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Database: UniProt
Entry: A0A0D8I5B7_9CLOT
LinkDB: A0A0D8I5B7_9CLOT
Original site: A0A0D8I5B7_9CLOT 
ID   A0A0D8I5B7_9CLOT        Unreviewed;       121 AA.
AC   A0A0D8I5B7;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Large ribosomal subunit protein bL12 {ECO:0000256|HAMAP-Rule:MF_00368};
GN   Name=rplL {ECO:0000256|HAMAP-Rule:MF_00368,
GN   ECO:0000313|EMBL:AKL97063.1};
GN   ORFNames=CACET_c36320 {ECO:0000313|EMBL:AKL97063.1};
OS   Clostridium aceticum.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=84022 {ECO:0000313|EMBL:AKL97063.1, ECO:0000313|Proteomes:UP000035704};
RN   [1] {ECO:0000313|EMBL:AKL97063.1, ECO:0000313|Proteomes:UP000035704}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1496 {ECO:0000313|EMBL:AKL97063.1,
RC   ECO:0000313|Proteomes:UP000035704};
RA   Poehlein A., Schiel-Bengelsdorf B., Gottschalk G., Duerre P., Daniel R.;
RT   "Genome sequence of Clostridium aceticum DSM 1496.";
RL   Submitted (OCT-2014) 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: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; CP009687; AKL97063.1; -; Genomic_DNA.
DR   RefSeq; WP_044826535.1; NZ_JYHU01000041.1.
DR   AlphaFoldDB; A0A0D8I5B7; -.
DR   STRING; 84022.CACET_c36320; -.
DR   KEGG; cace:CACET_c36320; -.
DR   PATRIC; fig|84022.5.peg.3360; -.
DR   OrthoDB; 9811748at2; -.
DR   Proteomes; UP000035704; 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:UP000035704};
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          2..48
FT                   /note="Large ribosomal subunit protein bL12
FT                   oligomerization"
FT                   /evidence="ECO:0000259|Pfam:PF16320"
FT   DOMAIN          55..121
FT                   /note="Large ribosomal subunit protein bL12 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00542"
SQ   SEQUENCE   121 AA;  12597 MW;  7F8FD5D1CC1754A3 CRC64;
     MTIEQILEAI ENMKVLELNE LVKAAEEKFG VSAAAPVVVG GAVAGAAAEE EKTEFDVILA
     SAGASKIGVI KIVREITGLG LKEAKELVDN APKPLKEGIA KDEAEAMKAK LEEAGAVIEV
     K
//
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