(data stored in ACNUC7421 zone)

SWISSPROT: D6XVQ1_BACIE

ID   D6XVQ1_BACIE            Unreviewed;       122 AA.
AC   D6XVQ1;
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 L14 {ECO:0000256|HAMAP-Rule:MF_01367, ECO:0000256|RuleBase:RU003950};
GN   Name=rplN {ECO:0000256|HAMAP-Rule:MF_01367};
GN   OrderedLocusNames=Bsel_0125 {ECO:0000313|EMBL:ADH97674.1};
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:ADH97674.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH97674.1, 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: Binds to 23S rRNA. Forms part of two intersubunit
CC       bridges in the 70S ribosome. {ECO:0000256|HAMAP-Rule:MF_01367,
CC       ECO:0000256|RuleBase:RU003950}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. Forms a cluster with
CC       proteins L3 and L19. In the 70S ribosome, L14 and L19 interact and
CC       together make contacts with the 16S rRNA in bridges B5 and B8.
CC       {ECO:0000256|HAMAP-Rule:MF_01367}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL14
CC       family. {ECO:0000256|HAMAP-Rule:MF_01367,
CC       ECO:0000256|RuleBase:RU003949}.
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DR   EMBL; CP001791; ADH97674.1; -; Genomic_DNA.
DR   RefSeq; WP_013171104.1; NC_014219.1.
DR   STRING; 439292.Bsel_0125; -.
DR   EnsemblBacteria; ADH97674; ADH97674; Bsel_0125.
DR   KEGG; bse:Bsel_0125; -.
DR   eggNOG; ENOG4108UNN; Bacteria.
DR   eggNOG; COG0093; LUCA.
DR   HOGENOM; HOG000183702; -.
DR   KO; K02874; -.
DR   OMA; IKGPVAR; -.
DR   OrthoDB; 1799923at2; -.
DR   BioCyc; BSEL439292:G1GLR-149-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   Gene3D; 2.40.150.20; -; 1.
DR   HAMAP; MF_01367; Ribosomal_L14; 1.
DR   InterPro; IPR036853; Ribosomal_L14_sf.
DR   InterPro; IPR000218; Ribosomal_L14P.
DR   InterPro; IPR005745; Ribosomal_L14P_bac-type.
DR   InterPro; IPR019972; Ribosomal_L14P_CS.
DR   PANTHER; PTHR11761; PTHR11761; 1.
DR   Pfam; PF00238; Ribosomal_L14; 1.
DR   SMART; SM01374; Ribosomal_L14; 1.
DR   SUPFAM; SSF50193; SSF50193; 1.
DR   TIGRFAMs; TIGR01067; rplN_bact; 1.
DR   PROSITE; PS00049; RIBOSOMAL_L14; 1.
PE   3: Inferred from homology;
DR   PRODOM; D6XVQ1.
DR   SWISS-2DPAGE; D6XVQ1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000271};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000271};
KW   Ribonucleoprotein {ECO:0000256|HAMAP-Rule:MF_01367,
KW   ECO:0000256|RuleBase:RU003949};
KW   Ribosomal protein {ECO:0000256|HAMAP-Rule:MF_01367,
KW   ECO:0000256|RuleBase:RU003949, ECO:0000313|EMBL:ADH97674.1};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01367,
KW   ECO:0000256|RuleBase:RU003950};
KW   rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01367,
KW   ECO:0000256|RuleBase:RU003950}.
SQ   SEQUENCE   122 AA;  13247 MW;  FABDA3331429F81D CRC64;
     MIQQESRLKV ADNSGAREVQ CIKVLGGTGR KTANIGDVIV CSVKQATPGG VVKKGEVVRA
     VIVRSKSGMR RKDGSYIRFD ENAAVIVRPD KGPRGTRIFG PVARELRDNQ FMKIVSLAPE
     VL
//

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