RL6_THETH
ID RL6_THETH Reviewed; 180 AA.
AC P24316; P74908;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=50S ribosomal protein L6 {ECO:0000255|HAMAP-Rule:MF_01365};
GN Name=rplF {ECO:0000255|HAMAP-Rule:MF_01365};
GN Synonyms=rpl6 {ECO:0000255|HAMAP-Rule:MF_01365};
OS Thermus thermophilus.
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=274;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=VK1;
RX PubMed=9249063; DOI=10.1016/s0378-1119(97)00072-3;
RA Vysotskaya V.S., Shcherbakov D.V., Garber M.B.;
RT "Sequencing and analysis of the Thermus thermophilus ribosomal protein gene
RT cluster equivalent to the spectinomycin operon.";
RL Gene 193:23-30(1997).
RN [2]
RP PROTEIN SEQUENCE OF 2-26.
RC STRAIN=VK1;
RX PubMed=1637860; DOI=10.1016/0300-9084(92)90110-z;
RA Garber M.B., Agalarov S.C., Eliseikina I.A., Fomenkova N.P., Nikonov S.V.,
RA Sedelnikova S.E., Shikaeva O.S., Vasiliev D., Zhdanov A.S., Liljas A.,
RA Svensson L.A.;
RT "Ribosomal proteins from Thermus thermophilus for structural
RT investigations.";
RL Biochimie 74:327-336(1992).
CC -!- FUNCTION: This protein binds to the 23S rRNA, and is important in its
CC secondary structure. It is located near the subunit interface in the
CC base of the L7/L12 stalk, and near the tRNA binding site of the
CC peptidyltransferase center. {ECO:0000255|HAMAP-Rule:MF_01365}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL6 family.
CC {ECO:0000255|HAMAP-Rule:MF_01365}.
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DR EMBL; X90765; CAA62288.1; -; Genomic_DNA.
DR PIR; S15442; S15442.
DR RefSeq; WP_011173704.1; NZ_AP019801.1.
DR AlphaFoldDB; P24316; -.
DR SMR; P24316; -.
DR GeneID; 3169807; -.
DR OMA; KPDPYKG; -.
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; 3.90.930.12; -; 2.
DR HAMAP; MF_01365_B; Ribosomal_L6_B; 1.
DR InterPro; IPR000702; Ribosomal_L6.
DR InterPro; IPR020040; Ribosomal_L6_a/b-dom.
DR InterPro; IPR036789; Ribosomal_L6_a/b-dom_sf.
DR InterPro; IPR019906; Ribosomal_L6_bac-type.
DR PANTHER; PTHR11655; PTHR11655; 1.
DR PANTHER; PTHR11655:SF14; PTHR11655:SF14; 1.
DR Pfam; PF00347; Ribosomal_L6; 2.
DR PIRSF; PIRSF002162; Ribosomal_L6; 1.
DR PRINTS; PR00059; RIBOSOMALL6.
DR SUPFAM; SSF56053; SSF56053; 2.
DR TIGRFAMs; TIGR03654; L6_bact; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding; rRNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1637860"
FT CHAIN 2..180
FT /note="50S ribosomal protein L6"
FT /id="PRO_0000131073"
FT CONFLICT 2
FT /note="S -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 180 AA; 19532 MW; 1913833C0C30E95D CRC64;
MSRIGRLPIP VPKGVSVEVA PGRVKVKGPK GELEVPVSPE MRVVVEEGVV RVERPSDERR
HKSLHGLTRT LIANAVKGVS EGYSKELLIK GIGYRARLVG RALELTVGFS HPVVVEPPEG
ITFEVPEPTR VRVSGIDKQK VGQVAANIRA IRKPSAYHEK GIYYAGEPVR LKPGKAGAKK
