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Database: UniProt
Entry: A0A0P0E2P4_9MICO
LinkDB: A0A0P0E2P4_9MICO
Original site: A0A0P0E2P4_9MICO 
ID   A0A0P0E2P4_9MICO        Unreviewed;       129 AA.
AC   A0A0P0E2P4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
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=AOA12_15870 {ECO:0000313|EMBL:ALJ21296.1};
OS   Microbacterium sp. No. 7.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=1714373 {ECO:0000313|EMBL:ALJ21296.1, ECO:0000313|Proteomes:UP000059097};
RN   [1] {ECO:0000313|EMBL:ALJ21296.1, ECO:0000313|Proteomes:UP000059097}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=No. 7 {ECO:0000313|EMBL:ALJ21296.1,
RC   ECO:0000313|Proteomes:UP000059097};
RA   Ohtsubo Y., Nagata Y., Numata M., Tsuchikane K., Hosoyama A., Yamazoe A.,
RA   Tsuda M., Fujita N., Kawai F.;
RT   "Complete genome sequence of a polypropylene glycol-degrading strain
RT   Microbacterium sp. No. 7.";
RL   Submitted (SEP-2015) 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; CP012697; ALJ21296.1; -; Genomic_DNA.
DR   RefSeq; WP_054684795.1; NZ_CP012697.1.
DR   AlphaFoldDB; A0A0P0E2P4; -.
DR   STRING; 1714373.AOA12_15870; -.
DR   KEGG; mio:AOA12_15870; -.
DR   PATRIC; fig|1714373.3.peg.3265; -.
DR   OrthoDB; 9811748at2; -.
DR   Proteomes; UP000059097; 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:UP000059097};
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          6..52
FT                   /note="Large ribosomal subunit protein bL12
FT                   oligomerization"
FT                   /evidence="ECO:0000259|Pfam:PF16320"
FT   DOMAIN          63..129
FT                   /note="Large ribosomal subunit protein bL12 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00542"
SQ   SEQUENCE   129 AA;  13182 MW;  2A623AD532F6F439 CRC64;
     MAKLSTEELL DAFKELTLIE LSEFVKAFEE AFDVTAAAPV AVAAAGAPAG GAPAEEAEEK
     DSFDVILEAA GDKKIQVIKV VRELTSLGLG EAKAVVDGAP KAVIEGANKE AAEKAKAALE
     EAGASVTLK
//
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