RL6_PROMP
ID RL6_PROMP Reviewed; 179 AA.
AC Q7UZV8;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 101.
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}; OrderedLocusNames=PMM1544;
OS Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / NIES-2087 /
OS MED4).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=59919;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1986 / NIES-2087 / MED4;
RX PubMed=12917642; DOI=10.1038/nature01947;
RA Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A.,
RA Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L.,
RA Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C.,
RA Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R.,
RA Chisholm S.W.;
RT "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche
RT differentiation.";
RL Nature 424:1042-1047(2003).
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. {ECO:0000255|HAMAP-
CC Rule:MF_01365}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL6 family.
CC {ECO:0000255|HAMAP-Rule:MF_01365}.
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DR EMBL; BX548174; CAE20003.1; -; Genomic_DNA.
DR RefSeq; WP_011133172.1; NC_005072.1.
DR AlphaFoldDB; Q7UZV8; -.
DR SMR; Q7UZV8; -.
DR STRING; 59919.PMM1544; -.
DR EnsemblBacteria; CAE20003; CAE20003; PMM1544.
DR KEGG; pmm:PMM1544; -.
DR eggNOG; COG0097; Bacteria.
DR HOGENOM; CLU_065464_1_2_3; -.
DR OMA; KPDPYKG; -.
DR OrthoDB; 1398618at2; -.
DR Proteomes; UP000001026; Chromosome.
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 InterPro; IPR002358; Ribosomal_L6_CS.
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.
DR PROSITE; PS00525; RIBOSOMAL_L6_1; 1.
PE 3: Inferred from homology;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT CHAIN 1..179
FT /note="50S ribosomal protein L6"
FT /id="PRO_0000260915"
SQ SEQUENCE 179 AA; 19630 MW; 1A43E35AE5CEA671 CRC64;
MSRIGKSPVQ IPEKVSVDIK GLSITVKGPK GELKRLMPEG VNFDQKENQI VVTPATTKRY
SRERHGLCRT LISNMVQGVT EGYEKKLEIV GVGSRAQVKG KNLVVSAGYS HPVEMTPPDG
ITYKVESNTN VTVSGIDKEI VGNEAAKIRS IRPPEPYKGK GIKYQDERII RKAGKSGKK