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   27-MAR-2024, entry version 151.
DE   RecName: Full=Large ribosomal subunit protein uL13 {ECO:0000255|HAMAP-Rule:MF_01366};
DE   AltName: Full=50S ribosomal protein L13 {ECO:0000305};
DE   AltName: Full=Hmal13;
GN   Name=rpl13 {ECO:0000255|HAMAP-Rule:MF_01366};
GN   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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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   PaxDb; 272569-rrnAC0065; -.
DR   EnsemblBacteria; AAV45145; AAV45145; rrnAC0065.
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   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   Gene3D; 3.90.1180.10; Ribosomal protein L13; 1.
DR   HAMAP; MF_01366; Ribosomal_uL13; 1.
DR   InterPro; IPR005822; Ribosomal_uL13.
DR   InterPro; IPR023563; Ribosomal_uL13_CS.
DR   InterPro; IPR005755; Ribosomal_uL13_euk/arc.
DR   InterPro; IPR036899; Ribosomal_uL13_sf.
DR   NCBIfam; TIGR01077; L13_A_E; 1.
DR   PANTHER; PTHR11545:SF3; 60S RIBOSOMAL PROTEIN L13A; 1.
DR   PANTHER; PTHR11545; RIBOSOMAL PROTEIN L13; 1.
DR   Pfam; PF00572; Ribosomal_L13; 1.
DR   PIRSF; PIRSF002181; Ribosomal_L13; 1.
DR   SUPFAM; SSF52161; Ribosomal protein L13; 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="Large ribosomal subunit protein uL13"
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
//