ID RL7_PETMO Reviewed; 128 AA.
AC A9BF34;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 24-JAN-2024, entry version 85.
DE RecName: Full=Large ribosomal subunit protein bL12 {ECO:0000255|HAMAP-Rule:MF_00368};
DE AltName: Full=50S ribosomal protein L7/L12 {ECO:0000305};
GN Name=rplL {ECO:0000255|HAMAP-Rule:MF_00368}; OrderedLocusNames=Pmob_0356;
OS Petrotoga mobilis (strain DSM 10674 / SJ95).
OC Bacteria; Thermotogota; Thermotogae; Petrotogales; Petrotogaceae;
OC Petrotoga.
OX NCBI_TaxID=403833;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10674 / SJ95;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Meincke L., Brettin T., Bruce D., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Noll K., Richardson P.;
RT "Complete sequence of Petroga mobilis SJ95.";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Forms part of the ribosomal stalk which helps the ribosome
CC interact with GTP-bound translation factors. Is thus essential for
CC accurate translation. {ECO:0000255|HAMAP-Rule:MF_00368}.
CC -!- SUBUNIT: Homodimer. Part of the ribosomal stalk of the 50S ribosomal
CC subunit. Forms a multimeric L10(L12)X complex, where L10 forms an
CC elongated spine to which 2 to 4 L12 dimers bind in a sequential
CC fashion. Binds GTP-bound translation factors. {ECO:0000255|HAMAP-
CC Rule:MF_00368}.
CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL12 family.
CC {ECO:0000255|HAMAP-Rule:MF_00368}.
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DR EMBL; CP000879; ABX31098.1; -; Genomic_DNA.
DR RefSeq; WP_012208205.1; NC_010003.1.
DR AlphaFoldDB; A9BF34; -.
DR SMR; A9BF34; -.
DR STRING; 403833.Pmob_0356; -.
DR KEGG; pmo:Pmob_0356; -.
DR eggNOG; COG0222; Bacteria.
DR HOGENOM; CLU_086499_3_2_0; -.
DR OMA; LEDKWGV; -.
DR OrthoDB; 9811748at2; -.
DR Proteomes; UP000000789; Chromosome.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR GO; GO:0005840; C:ribosome; 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; cd00387; Ribosomal_L7_L12; 1.
DR Gene3D; 3.30.1390.10; -; 1.
DR Gene3D; 1.20.5.710; Single helix bin; 1.
DR HAMAP; MF_00368; Ribosomal_bL12; 1.
DR InterPro; IPR000206; Ribosomal_bL12.
DR InterPro; IPR013823; Ribosomal_bL12_C.
DR InterPro; IPR014719; Ribosomal_bL12_C/ClpS-like.
DR InterPro; IPR008932; Ribosomal_bL12_oligo.
DR InterPro; IPR036235; Ribosomal_bL12_oligo_N_sf.
DR NCBIfam; TIGR00855; L12; 1.
DR PANTHER; PTHR45987; 39S RIBOSOMAL PROTEIN L12; 1.
DR PANTHER; PTHR45987:SF4; 39S RIBOSOMAL PROTEIN L12, MITOCHONDRIAL; 1.
DR Pfam; PF00542; Ribosomal_L12; 1.
DR Pfam; PF16320; Ribosomal_L12_N; 1.
DR SUPFAM; SSF54736; ClpS-like; 1.
DR SUPFAM; SSF48300; Ribosomal protein L7/12, oligomerisation (N-terminal) domain; 1.
PE 3: Inferred from homology;
KW Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1..128
FT /note="Large ribosomal subunit protein bL12"
FT /id="PRO_1000121467"
SQ SEQUENCE 128 AA; 13700 MW; F0E59FD9F20B75F6 CRC64;
MTKEELINEI KNMTVGELAE LVKALEDEFG VSAAAPVMAA VPGVAGVSPA QQEEEKTDFK
VVLKGFGDKK IGVIKVVREI TNLGLKEAKD LVEKAGTPDA VIKEGVPKEE AEEIKKKLEE
AGAEVELK
//