ID A0A142EL48_9BACT Unreviewed; 126 AA.
AC A0A142EL48;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Large ribosomal subunit protein bL12 {ECO:0000256|HAMAP-Rule:MF_00368};
GN Name=rplL {ECO:0000256|HAMAP-Rule:MF_00368};
GN ORFNames=AO498_05485 {ECO:0000313|EMBL:AMQ55853.1};
OS Algoriphagus sanaruensis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Algoriphagus.
OX NCBI_TaxID=1727163 {ECO:0000313|EMBL:AMQ55853.1, ECO:0000313|Proteomes:UP000073816};
RN [1] {ECO:0000313|Proteomes:UP000073816}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M8-2 {ECO:0000313|Proteomes:UP000073816};
RA Shintani M.;
RT "Complete sequence of Algoriphagus sp. M8-2.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AMQ55853.1, ECO:0000313|Proteomes:UP000073816}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M8-2 {ECO:0000313|EMBL:AMQ55853.1,
RC ECO:0000313|Proteomes:UP000073816};
RX PubMed=27174266;
RA Muraguchi Y., Kushimoto K., Ohtsubo Y., Suzuki T., Dohra H., Kimbara K.,
RA Shintani M.;
RT "Complete Genome Sequence of Algoriphagus sp. Strain M8-2, Isolated from a
RT Brackish Lake.";
RL Genome Announc. 4:0-0(2016).
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:0000256|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:0000256|HAMAP-
CC Rule:MF_00368}.
CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL12 family.
CC {ECO:0000256|ARBA:ARBA00007197, ECO:0000256|HAMAP-Rule:MF_00368}.
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DR EMBL; CP012836; AMQ55853.1; -; Genomic_DNA.
DR RefSeq; WP_067544565.1; NZ_CP012836.1.
DR AlphaFoldDB; A0A142EL48; -.
DR STRING; 1727163.AO498_05485; -.
DR KEGG; alm:AO498_05485; -.
DR PATRIC; fig|1727163.4.peg.1140; -.
DR OrthoDB; 9811748at2; -.
DR Proteomes; UP000073816; 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_L7_L12; 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 Reference proteome {ECO:0000313|Proteomes:UP000073816};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW Rule:MF_00368};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW Rule:MF_00368}.
FT DOMAIN 5..50
FT /note="Large ribosomal subunit protein bL12
FT oligomerization"
FT /evidence="ECO:0000259|Pfam:PF16320"
FT DOMAIN 60..126
FT /note="Large ribosomal subunit protein bL12 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00542"
SQ SEQUENCE 126 AA; 13052 MW; 01E0833DA0A72171 CRC64;
MADLTQLAEQ LVNLTVKEVK ELTDILKDQY GIEPAAAGAV MVAGPVGGGD APAEEEKTSF
DVILKAAGAQ KLAVVKLVKE LTGLGLKEAK DLVDGAPKAL KEGVAKDEAE ALKKSLEEAG
AEVEIK
//