RL1_BACSU
ID RL1_BACSU Reviewed; 232 AA.
AC Q06797;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 4.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=50S ribosomal protein L1 {ECO:0000255|HAMAP-Rule:MF_01318};
DE Short=BL1;
GN Name=rplA {ECO:0000255|HAMAP-Rule:MF_01318}; OrderedLocusNames=BSU01030;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
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 [2]
RP SEQUENCE REVISION TO 17; 53 AND 56.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-203.
RX PubMed=7968510; DOI=10.1111/j.1365-2958.1993.tb00910.x;
RA Jeong S., Yoshikawa H., Takahashi H.;
RT "Isolation and characterization of the secE homologue gene of Bacillus
RT subtilis.";
RL Mol. Microbiol. 10:133-142(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 203-232.
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 [5]
RP INTERACTION WITH CSHA, AND SUBUNIT.
RC STRAIN=168;
RX PubMed=23175651; DOI=10.1128/jb.01475-12;
RA Lehnik-Habrink M., Rempeters L., Kovacs A.T., Wrede C., Baierlein C.,
RA Krebber H., Kuipers O.P., Stulke J.;
RT "DEAD-box RNA helicases in Bacillus subtilis have multiple functions and
RT act independently from each other.";
RL J. Bacteriol. 195:534-544(2013).
RN [6] {ECO:0007744|PDB:6HA8}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS) OF 1-232 WITH
RP VIRGINIAMYCIN M, INTERACTION WITH VMLR, 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: Binds directly to 23S rRNA. The L1 stalk is quite mobile in
CC the ribosome, and is involved in E site tRNA release.
CC {ECO:0000255|HAMAP-Rule:MF_01318}.
CC -!- FUNCTION: Protein L1 is also a translational repressor protein, it
CC controls the translation of the L11 operon by binding to its mRNA.
CC {ECO:0000255|HAMAP-Rule:MF_01318}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit (PubMed:30126986). Interacts
CC with RNA helicase CshA (PubMed:23175651). Interacts with VmlR
CC (PubMed:30126986). {ECO:0000269|PubMed:23175651,
CC ECO:0000269|PubMed:30126986}.
CC -!- INTERACTION:
CC Q06797; P38424: engB; NbExp=3; IntAct=EBI-6401093, EBI-6401087;
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL1 family.
CC {ECO:0000255|HAMAP-Rule:MF_01318}.
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DR EMBL; AL009126; CAB11879.2; -; Genomic_DNA.
DR EMBL; D13303; BAA02562.1; -; Genomic_DNA.
DR EMBL; D50303; BAA08839.1; -; Genomic_DNA.
DR PIR; E69694; E69694.
DR RefSeq; NP_387984.2; NC_000964.3.
DR RefSeq; WP_003235040.1; NZ_JNCM01000029.1.
DR PDB; 3J3V; EM; 13.30 A; 5=1-232.
DR PDB; 3J3W; EM; 10.70 A; 5=1-232.
DR PDB; 6HA8; EM; 3.50 A; 8=1-232.
DR PDBsum; 3J3V; -.
DR PDBsum; 3J3W; -.
DR PDBsum; 6HA8; -.
DR AlphaFoldDB; Q06797; -.
DR SMR; Q06797; -.
DR IntAct; Q06797; 3.
DR MINT; Q06797; -.
DR STRING; 224308.BSU01030; -.
DR jPOST; Q06797; -.
DR PaxDb; Q06797; -.
DR PRIDE; Q06797; -.
DR EnsemblBacteria; CAB11879; CAB11879; BSU_01030.
DR GeneID; 936843; -.
DR KEGG; bsu:BSU01030; -.
DR PATRIC; fig|224308.179.peg.106; -.
DR eggNOG; COG0081; Bacteria.
DR InParanoid; Q06797; -.
DR OMA; GWTDVDV; -.
DR PhylomeDB; Q06797; -.
DR BioCyc; BSUB:BSU01030-MON; -.
DR PRO; PR:Q06797; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000470; P:maturation of LSU-rRNA; IBA:GO_Central.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR CDD; cd00403; Ribosomal_L1; 1.
DR Gene3D; 3.40.50.790; -; 1.
DR HAMAP; MF_01318_B; Ribosomal_L1_B; 1.
DR InterPro; IPR005878; Ribosom_L1_bac-type.
DR InterPro; IPR002143; Ribosomal_L1.
DR InterPro; IPR023674; Ribosomal_L1-like.
DR InterPro; IPR028364; Ribosomal_L1/biogenesis.
DR InterPro; IPR016095; Ribosomal_L1_3-a/b-sand.
DR InterPro; IPR023673; Ribosomal_L1_CS.
DR Pfam; PF00687; Ribosomal_L1; 1.
DR PIRSF; PIRSF002155; Ribosomal_L1; 1.
DR SUPFAM; SSF56808; SSF56808; 1.
DR TIGRFAMs; TIGR01169; rplA_bact; 1.
DR PROSITE; PS01199; RIBOSOMAL_L1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Repressor; Ribonucleoprotein;
KW Ribosomal protein; RNA-binding; rRNA-binding; Translation regulation;
KW tRNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..232
FT /note="50S ribosomal protein L1"
FT /id="PRO_0000125616"
FT CONFLICT 17
FT /note="R -> H (in Ref. 2; BAA02562)"
FT /evidence="ECO:0000305"
FT CONFLICT 53
FT /note="R -> S (in Ref. 2; BAA02562)"
FT /evidence="ECO:0000305"
FT CONFLICT 56
FT /note="D -> H (in Ref. 2; BAA02562)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 232 AA; 24989 MW; FE3880DD4E25AB43 CRC64;
MAKKGKKYVE AAKLVDRSKA YDVSEAVALV KKTNTAKFDA TVEVAFRLGV DPRKNDQQIR
GAVVLPNGTG KTQRVLVFAK GEKAKEAEAA GADFVGDTDY INKIQQGWFD FDVIVATPDM
MGEVGKIGRV LGPKGLMPNP KTGTVTFEVE KAIGEIKAGK VEYRVDKAGN IHVPIGKVSF
EDEKLVENFT TMYDTILKAK PAAAKGVYVK NVAVTSTMGP GVKVDSSTFN VK
