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Database: UniProt
Entry: RL1_DESAH
LinkDB: RL1_DESAH
Original site: RL1_DESAH 
ID   RL1_DESAH               Reviewed;         230 AA.
AC   C0Q9Y2;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=Large ribosomal subunit protein uL1 {ECO:0000255|HAMAP-Rule:MF_01318};
DE   AltName: Full=50S ribosomal protein L1 {ECO:0000305};
GN   Name=rplA {ECO:0000255|HAMAP-Rule:MF_01318}; OrderedLocusNames=HRM2_36350;
OS   Desulforapulum autotrophicum (strain ATCC 43914 / DSM 3382 / VKM B-1955 /
OS   HRM2) (Desulfobacterium autotrophicum).
OC   Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC   Desulfobacteraceae; Desulforapulum.
OX   NCBI_TaxID=177437;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43914 / DSM 3382 / VKM B-1955 / HRM2;
RX   PubMed=19187283; DOI=10.1111/j.1462-2920.2008.01825.x;
RA   Strittmatter A.W., Liesegang H., Rabus R., Decker I., Amann J., Andres S.,
RA   Henne A., Fricke W.F., Martinez-Arias R., Bartels D., Goesmann A.,
RA   Krause L., Puehler A., Klenk H.P., Richter M., Schuler M., Gloeckner F.O.,
RA   Meyerdierks A., Gottschalk G., Amann R.;
RT   "Genome sequence of Desulfobacterium autotrophicum HRM2, a marine sulfate
RT   reducer oxidizing organic carbon completely to carbon dioxide.";
RL   Environ. Microbiol. 11:1038-1055(2009).
CC   -!- FUNCTION: Binds directly to 23S rRNA. The L1 stalk is quite mobile in
CC       the ribosome, and is involved in E site tRNA release.
CC       {ECO:0000255|HAMAP-Rule:MF_01318}.
CC   -!- FUNCTION: Protein L1 is also a translational repressor protein, it
CC       controls the translation of the L11 operon by binding to its mRNA.
CC       {ECO:0000255|HAMAP-Rule:MF_01318}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01318}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL1 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01318}.
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DR   EMBL; CP001087; ACN16700.1; -; Genomic_DNA.
DR   RefSeq; WP_015905450.1; NC_012108.1.
DR   AlphaFoldDB; C0Q9Y2; -.
DR   SMR; C0Q9Y2; -.
DR   STRING; 177437.HRM2_36350; -.
DR   KEGG; dat:HRM2_36350; -.
DR   eggNOG; COG0081; Bacteria.
DR   HOGENOM; CLU_062853_0_0_7; -.
DR   OrthoDB; 9803740at2; -.
DR   Proteomes; UP000000442; Chromosome.
DR   GO; GO:0015934; C:large ribosomal subunit; IEA:InterPro.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   CDD; cd00403; Ribosomal_L1; 1.
DR   Gene3D; 3.30.190.20; -; 1.
DR   Gene3D; 3.40.50.790; -; 1.
DR   HAMAP; MF_01318_B; Ribosomal_uL1_B; 1.
DR   InterPro; IPR005878; Ribosom_uL1_bac-type.
DR   InterPro; IPR002143; Ribosomal_uL1.
DR   InterPro; IPR023674; Ribosomal_uL1-like.
DR   InterPro; IPR028364; Ribosomal_uL1/biogenesis.
DR   InterPro; IPR016095; Ribosomal_uL1_3-a/b-sand.
DR   InterPro; IPR023673; Ribosomal_uL1_CS.
DR   NCBIfam; TIGR01169; rplA_bact; 1.
DR   PANTHER; PTHR36427:SF3; 39S RIBOSOMAL PROTEIN L1, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR36427; 54S RIBOSOMAL PROTEIN L1, MITOCHONDRIAL; 1.
DR   Pfam; PF00687; Ribosomal_L1; 1.
DR   PIRSF; PIRSF002155; Ribosomal_L1; 1.
DR   SUPFAM; SSF56808; Ribosomal protein L1; 1.
DR   PROSITE; PS01199; RIBOSOMAL_L1; 1.
PE   3: Inferred from homology;
KW   Reference proteome; Repressor; Ribonucleoprotein; Ribosomal protein;
KW   RNA-binding; rRNA-binding; Translation regulation; tRNA-binding.
FT   CHAIN           1..230
FT                   /note="Large ribosomal subunit protein uL1"
FT                   /id="PRO_1000214417"
SQ   SEQUENCE   230 AA;  24917 MW;  D8613A9040F1FA41 CRC64;
     MPKHGKKYTE MSKKIDKQAR YDFNEALELS LASSYVKFDE TVDIAVRLGV DPRHADQMVR
     GTVALPNGLG KEVKVLVFAK GEKEKEALDA GADFIADEET VAKIKDGWFG FDKAIATPDM
     MGTVGKLGRV LGPRGLMPNA KTGTVTFDVA KAVEELKAGK IDFRVEKAGI IHVPVGKVSF
     GPEKLVENVK AFINMIIALK PASSKGTYLK TITVSTTMGP GVKIDPMFTK
//
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