RL6_MARSD
ID RL6_MARSD Reviewed; 178 AA.
AC C6C1A0;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=50S ribosomal protein L6 {ECO:0000255|HAMAP-Rule:MF_01365};
GN Name=rplF {ECO:0000255|HAMAP-Rule:MF_01365}; OrderedLocusNames=Desal_1200;
OS Maridesulfovibrio salexigens (strain ATCC 14822 / DSM 2638 / NCIMB 8403 /
OS VKM B-1763) (Desulfovibrio salexigens).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Maridesulfovibrio.
OX NCBI_TaxID=526222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14822 / DSM 2638 / NCIMB 8403 / VKM B-1763;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Anderson I.,
RA Wall J.D., Arkin A.P., Dehal P., Chivian D., Giles B., Hazen T.C.;
RT "Complete sequence of Desulfovibrio salexigens DSM 2638.";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001649; ACS79263.1; -; Genomic_DNA.
DR RefSeq; WP_015851081.1; NC_012881.1.
DR AlphaFoldDB; C6C1A0; -.
DR SMR; C6C1A0; -.
DR STRING; 526222.Desal_1200; -.
DR PRIDE; C6C1A0; -.
DR EnsemblBacteria; ACS79263; ACS79263; Desal_1200.
DR KEGG; dsa:Desal_1200; -.
DR eggNOG; COG0097; Bacteria.
DR HOGENOM; CLU_065464_1_2_7; -.
DR OMA; KPDPYKG; -.
DR OrthoDB; 1398618at2; -.
DR Proteomes; UP000002601; 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 Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding.
FT CHAIN 1..178
FT /note="50S ribosomal protein L6"
FT /id="PRO_1000214922"
SQ SEQUENCE 178 AA; 18980 MW; 1D14BD9632E56DA3 CRC64;
MSRIGKKPID IPSGVEVTVG ADVVSVKGPK GTITTPVHPM VSFTVADNAV EVKRSGDSRQ
ERAQHGLHRS LLANCIEGVS KGFSKTLEVV GVGYKVNVQG KNIVLNVGFS HPVNYELPAG
IEASAEGNTK LTISGVDKQL VGEVAAQLRR VRPPEPYKGK GIKYIDEQIR RKAGKSGK