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Database: UniProt
Entry: A0A1N6VYI9_9FIRM
LinkDB: A0A1N6VYI9_9FIRM
Original site: A0A1N6VYI9_9FIRM 
ID   A0A1N6VYI9_9FIRM        Unreviewed;       113 AA.
AC   A0A1N6VYI9;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
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=SAMN05421834_1098 {ECO:0000313|EMBL:SIQ82947.1};
OS   Halanaerobium kushneri.
OC   Bacteria; Bacillota; Clostridia; Halanaerobiales; Halanaerobiaceae;
OC   Halanaerobium.
OX   NCBI_TaxID=56779 {ECO:0000313|EMBL:SIQ82947.1, ECO:0000313|Proteomes:UP000185669};
RN   [1] {ECO:0000313|Proteomes:UP000185669}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700103 {ECO:0000313|Proteomes:UP000185669};
RA   Varghese N., Submissions S.;
RL   Submitted (JAN-2017) 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}.
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DR   EMBL; FTNC01000009; SIQ82947.1; -; Genomic_DNA.
DR   RefSeq; WP_076544732.1; NZ_FTNC01000009.1.
DR   AlphaFoldDB; A0A1N6VYI9; -.
DR   STRING; 56779.SAMN05421834_1098; -.
DR   OrthoDB; 9805969at2; -.
DR   Proteomes; UP000185669; 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   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   113 AA;  12401 MW;  6A15EEE6622BA6B6 CRC64;
     MEAKAVAKHL RITARKARLV TDLIKGKDVN TAVAILKSTP KKAAKMVEKV LNSATANAEN
     NHDMFVDDLY VKKAFVDEGP TMKRWKARAQ GSASPINKRT SHITIVLSDT KEG
//
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