ID F5HRT3_BACIU Unreviewed; 113 AA.
AC F5HRT3; A0A0M0KV07;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 96.
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=KS08_00695 {ECO:0000313|EMBL:AIW32238.1},
GN SC09_Contig26orf00065 {ECO:0000313|EMBL:KIU10286.1};
OS Bacillus subtilis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1423 {ECO:0000313|EMBL:BAK26486.1};
RN [1] {ECO:0000313|EMBL:BAK26486.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NBRC 101246 {ECO:0000313|EMBL:BAK26494.1}, NBRC 101588
RC {ECO:0000313|EMBL:BAK26486.1}, NBRC 14415
RC {ECO:0000313|EMBL:BAK26471.1}, and NBRC 14474
RC {ECO:0000313|EMBL:BAK26478.1};
RA Hotta Y., Sato J., Sato H., Hosoda A., Tamura H.;
RT "Classification of the Genus Bacillus Based on MALDI-TOF MS Analysis of
RT Ribosomal Proteins Coded in S10 and spc Operons.";
RL J. Agric. Food Chem. 59:5222-5230(2011).
RN [2] {ECO:0000313|EMBL:AIW32238.1, ECO:0000313|Proteomes:UP000030075}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13952 {ECO:0000313|EMBL:AIW32238.1,
RC ECO:0000313|Proteomes:UP000030075};
RA Yang H., Li E., Wang X., Zhu D.;
RT "Complete genome sequence of Bacillus subtilis ATCC 13952, which exhibits
RT production of inosine.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KIU10286.1, ECO:0000313|Proteomes:UP000032247}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HM-66 {ECO:0000313|EMBL:KIU10286.1,
RC ECO:0000313|Proteomes:UP000032247};
RA Zhang H.;
RT "Comparative genome analysis of Bacillus coagulans HM-08, Clostridium
RT butyricum HM-68, Bacillus subtilis HM-66 and Bacillus licheniformis
RT BL-09.";
RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0007829|PDB:7QGU, ECO:0007829|PDB:7QH4}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.75 ANGSTROMS).
RX PubMed=35264790; DOI=10.1038/s41586-022-04416-7;
RA Saito K., Kratzat H., Campbell A., Buschauer R., Burroughs A.M.,
RA Berninghausen O., Aravind L., Green R., Beckmann R., Buskirk A.R.;
RT "Ribosome collisions induce mRNA cleavage and ribosome rescue in
RT bacteria.";
RL Nature 603:503-508(2022).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP009748; AIW32238.1; -; Genomic_DNA.
DR EMBL; AB609267; BAK26471.1; -; Genomic_DNA.
DR EMBL; AB609274; BAK26478.1; -; Genomic_DNA.
DR EMBL; AB609282; BAK26486.1; -; Genomic_DNA.
DR EMBL; AB609290; BAK26494.1; -; Genomic_DNA.
DR EMBL; JXBC01000005; KIU10286.1; -; Genomic_DNA.
DR RefSeq; WP_003156475.1; NZ_WVTC01000009.1.
DR PDB; 7QGU; EM; 4.75 A; S=1-113.
DR PDB; 7QH4; EM; 5.45 A; S=1-113.
DR EMDB; EMD-13959; -.
DR EMDB; EMD-13961; -.
DR STRING; 483913.AN935_00615; -.
DR GeneID; 76976497; -.
DR PATRIC; fig|1423.134.peg.1043; -.
DR OMA; KRIQPRA; -.
DR OrthoDB; 9805969at2; -.
DR Proteomes; UP000030075; Chromosome.
DR Proteomes; UP000032247; 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 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:7QGU, ECO:0007829|PDB:7QH4};
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; 12460 MW; 30C20D40F7C21F09 CRC64;
MQAKAVARTV RIAPRKARLV MDLIRGKQVG EAVSILNLTP RAASPIIEKV LKSAIANAEH
NYEMDANNLV ISQAFVDEGP TLKRFRPRAM GRASQINKRT SHITIVVSEK KEG
//
