ID M6RGE4_LEPIR Unreviewed; 127 AA.
AC M6RGE4;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 42.
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:EMO04841.1};
GN ORFNames=LEP1GSC116_2099 {ECO:0000313|EMBL:EMO04841.1};
OS Leptospira interrogans serovar Icterohaemorrhagiae str. Verdun HP.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1049910 {ECO:0000313|EMBL:EMO04841.1, ECO:0000313|Proteomes:UP000012092};
RN [1] {ECO:0000313|EMBL:EMO04841.1, ECO:0000313|Proteomes:UP000012092}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Verdun HP {ECO:0000313|EMBL:EMO04841.1,
RC ECO:0000313|Proteomes:UP000012092};
RA Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA Sanka R., DePew J., Purushe J., Picardeau M., Werts C., Goarant C.,
RA Vinetz J.M., Sutton G.G., Nierman W.C., Fouts D.E.;
RL Submitted (JAN-2013) 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}.
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:EMO04841.1}.
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DR EMBL; AHNZ02000571; EMO04841.1; -; Genomic_DNA.
DR AlphaFoldDB; M6RGE4; -.
DR SMR; M6RGE4; -.
DR Proteomes; UP000012092; 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 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 3..51
FT /note="Large ribosomal subunit protein bL12
FT oligomerization"
FT /evidence="ECO:0000259|Pfam:PF16320"
FT DOMAIN 58..125
FT /note="Large ribosomal subunit protein bL12 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00542"
SQ SEQUENCE 127 AA; 12808 MW; D2FAC7FF66A13161 CRC64;
MSTEALLEQI GKLTLVEAAD LVKKMEDKFG ISAAAPVAVA AVGAAPAGAG AAEEASTFNV
ILKGFDSAKK IEVIKLVREI TGLGLADAKG LVEAGGKAVK EGVAKAEADD LKKKFEGAGA
QIELKAS
//