(data stored in ACNUC7421 zone)

SWISSPROT: 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   11-DEC-2019, entry version 118.
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).
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   -!- SIMILARITY: Belongs to the universal ribosomal protein uL22 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01331}.
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   PDBsum; 3J3V; -.
DR   PDBsum; 3J3W; -.
DR   PDBsum; 3J9W; -.
DR   PDBsum; 5NJT; -.
DR   PDBsum; 6HA1; -.
DR   PDBsum; 6HA8; -.
DR   SMR; P42060; -.
DR   STRING; 224308.BSU01210; -.
DR   jPOST; P42060; -.
DR   PaxDb; P42060; -.
DR   PRIDE; P42060; -.
DR   EnsemblBacteria; CAB11897; CAB11897; BSU01210.
DR   GeneID; 938123; -.
DR   GeneID; 9780022; -.
DR   KEGG; bsu:BSU01210; -.
DR   PATRIC; fig|224308.179.peg.124; -.
DR   eggNOG; ENOG4105KAP; Bacteria.
DR   eggNOG; COG0091; LUCA.
DR   HOGENOM; HOG000205046; -.
DR   InParanoid; P42060; -.
DR   KO; K02890; -.
DR   OMA; KRIQPRA; -.
DR   PhylomeDB; P42060; -.
DR   BioCyc; BSUB:BSU01210-MONOMER; -.
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;
DR   PRODOM; P42060.
DR   SWISS-2DPAGE; P42060.
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"
SQ   SEQUENCE   113 AA;  12460 MW;  30C20D40F7C21F09 CRC64;
     MQAKAVARTV RIAPRKARLV MDLIRGKQVG EAVSILNLTP RAASPIIEKV LKSAIANAEH
     NYEMDANNLV ISQAFVDEGP TLKRFRPRAM GRASQINKRT SHITIVVSEK KEG
//

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