RL7_HALEU
ID RL7_HALEU Reviewed; 123 AA.
AC P07472;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=50S ribosomal protein L7/L12 {ECO:0000255|HAMAP-Rule:MF_00368};
DE AltName: Full=Ribosomal protein 'A';
GN Name=rplL {ECO:0000255|HAMAP-Rule:MF_00368};
OS Halophilic eubacterium NRCC 41227.
OC Bacteria.
OX NCBI_TaxID=27;
RN [1]
RP PROTEIN SEQUENCE OF 2-123.
RX PubMed=3756001; DOI=10.1139/o86-093;
RA Falkenberg P., Yaguchi M., Roy C., Zuker M., Matheson A.T.;
RT "The primary structure of the ribosomal A-protein (L12) from the moderate
RT halophile NRCC 41227.";
RL Biochem. Cell Biol. 64:675-680(1986).
RN [2]
RP PROTEIN SEQUENCE OF 2-39, AND METHYLATION AT LYS-84.
RX PubMed=454666; DOI=10.1016/0005-2795(79)90128-4;
RA Falkenberg P., Yaguchi M., Rollin C.F., Matheson A.T., Wydro R.;
RT "The N-terminal sequence of the ribosomal 'A' protein from two moderate
RT halophiles, Vibrio costicola and an unidentified moderate (NRCC 11227).";
RL Biochim. Biophys. Acta 578:207-215(1979).
CC -!- FUNCTION: Seems to be the binding site for several of the factors
CC involved in protein synthesis and appears to be essential for accurate
CC translation.
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}.
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DR PIR; A24753; A24753.
DR AlphaFoldDB; P07472; -.
DR SMR; P07472; -.
DR iPTMnet; P07472; -.
DR PRIDE; P07472; -.
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; Methylation; Ribonucleoprotein;
KW Ribosomal protein.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3756001,
FT ECO:0000269|PubMed:454666"
FT CHAIN 2..123
FT /note="50S ribosomal protein L7/L12"
FT /id="PRO_0000157534"
FT REGION 94..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 84
FT /note="N6-methyllysine"
FT /evidence="ECO:0000269|PubMed:454666"
SQ SEQUENCE 123 AA; 12665 MW; F93812254C667ED1 CRC64;
MALTQEDIIN AVAEMSVMEV AELVSAMEEK FGVSAAAAVV AGPGGGEAEE AEEQTEFDLV
LTSAGEKKVN VIKVVREITG LGLKEAKAAV DGAPATLKEG MSKEDGDEAK TKLEEAGASV
ELK
