ID A0A2N7WZ31_9BURK Unreviewed; 109 AA.
AC A0A2N7WZ31;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Large ribosomal subunit protein uL22 {ECO:0000256|HAMAP-Rule:MF_01331};
GN Name=rplV {ECO:0000256|HAMAP-Rule:MF_01331};
GN ORFNames=C0Z20_21560 {ECO:0000313|EMBL:PMS34637.1}, C9I57_23510
GN {ECO:0000313|EMBL:PTB18165.1};
OS Trinickia symbiotica.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Trinickia.
OX NCBI_TaxID=863227 {ECO:0000313|EMBL:PMS34637.1, ECO:0000313|Proteomes:UP000235777};
RN [1] {ECO:0000313|EMBL:PMS34637.1, ECO:0000313|Proteomes:UP000235777}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JPY 581 {ECO:0000313|EMBL:PMS34637.1,
RC ECO:0000313|Proteomes:UP000235777};
RA Estrada-de los Santos P., Palmer M., Chavez-Ramirez B., Beukes C.,
RA Steenkamp E.T., Hirsch A.M., Manyaka P., Maluk M., Lafos M., Crook M.,
RA Gross E., Simon M.F., Bueno dos Reis Junior F., Poole P.S., Venter S.N.,
RA James E.K.;
RT "Whole genome analyses suggest that Burkholderia sensu lato contains two
RT further novel genera in the rhizoxinica-symbiotica group Mycetohabitans
RT gen. nov., and Trinickia gen. nov.: implications for the evolution of
RT diazotrophy and nodulation in the Burkholderiaceae.";
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PTB18165.1, ECO:0000313|Proteomes:UP000240638}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JPY-366 {ECO:0000313|EMBL:PTB18165.1,
RC ECO:0000313|Proteomes:UP000240638};
RA Estrada De Los Santos P., Palmer M., Chavez-Ramirez B., Steenkamp E.T.,
RA Hirsch A.M., Manyaka P., Maluk M., Lafos M., Crook M., Gross E.,
RA Simon M.F., Bueno Dos Reis Junior F., Poole P.S., Venter S.N., James E.K.;
RT "Whole genome analyses suggest that Burkholderia sensu lato contains two
RT further novel genera in the rhizoxinica-symbiotica group Mycetohabitans
RT gen. nov., and Trinickia gen. nov.: implications for the evolution of
RT diazotrophy and nodulation in the Burkholderiaceae.";
RL Submitted (MAR-2018) 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 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 -!- 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:PMS34637.1}.
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DR EMBL; PNYC01000015; PMS34637.1; -; Genomic_DNA.
DR EMBL; PYUC01000013; PTB18165.1; -; Genomic_DNA.
DR RefSeq; WP_004199272.1; NZ_PYUC01000013.1.
DR AlphaFoldDB; A0A2N7WZ31; -.
DR SMR; A0A2N7WZ31; -.
DR STRING; 863227.GCA_000373005_01924; -.
DR GeneID; 84791221; -.
DR OrthoDB; 9805969at2; -.
DR Proteomes; UP000235777; Unassembled WGS sequence.
DR Proteomes; UP000240638; Unassembled WGS sequence.
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; Ribosomal protein L22/L17; 1.
DR HAMAP; MF_01331_B; Ribosomal_L22_B; 1.
DR InterPro; IPR001063; Ribosomal_uL22.
DR InterPro; IPR005727; Ribosomal_uL22_bac/chlpt-type.
DR InterPro; IPR047867; Ribosomal_uL22_bac/org-type.
DR InterPro; IPR018260; Ribosomal_uL22_CS.
DR InterPro; IPR036394; Ribosomal_uL22_sf.
DR NCBIfam; TIGR01044; rplV_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 SUPFAM; SSF54843; Ribosomal protein L22; 1.
DR PROSITE; PS00464; RIBOSOMAL_L22; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000235777};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW Rule:MF_01331};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW Rule:MF_01331};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_01331};
KW rRNA-binding {ECO:0000256|ARBA:ARBA00022730, ECO:0000256|HAMAP-
KW Rule:MF_01331}.
SQ SEQUENCE 109 AA; 11816 MW; 1338BA8B44DFC6AF CRC64;
MEVKAIHRGA RISAQKTRLV ADQIRGLPVD KALNVLTFSP KKAAGIVKKV VLSAIANAEH
NEGADIDELK IKSIYVDKAA SLKRFTARAK GRGNRIEKQS CHITVTVGN
//
