RL7_HALPR
ID RL7_HALPR Reviewed; 122 AA.
AC P14134;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=50S ribosomal protein L7/L12 {ECO:0000255|HAMAP-Rule:MF_00368};
GN Name=rplL {ECO:0000255|HAMAP-Rule:MF_00368};
OS Halanaerobium praevalens.
OC Bacteria; Firmicutes; Clostridia; Halanaerobiales; Halanaerobiaceae;
OC Halanaerobium.
OX NCBI_TaxID=2331;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=3126821; DOI=10.1016/0300-9084(87)90001-0;
RA Matheson A.T., Louie K.A., Tak B.D., Zuker M.;
RT "The primary structure of the ribosomal A-protein (L12) from the halophilic
RT eubacterium Haloanaerobium praevalens.";
RL Biochimie 69:1013-1020(1987).
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:0000255|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:0000255|HAMAP-
CC Rule:MF_00368}.
CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL12 family.
CC {ECO:0000255|HAMAP-Rule:MF_00368}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR PIR; S06332; R5HG12.
DR AlphaFoldDB; P14134; -.
DR SMR; P14134; -.
DR PRIDE; P14134; -.
DR OMA; LEDKWGV; -.
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; 1.20.5.710; -; 1.
DR Gene3D; 3.30.1390.10; -; 1.
DR HAMAP; MF_00368; Ribosomal_L7_L12; 1.
DR InterPro; IPR000206; Ribosomal_L7/12.
DR InterPro; IPR014719; Ribosomal_L7/12_C/ClpS-like.
DR InterPro; IPR013823; Ribosomal_L7/L12_C.
DR InterPro; IPR008932; Ribosomal_L7/L12_oligo.
DR InterPro; IPR036235; Ribosomal_L7/L12_oligo_N_sf.
DR PANTHER; PTHR45987; PTHR45987; 1.
DR Pfam; PF00542; Ribosomal_L12; 1.
DR Pfam; PF16320; Ribosomal_L12_N; 1.
DR SUPFAM; SSF48300; SSF48300; 1.
DR SUPFAM; SSF54736; SSF54736; 1.
DR TIGRFAMs; TIGR00855; L12; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1..122
FT /note="50S ribosomal protein L7/L12"
FT /id="PRO_0000157535"
FT REGION 94..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..122
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 122 AA; 12705 MW; 8D05EA496A5CB21D CRC64;
MNKEEIMSAI EEMSVLELSE LVEDLEEKFG VSAAAPVAVA GGAAGAGAAA EEKSEFDVFL
ADIGGKKIKV IKAVRELTGL GLKEAKGVVD DAPGNVKEGL SKEDAEEMKE KLEEAGATVE
LK