(data stored in ACNUC7421 zone)

SWISSPROT: D6XVP6_BACIE

ID   D6XVP6_BACIE            Unreviewed;       113 AA.
AC   D6XVP6;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 55.
DE   RecName: Full=50S ribosomal protein L22 {ECO:0000256|HAMAP-Rule:MF_01331, ECO:0000256|RuleBase:RU004008};
GN   Name=rplV {ECO:0000256|HAMAP-Rule:MF_01331};
GN   OrderedLocusNames=Bsel_0120 {ECO:0000313|EMBL:ADH97669.1};
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:ADH97669.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH97669.1, 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: The globular domain of the protein is located near the
CC       polypeptide exit tunnel on the outside of the subunit, while an
CC       extended beta-hairpin is found that lines the wall of the exit
CC       tunnel in the center of the 70S ribosome. {ECO:0000256|HAMAP-
CC       Rule:MF_01331}.
CC   -!- FUNCTION: This protein binds specifically to 23S rRNA; its binding
CC       is stimulated by other ribosomal proteins, e.g., L4, L17, and L20.
CC       It is important during the early stages of 50S assembly. It makes
CC       multiple contacts with different domains of the 23S rRNA in the
CC       assembled 50S subunit and ribosome. {ECO:0000256|HAMAP-
CC       Rule:MF_01331, ECO:0000256|RuleBase:RU004008}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01331, ECO:0000256|RuleBase:RU004006}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL22
CC       family. {ECO:0000256|HAMAP-Rule:MF_01331,
CC       ECO:0000256|RuleBase:RU004005}.
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DR   EMBL; CP001791; ADH97669.1; -; Genomic_DNA.
DR   RefSeq; WP_013171099.1; NC_014219.1.
DR   STRING; 439292.Bsel_0120; -.
DR   EnsemblBacteria; ADH97669; ADH97669; Bsel_0120.
DR   KEGG; bse:Bsel_0120; -.
DR   eggNOG; ENOG4105KAP; Bacteria.
DR   eggNOG; COG0091; LUCA.
DR   HOGENOM; HOG000205046; -.
DR   KO; K02890; -.
DR   OMA; PQGRAHR; -.
DR   OrthoDB; 1666043at2; -.
DR   BioCyc; BSEL439292:G1GLR-144-MONOMER; -.
DR   Proteomes; UP000000271; 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:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   CDD; cd00336; Ribosomal_L22; 1.
DR   Gene3D; 3.90.470.10; -; 1.
DR   HAMAP; MF_01331_B; Ribosomal_L22_B; 1.
DR   InterPro; IPR001063; Ribosomal_L22.
DR   InterPro; IPR018260; Ribosomal_L22/L17_CS.
DR   InterPro; IPR036394; Ribosomal_L22/L17_sf.
DR   InterPro; IPR005727; Ribosomal_L22_bac/chlpt-type.
DR   PANTHER; PTHR13501; PTHR13501; 1.
DR   Pfam; PF00237; Ribosomal_L22; 1.
DR   SUPFAM; SSF54843; SSF54843; 1.
DR   TIGRFAMs; TIGR01044; rplV_bact; 1.
DR   PROSITE; PS00464; RIBOSOMAL_L22; 1.
PE   3: Inferred from homology;
DR   PRODOM; D6XVP6.
DR   SWISS-2DPAGE; D6XVP6.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000271};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000271};
KW   Ribonucleoprotein {ECO:0000256|HAMAP-Rule:MF_01331,
KW   ECO:0000256|RuleBase:RU004005};
KW   Ribosomal protein {ECO:0000256|HAMAP-Rule:MF_01331,
KW   ECO:0000256|RuleBase:RU004005, ECO:0000313|EMBL:ADH97669.1};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01331,
KW   ECO:0000256|RuleBase:RU004006};
KW   rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01331,
KW   ECO:0000256|RuleBase:RU004006}.
SQ   SEQUENCE   113 AA;  12592 MW;  C9C8911D15C33DDC CRC64;
     MEAKAVAKQV RIAPRKVRLV IDLIRGKEVG EAISILNHTP KKASPVVEKL LNSAIANAEH
     NYEMEPDNLV VSQAFVDEGV TLKRFRPRAQ GRASRINKRT SHITLVLTEK KEG
//

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