ID D2TTH2_CITRI Unreviewed; 121 AA.
AC D2TTH2;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 24-JAN-2024, entry version 76.
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:CBG90471.1};
GN OrderedLocusNames=ROD_37661 {ECO:0000313|EMBL:CBG90471.1};
OS Citrobacter rodentium (strain ICC168) (Citrobacter freundii biotype 4280).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter.
OX NCBI_TaxID=637910 {ECO:0000313|EMBL:CBG90471.1, ECO:0000313|Proteomes:UP000001889};
RN [1] {ECO:0000313|EMBL:CBG90471.1, ECO:0000313|Proteomes:UP000001889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICC168 {ECO:0000313|EMBL:CBG90471.1,
RC ECO:0000313|Proteomes:UP000001889};
RX PubMed=19897651; DOI=10.1128/JB.01144-09;
RA Petty N.K., Bulgin R., Crepin V.F., Cerdeno-Tarraga A.M., Schroeder G.N.,
RA Quail M.A., Lennard N., Corton C., Barron A., Clark L., Toribio A.L.,
RA Parkhill J., Dougan G., Frankel G., Thomson N.R.;
RT "The Citrobacter rodentium genome sequence reveals convergent evolution
RT with human pathogenic Escherichia coli.";
RL J. Bacteriol. 192:525-538(2010).
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; FN543502; CBG90471.1; -; Genomic_DNA.
DR RefSeq; WP_012133812.1; NC_013716.1.
DR AlphaFoldDB; D2TTH2; -.
DR SMR; D2TTH2; -.
DR STRING; 637910.ROD_37661; -.
DR GeneID; 84238608; -.
DR KEGG; cro:ROD_37661; -.
DR eggNOG; COG0222; Bacteria.
DR HOGENOM; CLU_086499_3_2_6; -.
DR OMA; LEDKWGV; -.
DR OrthoDB; 9811748at2; -.
DR Proteomes; UP000001889; 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 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..50
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; 12327 MW; A8B04E49E00B3FC8 CRC64;
MSITKDQIIE AVSAMSVMDV VELISAMEEK FGVSAAAAVA VAAGPVEAAE EKTEFDVILK
AAGANKVAVI KAVRGATGLG LKEAKDLVES APAALKEGVS KDDAEALKKS LEEAGAEVEV
K
//