHR11545:SF3; 1.
DR Pfam; PF00572; Ribosomal_L13; 1.
DR PIRSF; PIRSF002181; Ribosomal_L13; 1.
DR SUPFAM; SSF52161; SSF52161; 1.
DR TIGRFAMs; TIGR01077; L13_A_E; 1.
DR PROSITE; PS00783; RIBOSOMAL_L13; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding; rRNA-binding.
FT CHAIN 1..145
FT /note="50S ribosomal protein L13"
FT /id="PRO_0000133758"
FT STRAND 9..13
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 19..31
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 50..62
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 75..84
FT /evidence="ECO:0007829|PDB:1VQ8"
FT TURN 85..90
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 92..99
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:1VQ8"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:1VQ8"
FT TURN 117..119
FT /evidence="ECO:0007829|PDB:3CC4"
FT TURN 123..125
FT /evidence="ECO:0007829|PDB:1VQO"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:1VQ8"
FT HELIX 132..139
FT /evidence="ECO:0007829|PDB:1VQ8"
SQ SEQUENCE 145 AA; 16228 MW; 069CE666662AE3BC CRC64;
MSVAEFDADV IVDARDCIMG RVASQVAEQA LDGETVAVVN AERAVITGRE EQIVEKYEKR
VDIGNDNGYF YPKRPDGIFK RTIRGMLPHK KQRGREAFES VRVYLGNPYD EDGEVLDGTS
LDRLSNIKFV TLGEISETLG ANKTW
