ID I3YMY4_ALIFI Unreviewed; 125 AA.
AC I3YMY4;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Large ribosomal subunit protein bL12 {ECO:0000256|HAMAP-Rule:MF_00368};
GN Name=rplL {ECO:0000256|HAMAP-Rule:MF_00368};
GN OrderedLocusNames=Alfi_2049 {ECO:0000313|EMBL:AFL78352.1};
OS Alistipes finegoldii (strain DSM 17242 / JCM 16770 / CCUG 46020 / CIP
OS 107999 / KCTC 15236 / AHN 2437).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC Alistipes.
OX NCBI_TaxID=679935 {ECO:0000313|EMBL:AFL78352.1, ECO:0000313|Proteomes:UP000006052};
RN [1] {ECO:0000313|Proteomes:UP000006052}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 17242 / JCM 16770 / AHN 2437 / CCUG 46020 / CIP 107999
RC {ECO:0000313|Proteomes:UP000006052};
RX PubMed=23961309; DOI=10.4056/sigs.3527032;
RA Mavromatis K., Stackebrandt E., Munk C., Lapidus A., Nolan M., Lucas S.,
RA Hammon N., Deshpande S., Cheng J.F., Tapia R., Goodwin L.A., Pitluck S.,
RA Liolios K., Pagani I., Ivanova N., Mikhailova N., Huntemann M., Pati A.,
RA Chen A., Palaniappan K., Land M., Hauser L., Rohde M., Gronow S., Goker M.,
RA Detter J.C., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Woyke T.;
RT "Complete genome sequence of the bile-resistant pigment-producing anaerobe
RT Alistipes finegoldii type strain (AHN2437(T)).";
RL Stand. Genomic Sci. 8:26-36(2013).
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; CP003274; AFL78352.1; -; Genomic_DNA.
DR RefSeq; WP_009596324.1; NC_018011.1.
DR AlphaFoldDB; I3YMY4; -.
DR STRING; 679935.Alfi_2049; -.
DR GeneID; 79838331; -.
DR KEGG; afd:Alfi_2049; -.
DR PATRIC; fig|679935.3.peg.1977; -.
DR eggNOG; COG0222; Bacteria.
DR HOGENOM; CLU_086499_3_1_10; -.
DR Proteomes; UP000006052; 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 5..51
FT /note="Large ribosomal subunit protein bL12
FT oligomerization"
FT /evidence="ECO:0000259|Pfam:PF16320"
FT DOMAIN 59..125
FT /note="Large ribosomal subunit protein bL12 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00542"
SQ SEQUENCE 125 AA; 12738 MW; DC2E1B24C5B34EEA CRC64;
MADVKKLAEE LVNLKVTEVN ELATILKEEY GIEPAAAAVA VAAPAAGAGE AAAAEKSTFD
VILKTAGQAK LQVIKVVKDL AGLSLGDAKA LVDGAPKAVK EGVSKEEAES IKAQLEEAGA
EVELK
//
