(data stored in SCRATCH zone)

SWISSPROT: D6XVN0_BACIE

ID   D6XVN0_BACIE            Unreviewed;       121 AA.
AC   D6XVN0;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 60.
DE   RecName: Full=50S ribosomal protein L7/L12 {ECO:0000256|HAMAP-Rule:MF_00368};
GN   Name=rplL {ECO:0000256|HAMAP-Rule:MF_00368};
GN   OrderedLocusNames=Bsel_0104 {ECO:0000313|EMBL:ADH97653.1};
OS   Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae;
OC   unclassified Sporolactobacillaceae.
OX   NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH97653.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH97653.1, ECO:0000313|Proteomes:UP000000271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC   {ECO:0000313|Proteomes:UP000000271};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Stolz J.;
RT   "Complete sequence of Bacillus selenitireducens MLS10.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Forms part of the ribosomal stalk which helps the
CC       ribosome interact with GTP-bound translation factors. Is thus
CC       essential for accurate translation. {ECO:0000256|HAMAP-
CC       Rule:MF_00368}.
CC   -!- SUBUNIT: Homodimer. Part of the ribosomal stalk of the 50S
CC       ribosomal subunit. Forms a multimeric L10(L12)X complex, where L10
CC       forms an elongated spine to which 2 to 4 L12 dimers bind in a
CC       sequential fashion. Binds GTP-bound translation factors.
CC       {ECO:0000256|HAMAP-Rule:MF_00368}.
CC   -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL12
CC       family. {ECO:0000256|HAMAP-Rule:MF_00368}.
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DR   EMBL; CP001791; ADH97653.1; -; Genomic_DNA.
DR   RefSeq; WP_013171083.1; NC_014219.1.
DR   STRING; 439292.Bsel_0104; -.
DR   EnsemblBacteria; ADH97653; ADH97653; Bsel_0104.
DR   KEGG; bse:Bsel_0104; -.
DR   eggNOG; ENOG4105KBC; Bacteria.
DR   eggNOG; COG0222; LUCA.
DR   HOGENOM; HOG000248813; -.
DR   KO; K02935; -.
DR   OMA; VDNAPKP; -.
DR   OrthoDB; 1822695at2; -.
DR   BioCyc; BSEL439292:G1GLR-128-MONOMER; -.
DR   Proteomes; UP000000271; Chromosome.
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   Pfam; PF00542; Ribosomal_L12; 1.
DR   Pfam; PF16320; Ribosomal_L12_N; 1.
DR   ProDom; PD001326; Ribosomal_L7/L12_C; 1.
DR   SUPFAM; SSF48300; SSF48300; 1.
DR   SUPFAM; SSF54736; SSF54736; 1.
DR   TIGRFAMs; TIGR00855; L12; 1.
PE   3: Inferred from homology;
DR   PRODOM; D6XVN0.
DR   SWISS-2DPAGE; D6XVN0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000271};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000271};
KW   Ribonucleoprotein {ECO:0000256|HAMAP-Rule:MF_00368};
KW   Ribosomal protein {ECO:0000256|HAMAP-Rule:MF_00368,
KW   ECO:0000313|EMBL:ADH97653.1}.
FT   DOMAIN        3     48       Ribosomal_L12_N. {ECO:0000259|Pfam:
FT                                PF16320}.
FT   DOMAIN       55    121       Ribosomal_L12. {ECO:0000259|Pfam:
FT                                PF00542}.
SQ   SEQUENCE   121 AA;  12400 MW;  0815BC511680E896 CRC64;
     MTHQDMIAAI KEMSVLELND LVKAIEEEFG VTAAAPVAAA GAGAGEEAAA EQTEFDVVLE
     SAGSSKIGVI KIVREITGLG LKDAKALVDG VPAPVKEGVE KAEAEEIKGK LEEAGASVEL
     K
//

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