RL22_BACSU
ID RL22_BACSU Reviewed; 113 AA.
AC P42060;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=50S ribosomal protein L22 {ECO:0000255|HAMAP-Rule:MF_01331};
GN Name=rplV {ECO:0000255|HAMAP-Rule:MF_01331}; OrderedLocusNames=BSU01210;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RA Bischof O., Wittmann-Liebold B., Kruft V.;
RL Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SG38;
RX PubMed=9371452; DOI=10.1128/jb.179.22.7046-7054.1997;
RA Li X., Lindahl L., Sha Y., Zengel J.M.;
RT "Analysis of the Bacillus subtilis S10 ribosomal protein gene cluster
RT identifies two promoters that may be responsible for transcription of the
RT entire 15-kilobase S10-spc-alpha cluster.";
RL J. Bacteriol. 179:7046-7054(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8969501; DOI=10.1099/13500872-142-11-3039;
RA Yasumoto K., Liu H., Jeong S.M., Ohashi Y., Kakinuma S., Tanaka K.,
RA Kawamura F., Yoshikawa H., Takahashi H.;
RT "Sequence analysis of a 50 kb region between spo0H and rrnH on the Bacillus
RT subtilis chromosome.";
RL Microbiology 142:3039-3046(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [5] {ECO:0007744|PDB:6HA1, ECO:0007744|PDB:6HA8}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.10 ANGSTROMS) OF 1-113 WITH AND WITHOUT
RP VIRGINIAMYCIN M, AND SUBUNIT.
RX PubMed=30126986; DOI=10.1073/pnas.1808535115;
RA Crowe-McAuliffe C., Graf M., Huter P., Takada H., Abdelshahid M.,
RA Novacek J., Murina V., Atkinson G.C., Hauryliuk V., Wilson D.N.;
RT "Structural basis for antibiotic resistance mediated by the Bacillus
RT subtilis ABCF ATPase VmlR.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:8978-8983(2018).
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 (By similarity). {ECO:0000255|HAMAP-
CC Rule:MF_01331}.
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:0000255|HAMAP-Rule:MF_01331}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit.
CC {ECO:0000269|PubMed:30126986}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL22 family.
CC {ECO:0000255|HAMAP-Rule:MF_01331}.
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DR EMBL; Z47978; CAA88014.1; -; Genomic_DNA.
DR EMBL; U43929; AAC45961.1; -; Genomic_DNA.
DR EMBL; D50303; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; D50302; BAA08836.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB11897.1; -; Genomic_DNA.
DR PIR; H69696; H69696.
DR RefSeq; NP_388002.1; NC_000964.3.
DR RefSeq; WP_003156475.1; NZ_JNCM01000029.1.
DR PDB; 3J3V; EM; 13.30 A; S=1-113.
DR PDB; 3J3W; EM; 10.70 A; S=1-113.
DR PDB; 3J9W; EM; 3.90 A; BV=1-113.
DR PDB; 5NJT; EM; 3.80 A; l=2-110.
DR PDB; 6HA1; EM; 3.10 A; S=1-113.
DR PDB; 6HA8; EM; 3.50 A; S=1-113.
DR PDB; 6HTQ; EM; 4.50 A; S=2-110.
DR PDB; 6PPF; EM; 3.40 A; S=1-113.
DR PDB; 6PPK; EM; 4.40 A; S=1-113.
DR PDB; 6PVK; EM; 3.40 A; S=1-113.
DR PDB; 6TNN; EM; 3.07 A; l=1-113.
DR PDB; 6TPQ; EM; 3.07 A; l=1-113.
DR PDB; 7AQC; EM; 2.99 A; S=1-113.
DR PDB; 7AQD; EM; 3.10 A; S=1-113.
DR PDB; 7AS8; EM; 2.90 A; W=1-113.
DR PDB; 7AS9; EM; 3.50 A; W=1-113.
DR PDB; 7O5B; EM; 3.33 A; r=1-113.
DR PDB; 7OPE; EM; 3.20 A; W=1-113.
DR PDB; 7QV1; EM; 3.50 A; S=1-113.
DR PDB; 7QV2; EM; 3.50 A; S=1-113.
DR PDB; 7QV3; EM; 5.14 A; S=1-113.
