ID A0A0L0GXR1_9ENTR Unreviewed; 123 AA.
AC A0A0L0GXR1;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
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:KNC88639.1};
GN ORFNames=GM31_10235 {ECO:0000313|EMBL:KNC88639.1};
OS Trabulsiella odontotermitis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Trabulsiella.
OX NCBI_TaxID=379893 {ECO:0000313|EMBL:KNC88639.1, ECO:0000313|Proteomes:UP000037393};
RN [1] {ECO:0000313|EMBL:KNC88639.1, ECO:0000313|Proteomes:UP000037393}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12 {ECO:0000313|EMBL:KNC88639.1,
RC ECO:0000313|Proteomes:UP000037393};
RX PubMed=26162887;
RA Sapountzis P., Gruntjes T., Otani S., Estevez J., da Costa R.R.,
RA Plunkett G.3rd., Perna N.T., Poulsen M.;
RT "The Enterobacterium Trabulsiella odontotermitis Presents Novel Adaptations
RT Related to Its Association with Fungus-Growing Termites.";
RL Appl. Environ. Microbiol. 81:6577-6588(2015).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KNC88639.1}.
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DR EMBL; JNGI01000181; KNC88639.1; -; Genomic_DNA.
DR RefSeq; WP_038160598.1; NZ_LIFY01000021.1.
DR AlphaFoldDB; A0A0L0GXR1; -.
DR STRING; 379893.GCA_001297775_02155; -.
DR PATRIC; fig|379893.3.peg.3201; -.
DR OrthoDB; 9811748at2; -.
DR Proteomes; UP000037393; Unassembled WGS sequence.
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:UP000037393};
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 4..51
FT /note="Large ribosomal subunit protein bL12
FT oligomerization"
FT /evidence="ECO:0000259|Pfam:PF16320"
FT DOMAIN 57..123
FT /note="Large ribosomal subunit protein bL12 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00542"
SQ SEQUENCE 123 AA; 12415 MW; 255D5453D1B9C4C8 CRC64;
MSITKDQIIE AVAAMSVMDV VELISAMEEK FGVSAAAAVA VAGAGAATEA AEEKTEFDVI
LKAAGANKVA VIKAVRGATG LGLKEAKDLV ESAPAALKEG VSKDDAEALK KSLEEAGAEV
EVK
//
