RL24_BACSU
ID RL24_BACSU Reviewed; 103 AA.
AC P0CI78; P12876;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=50S ribosomal protein L24;
DE AltName: Full=12 kDa DNA-binding protein;
DE AltName: Full=BL23;
DE AltName: Full=HPB12;
GN Name=rplX; OrderedLocusNames=BSU01270;
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;
RX PubMed=2508062; DOI=10.1093/nar/17.18.7469;
RA Henkin T.M., Moon S.H., Mattheakis L.C., Nomura M.;
RT "Cloning and analysis of the spc ribosomal protein operon of Bacillus
RT subtilis: comparison with the spc operon of Escherichia coli.";
RL Nucleic Acids Res. 17:7469-7486(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / JH642;
RX PubMed=1556555; DOI=10.1099/00221287-138-1-39;
RA Sharp P.M., Nolan N.C., Ni Cholmain N., Devine K.M.;
RT "DNA sequence variability at the rplX locus of Bacillus subtilis.";
RL J. Gen. Microbiol. 138:39-45(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=8635744; DOI=10.1016/0378-1119(95)00757-1;
RA Suh J.-W., Boylan S.A., Oh S.H., Price C.W.;
RT "Genetic and transcriptional organization of the Bacillus subtilis spc-
RT alpha region.";
RL Gene 169:17-23(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]
RP PROTEIN SEQUENCE OF 3-29, AND CHARACTERIZATION OF DNA-BINDING ABILITIES.
RC STRAIN=168;
RX PubMed=8282710; DOI=10.1128/jb.176.1.50-60.1994;
RA Arnold-Schulz-Gahmen B., Salti-Montesanto V., Nguyen J., Hirschbein L.,
RA le Hegarat F.;
RT "The Bacillus subtilis nucleoid-associated protein HPB12 strongly compacts
RT DNA.";
RL J. Bacteriol. 176:50-60(1994).
RN [6]
RP SUBCELLULAR LOCATION DURING THE CELL CYCLE, AND POSSIBLE ROLE IN NUCLEOID
RP ORGANIZATION/SEGREGATION.
RX PubMed=11278078; DOI=10.1016/s0300-9084(00)01228-1;
RA Exley R., Zouine M., Pernelle J.-J., Beloin C., le Hegarat F.,
RA Deneubourg A.M.;
RT "A possible role for L24 of Bacillus subtilis in nucleoid organization and
RT segregation.";
RL Biochimie 83:269-275(2001).
RN [7] {ECO:0007744|PDB:6HA1, ECO:0007744|PDB:6HA8}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.10 ANGSTROMS) OF 1-103 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: One of two assembly initiator proteins, it binds directly to
CC the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S
CC subunit. {ECO:0000250}.
CC -!- FUNCTION: One of the proteins that surrounds the polypeptide exit
CC tunnel on the outside of the subunit. {ECO:0000250}.
CC -!- FUNCTION: Has also been isolated as a basic, heat-shock stable DNA-
CC binding protein from the B.subtilis nucleoid. It binds cooperatively to
CC double-stranded supercoiled DNA which it further compacts into
CC complexes 15-17 nm in diameter. Overexpression of the protein disrupts
CC nucleoid segregation and positioning.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit.
CC {ECO:0000269|PubMed:30126986}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11278078}.
CC Cytoplasm, nucleoid {ECO:0000269|PubMed:11278078}. Note=Is located
CC predominantly at the nucleoid poles during exponential phase, while in
CC stationary phase the protein is more evenly distributed in the whole
CC cell.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL24 family.
CC {ECO:0000305}.
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DR EMBL; X15664; CAA33702.1; -; Genomic_DNA.
DR EMBL; M81748; AAB59023.1; -; Genomic_DNA.
DR EMBL; L47971; AAB06810.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB11903.1; -; Genomic_DNA.
DR PIR; S05993; R5BS2B.
DR RefSeq; NP_388008.1; NC_000964.3.
DR RefSeq; WP_003156486.1; NZ_JNCM01000029.1.
DR PDB; 3J3V; EM; 13.30 A; U=1-103.
DR PDB; 3J3W; EM; 10.70 A; U=1-103.
DR PDB; 3J9W; EM; 3.90 A; BX=1-103.