DR PDBsum; 3J3V; -.
DR PDBsum; 3J3W; -.
DR PDBsum; 3J9W; -.
DR PDBsum; 5NJT; -.
DR PDBsum; 6HA1; -.
DR PDBsum; 6HA8; -.
DR PDBsum; 6HTQ; -.
DR PDBsum; 6PPF; -.
DR PDBsum; 6PPK; -.
DR PDBsum; 6PVK; -.
DR PDBsum; 6TNN; -.
DR PDBsum; 6TPQ; -.
DR PDBsum; 7AQC; -.
DR PDBsum; 7AQD; -.
DR PDBsum; 7AS8; -.
DR PDBsum; 7AS9; -.
DR PDBsum; 7O5B; -.
DR PDBsum; 7OPE; -.
DR PDBsum; 7QV1; -.
DR PDBsum; 7QV2; -.
DR PDBsum; 7QV3; -.
DR AlphaFoldDB; P42060; -.
DR SMR; P42060; -.
DR IntAct; P42060; 1.
DR STRING; 224308.BSU01210; -.
DR jPOST; P42060; -.
DR PaxDb; P42060; -.
DR PRIDE; P42060; -.
DR EnsemblBacteria; CAB11897; CAB11897; BSU_01210.
DR GeneID; 66327858; -.
DR GeneID; 938123; -.
DR KEGG; bsu:BSU01210; -.
DR PATRIC; fig|224308.179.peg.124; -.
DR eggNOG; COG0091; Bacteria.
DR InParanoid; P42060; -.
DR OMA; KRIQPRA; -.
DR PhylomeDB; P42060; -.
DR BioCyc; BSUB:BSU01210-MON; -.
DR PRO; PR:P42060; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
DR GO; GO:0015934; C:large ribosomal subunit; IBA:GO_Central.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0042255; P:ribosome assembly; IBA:GO_Central.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR CDD; cd00336; Ribosomal_L22; 1.
DR Gene3D; 3.90.470.10; -; 1.
DR HAMAP; MF_01331_B; Ribosomal_L22_B; 1.
DR InterPro; IPR001063; Ribosomal_L22.
DR InterPro; IPR018260; Ribosomal_L22/L17_CS.
DR InterPro; IPR036394; Ribosomal_L22/L17_sf.
DR InterPro; IPR005727; Ribosomal_L22_bac/chlpt-type.
DR PANTHER; PTHR13501; PTHR13501; 1.
DR Pfam; PF00237; Ribosomal_L22; 1.
DR SUPFAM; SSF54843; SSF54843; 1.
DR TIGRFAMs; TIGR01044; rplV_bact; 1.
DR PROSITE; PS00464; RIBOSOMAL_L22; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding; rRNA-binding.
FT CHAIN 1..113
FT /note="50S ribosomal protein L22"
FT /id="PRO_0000125119"
FT CONFLICT 35
FT /note="I -> N (in Ref. 1; CAA88014)"
FT /evidence="ECO:0000305"
FT CONFLICT 41..42
FT /note="RA -> IS (in Ref. 1; CAA88014)"
FT /evidence="ECO:0000305"
FT CONFLICT 85
FT /note="F -> L (in Ref. 1; CAA88014)"
FT /evidence="ECO:0000305"
FT CONFLICT 105
FT /note="I -> V (in Ref. 1; CAA88014)"
FT /evidence="ECO:0000305"
FT STRAND 3..12
FT /evidence="ECO:0007829|PDB:7AS8"
FT HELIX 14..24
FT /evidence="ECO:0007829|PDB:7AS8"
FT HELIX 29..38
FT /evidence="ECO:0007829|PDB:7AS8"
FT HELIX 44..61
FT /evidence="ECO:0007829|PDB:7AS8"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 69..78
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:7AS8"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:6TNN"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 101..109
FT /evidence="ECO:0007829|PDB:7AS8"
SQ SEQUENCE 113 AA; 12460 MW; 30C20D40F7C21F09 CRC64;
MQAKAVARTV RIAPRKARLV MDLIRGKQVG EAVSILNLTP RAASPIIEKV LKSAIANAEH
NYEMDANNLV ISQAFVDEGP TLKRFRPRAM GRASQINKRT SHITIVVSEK KEG
