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Database: UniProt
Entry: A0A0P8C483_9CYAN
LinkDB: A0A0P8C483_9CYAN
Original site: A0A0P8C483_9CYAN 
ID   A0A0P8C483_9CYAN        Unreviewed;       128 AA.
AC   A0A0P8C483;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
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:KPQ36389.1};
GN   Synonyms=rpl12 {ECO:0000256|HAMAP-Rule:MF_00368};
GN   ORFNames=HLUCCA11_05880 {ECO:0000313|EMBL:KPQ36389.1};
OS   Phormidesmis priestleyi Ana.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC   Phormidesmis.
OX   NCBI_TaxID=1666911 {ECO:0000313|EMBL:KPQ36389.1, ECO:0000313|Proteomes:UP000050465};
RN   [1] {ECO:0000313|EMBL:KPQ36389.1, ECO:0000313|Proteomes:UP000050465}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ana {ECO:0000313|EMBL:KPQ36389.1};
RA   Nelson W.C., Romine M.F., Lindemann S.R.;
RT   "Identification and resolution of microdiversity through metagenomic
RT   sequencing of parallel consortia.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KPQ36389.1}.
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DR   EMBL; LJZR01000006; KPQ36389.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P8C483; -.
DR   STRING; 1666911.HLUCCA11_05880; -.
DR   PATRIC; fig|1666911.3.peg.5097; -.
DR   Proteomes; UP000050465; Unassembled WGS sequence.
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          61..128
FT                   /note="Large ribosomal subunit protein bL12 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00542"
SQ   SEQUENCE   128 AA;  13187 MW;  112A4C4F1F27CEA4 CRC64;
     MSAATDEILE KLKTLSLLEA SELVSQIEEA FGVSAAAPVG GMMMAAGGGG AAEEVEEKTE
     FDVVLDEVPG DKKIAILKVV RTMTGLGLKE AKGMVESAPV TVKEAIPKDA AEEAKKALED
     AGAKVTVK
//
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