ID A0A0G1VHE2_9BACT Unreviewed; 216 AA.
AC A0A0G1VHE2;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 08-NOV-2023, entry version 39.
DE RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00531, ECO:0000256|HAMAP-Rule:MF_01331};
DE Includes:
DE RecName: Full=Small ribosomal subunit protein uS19 {ECO:0000256|HAMAP-Rule:MF_00531};
DE Includes:
DE RecName: Full=Large ribosomal subunit protein uL22 {ECO:0000256|HAMAP-Rule:MF_01331};
GN Name=rplV {ECO:0000256|HAMAP-Rule:MF_01331};
GN Synonyms=rpsS {ECO:0000256|HAMAP-Rule:MF_00531};
GN ORFNames=UY05_C0076G0005 {ECO:0000313|EMBL:KKU77633.1};
OS Candidatus Peregrinibacteria bacterium GW2011_GWA2_47_7.
OC Bacteria; Candidatus Peregrinibacteria.
OX NCBI_TaxID=1619058 {ECO:0000313|EMBL:KKU77633.1, ECO:0000313|Proteomes:UP000034737};
RN [1] {ECO:0000313|EMBL:KKU77633.1, ECO:0000313|Proteomes:UP000034737}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
CC -!- FUNCTION: Protein S19 forms a complex with S13 that binds strongly to
CC the 16S ribosomal RNA. {ECO:0000256|HAMAP-Rule:MF_00531}.
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 tunnel
CC in the center of the 70S ribosome. {ECO:0000256|HAMAP-Rule:MF_01331}.
CC -!- FUNCTION: This protein binds specifically to 23S rRNA; its binding is
CC stimulated by other ribosomal proteins, e.g., L4, L17, and L20. It is
CC important during the early stages of 50S assembly. It makes multiple
CC contacts with different domains of the 23S rRNA in the assembled 50S
CC subunit and ribosome. {ECO:0000256|HAMAP-Rule:MF_01331,
CC 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 family.
CC {ECO:0000256|ARBA:ARBA00009451, ECO:0000256|HAMAP-Rule:MF_01331,
CC ECO:0000256|RuleBase:RU004005}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS19 family.
CC {ECO:0000256|ARBA:ARBA00007345, ECO:0000256|HAMAP-Rule:MF_00531,
CC ECO:0000256|RuleBase:RU003485}.
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:KKU77633.1}.
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DR EMBL; LCON01000076; KKU77633.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1VHE2; -.
DR PATRIC; fig|1619058.3.peg.746; -.
DR Proteomes; UP000034737; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0015934; C:large ribosomal subunit; IEA:InterPro.
DR GO; GO:0015935; C:small 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; Ribosomal protein L22/L17; 1.
DR HAMAP; MF_01331_B; Ribosomal_L22_B; 1.
DR HAMAP; MF_00531; Ribosomal_S19; 1.
DR InterPro; IPR001063; Ribosomal_uL22.
DR InterPro; IPR005727; Ribosomal_uL22_bac/chlpt-type.
DR InterPro; IPR047867; Ribosomal_uL22_bac/org-type.
DR InterPro; IPR036394; Ribosomal_uL22_sf.
DR InterPro; IPR002222; Ribosomal_uS19.
DR InterPro; IPR005732; Ribosomal_uS19_bac-type.
DR InterPro; IPR020934; Ribosomal_uS19_CS.
DR InterPro; IPR023575; Ribosomal_uS19_SF.
DR NCBIfam; TIGR01044; rplV_bact; 1.
DR NCBIfam; TIGR01050; rpsS_bact; 1.
DR PANTHER; PTHR13501:SF10; 50S RIBOSOMAL PROTEIN L22, CHLOROPLASTIC; 1.
DR PANTHER; PTHR13501; CHLOROPLAST 50S RIBOSOMAL PROTEIN L22-RELATED; 1.
DR Pfam; PF00237; Ribosomal_L22; 1.
DR Pfam; PF00203; Ribosomal_S19; 1.
DR PRINTS; PR00975; RIBOSOMALS19.
DR SUPFAM; SSF54843; Ribosomal protein L22; 1.
DR SUPFAM; SSF54570; Ribosomal protein S19; 1.
DR PROSITE; PS00323; RIBOSOMAL_S19; 1.
PE 3: Inferred from homology;
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW Rule:MF_00531};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW Rule:MF_00531};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_00531};
KW rRNA-binding {ECO:0000256|ARBA:ARBA00022730, ECO:0000256|HAMAP-
KW Rule:MF_00531}.
SQ SEQUENCE 216 AA; 23849 MW; AF928414D6BB573F CRC64;
MARSTKKGPY VDPKLLQKVL RAHNTNDQKI IKTWARACQI PPEFVGHTFA VHNGKIFIPV
FVSENMVGHR LGEFALTRKF KAHGGKLAKD AAAIRISPKK VNLVAGLVRR KSVLSALDYL
QFLPKGAARP LRQVILSALS NAVNNFKQDK KKLVIKSITV SSGATLHRFR PVSRGRAHPI
RKRSSHISVE LEVGTTPETT TAKNAKKIIK KASPKS
//