DR PDB; 5NJT; EM; 3.80 A; n=2-101.
DR PDB; 6HA1; EM; 3.10 A; U=1-103.
DR PDB; 6HA8; EM; 3.50 A; U=1-103.
DR PDB; 6HTQ; EM; 4.50 A; U=1-101.
DR PDB; 6PPF; EM; 3.40 A; U=1-103.
DR PDB; 6PPK; EM; 4.40 A; U=1-103.
DR PDB; 6PVK; EM; 3.40 A; U=1-103.
DR PDB; 6TNN; EM; 3.07 A; n=1-103.
DR PDB; 6TPQ; EM; 3.07 A; n=1-103.
DR PDB; 7AQC; EM; 2.99 A; U=1-103.
DR PDB; 7AQD; EM; 3.10 A; U=1-103.
DR PDB; 7AS8; EM; 2.90 A; Y=1-103.
DR PDB; 7AS9; EM; 3.50 A; Y=1-103.
DR PDB; 7O5B; EM; 3.33 A; t=1-103.
DR PDB; 7OPE; EM; 3.20 A; Y=1-103.
DR PDB; 7QV1; EM; 3.50 A; U=1-103.
DR PDB; 7QV2; EM; 3.50 A; U=1-103.
DR PDB; 7QV3; EM; 5.14 A; U=1-103.
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; P0CI78; -.
DR SMR; P0CI78; -.
DR IntAct; P0CI78; 1.
DR STRING; 224308.BSU01270; -.
DR jPOST; P0CI78; -.
DR PaxDb; P0CI78; -.
DR PRIDE; P0CI78; -.
DR EnsemblBacteria; CAB11903; CAB11903; BSU_01270.
DR GeneID; 64301965; -.
DR GeneID; 66327852; -.
DR GeneID; 936799; -.
DR KEGG; bsu:BSU01270; -.
DR PATRIC; fig|224308.179.peg.130; -.
DR eggNOG; COG0198; Bacteria.
DR InParanoid; P0CI78; -.
DR OMA; HVKPTQE; -.
DR PhylomeDB; P0CI78; -.
DR PRO; PR:P0CI78; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
DR GO; GO:0009295; C:nucleoid; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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; IBA:GO_Central.
DR CDD; cd06089; KOW_RPL26; 1.
DR Gene3D; 2.30.30.30; -; 1.
DR HAMAP; MF_01326_B; Ribosomal_L24_B; 1.
DR InterPro; IPR005824; KOW.
DR InterPro; IPR041988; KOW_RPL26/RPL24.
DR InterPro; IPR014722; Rib_L2_dom2.
DR InterPro; IPR003256; Ribosomal_L24.
DR InterPro; IPR005825; Ribosomal_L24/26_CS.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR PANTHER; PTHR12903; PTHR12903; 1.
DR Pfam; PF00467; KOW; 1.
DR Pfam; PF17136; ribosomal_L24; 1.
DR SMART; SM00739; KOW; 1.
DR SUPFAM; SSF50104; SSF50104; 1.
DR TIGRFAMs; TIGR01079; rplX_bact; 1.
DR PROSITE; PS01108; RIBOSOMAL_L24; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; DNA-binding;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding;
KW rRNA-binding.
FT CHAIN 1..103
FT /note="50S ribosomal protein L24"
FT /id="PRO_0000130623"
FT CONFLICT 20
FT /note="Q -> E (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 5..7
FT /evidence="ECO:0007829|PDB:6PVK"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 13..16
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 18..21
FT /evidence="ECO:0007829|PDB:7AS9"
FT STRAND 23..27
FT /evidence="ECO:0007829|PDB:7AS8"
FT TURN 28..31
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 38..44
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:7AS8"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:7AQC"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 81..94
FT /evidence="ECO:0007829|PDB:7AS8"
FT TURN 95..98
FT /evidence="ECO:0007829|PDB:7AS8"
SQ SEQUENCE 103 AA; 11142 MW; BB635A9CBD673EF1 CRC64;
MHVKKGDKVM VISGKDKGKQ GTILAAFPKK DRVLVEGVNM VKKHSKPTQA NPQGGISNQE
APIHVSNVMP LDPKTGEVTR VGYKVEDGKK VRVAKKSGQV LDK
