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Database: UniProt
Entry: I8I5V4_9GAMM
LinkDB: I8I5V4_9GAMM
Original site: I8I5V4_9GAMM 
ID   I8I5V4_9GAMM            Unreviewed;       125 AA.
AC   I8I5V4;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=Large ribosomal subunit protein bL12 {ECO:0000256|HAMAP-Rule:MF_00368};
GN   Name=rplL {ECO:0000256|HAMAP-Rule:MF_00368};
GN   ORFNames=WQQ_20830 {ECO:0000313|EMBL:EIT71946.1};
OS   Hydrocarboniphaga effusa AP103.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Nevskiales; Nevskiaceae;
OC   Hydrocarboniphaga.
OX   NCBI_TaxID=1172194 {ECO:0000313|EMBL:EIT71946.1, ECO:0000313|Proteomes:UP000003704};
RN   [1] {ECO:0000313|EMBL:EIT71946.1, ECO:0000313|Proteomes:UP000003704}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AP103 {ECO:0000313|EMBL:EIT71946.1,
RC   ECO:0000313|Proteomes:UP000003704};
RX   PubMed=22933753; DOI=10.1128/JB.01017-12;
RA   Chang H.K., Zylstra G.J., Chae J.C.;
RT   "Genome Sequence of n-Alkane-Degrading Hydrocarboniphaga effusa Strain
RT   AP103T (ATCC BAA-332T).";
RL   J. Bacteriol. 194:5120-5120(2012).
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:EIT71946.1}.
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DR   EMBL; AKGD01000001; EIT71946.1; -; Genomic_DNA.
DR   RefSeq; WP_007185031.1; NZ_AKGD01000001.1.
DR   AlphaFoldDB; I8I5V4; -.
DR   STRING; 1172194.WQQ_20830; -.
DR   PATRIC; fig|1172194.4.peg.2019; -.
DR   OrthoDB; 9811748at2; -.
DR   Proteomes; UP000003704; 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   Reference proteome {ECO:0000313|Proteomes:UP000003704};
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;  12854 MW;  ED80D83D2A31CF82 CRC64;
     MSLSNQEILD AIAAKSVMDI VELVKAMEEK FGVSAAAPVA VAAGPAAAAA APVEEKTEFT
     VVLAAFGEKK VEVIKVVREI TGLGLKEAKD LVEGAPQTVK DGVPKADAEA IKKKLEAAGA
     KVDIK
//
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