RL10_BACSU
ID RL10_BACSU Reviewed; 166 AA.
AC P42923;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 4.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=50S ribosomal protein L10;
DE AltName: Full=BL5;
DE AltName: Full=Cold acclimatization protein;
DE Short=CAP;
DE AltName: Full=Vegetative protein 300;
DE Short=VEG300;
GN Name=rplJ; OrderedLocusNames=BSU01040;
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=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 [2]
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 [3]
RP SEQUENCE REVISION TO 52; 131 AND 144.
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 [4]
RP PROTEIN SEQUENCE OF 2-12.
RC STRAIN=168 / IS58;
RX PubMed=9298659; DOI=10.1002/elps.1150180820;
RA Antelmann H., Bernhardt J., Schmid R., Mach H., Voelker U., Hecker M.;
RT "First steps from a two-dimensional protein index towards a response-
RT regulation map for Bacillus subtilis.";
RL Electrophoresis 18:1451-1463(1997).
RN [5]
RP PROTEIN SEQUENCE OF 2-12.
RC STRAIN=168 / JH642;
RA Graumann P.L., Schmid R., Marahiel M.A.;
RL Submitted (OCT-1997) to UniProtKB.
RN [6]
RP SUBUNIT, STOICHIOMETRY, AND MASS SPECTROMETRY.
RX PubMed=15923259; DOI=10.1073/pnas.0502193102;
RA Ilag L.L., Videler H., McKay A.R., Sobott F., Fucini P., Nierhaus K.H.,
RA Robinson C.V.;
RT "Heptameric (L12)6/L10 rather than canonical pentameric complexes are found
RT by tandem MS of intact ribosomes from thermophilic bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:8192-8197(2005).
RN [7]
RP SUBUNIT, STOICHIOMETRY, AND MASS SPECTROMETRY.
RX PubMed=20467040; DOI=10.1074/mcp.m000072-mcp201;
RA Gordiyenko Y., Videler H., Zhou M., McKay A.R., Fucini P., Biegel E.,
RA Muller V., Robinson C.V.;
RT "Mass spectrometry defines the stoichiometry of ribosomal stalk complexes
RT across the phylogenetic tree.";
RL Mol. Cell. Proteomics 9:1774-1783(2010).
CC -!- FUNCTION: Forms part of the ribosomal stalk, playing a central role in
CC the interaction of the ribosome with GTP-bound translation factors
CC (such as IF-2, EF-Tu, EF-G and RF3). {ECO:0000305}.
CC -!- SUBUNIT: Part of the ribosomal stalk of the 50S ribosomal subunit. The
CC N-terminus interacts with L11 and 23S rRNA to form the base of the
CC stalk. The C-terminus forms an elongated spine to which L12 dimers bind
CC in a sequential fashion forming a pentameric L10(L12)2(L12)2 complex.
CC {ECO:0000269|PubMed:15923259, ECO:0000269|PubMed:20467040}.
CC -!- INDUCTION: In response to low temperature and salt stress.
CC -!- MASS SPECTROMETRY: Mass=68501.3; Mass_error=18.0; Method=Electrospray;
CC Note=Isolated L10(L12)4.; Evidence={ECO:0000269|PubMed:20467040};
CC -!- MASS SPECTROMETRY: Mass=17952.79; Mass_error=0.4; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:20467040};
CC -!- MASS SPECTROMETRY: Mass=68414; Mass_error=9; Method=Electrospray;
CC Note=Isolated L10(L12)4.; Evidence={ECO:0000269|PubMed:15923259};
CC -!- MASS SPECTROMETRY: Mass=17953; Mass_error=1; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:15923259};
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL10 family.
CC {ECO:0000305}.
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DR EMBL; D50303; BAA08840.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB11880.2; -; Genomic_DNA.
DR PIR; D69695; D69695.
DR RefSeq; NP_387985.2; NC_000964.3.
DR RefSeq; WP_003235042.1; NZ_JNCM01000029.1.
DR PDB; 3J9W; EM; 3.90 A; BJ=1-166.
DR PDB; 5NJT; EM; 3.80 A; b=4-126.
DR PDB; 6TNN; EM; 3.07 A; b=1-166.
DR PDB; 6TPQ; EM; 3.07 A; b=1-166.
DR PDB; 7AS8; EM; 2.90 A; L=1-166.
DR PDB; 7AS9; EM; 3.50 A; L=1-166.
DR PDB; 7O5B; EM; 3.33 A; p=1-166.
DR PDB; 7OPE; EM; 3.20 A; L=1-166.
DR PDBsum; 3J9W; -.
DR PDBsum; 5NJT; -.
DR PDBsum; 6TNN; -.
DR PDBsum; 6TPQ; -.
DR PDBsum; 7AS8; -.
DR PDBsum; 7AS9; -.
DR PDBsum; 7O5B; -.
DR PDBsum; 7OPE; -.
DR AlphaFoldDB; P42923; -.
DR SMR; P42923; -.
DR IntAct; P42923; 2.
DR MINT; P42923; -.
DR STRING; 224308.BSU01040; -.
DR jPOST; P42923; -.
DR PaxDb; P42923; -.
DR PRIDE; P42923; -.
DR EnsemblBacteria; CAB11880; CAB11880; BSU_01040.
DR GeneID; 936153; -.
DR KEGG; bsu:BSU01040; -.
DR PATRIC; fig|224308.179.peg.107; -.
DR eggNOG; COG0244; Bacteria.
DR InParanoid; P42923; -.
DR OMA; VRDQKQA; -.
DR PhylomeDB; P42923; -.
DR BioCyc; BSUB:BSU01040-MON; -.
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:0070180; F:large ribosomal subunit rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR CDD; cd05797; Ribosomal_L10; 1.
DR Gene3D; 3.30.70.1730; -; 1.
DR HAMAP; MF_00362; Ribosomal_L10; 1.
DR InterPro; IPR022973; Ribosomal_L10.
DR InterPro; IPR043141; Ribosomal_L10-like_sf.
DR InterPro; IPR002363; Ribosomal_L10_eubac_CS.
DR InterPro; IPR001790; Ribosomal_L10P.
DR PANTHER; PTHR11560; PTHR11560; 1.
DR Pfam; PF00466; Ribosomal_L10; 1.
DR SUPFAM; SSF160369; SSF160369; 1.
DR PROSITE; PS01109; RIBOSOMAL_L10; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding;
KW Stress response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9298659, ECO:0000269|Ref.5"
FT CHAIN 2..166
FT /note="50S ribosomal protein L10"
FT /id="PRO_0000154588"
FT CONFLICT 52
FT /note="F -> S (in Ref. 1; BAA08840)"
FT /evidence="ECO:0000305"
FT CONFLICT 131
FT /note="S -> P (in Ref. 1; BAA08840)"
FT /evidence="ECO:0000305"
FT CONFLICT 144
FT /note="Q -> K (in Ref. 1; BAA08840)"
FT /evidence="ECO:0000305"
FT HELIX 6..21
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 23..28
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:6TNN"
FT HELIX 35..48
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:7AS8"
FT HELIX 57..64
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:6TNN"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:6TPQ"
FT HELIX 93..103
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:6TNN"
FT STRAND 110..113
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:7AS8"
FT HELIX 120..127
FT /evidence="ECO:0007829|PDB:7AS8"
SQ SEQUENCE 166 AA; 18079 MW; 82A1D4A155C7F26A CRC64;
MSSAIETKKV VVEEIASKLK ESKSTIIVDY RGLNVSEVTE LRKQLREANV EFKVYKNTMT
RRAVEQAELN GLNDFLTGPN AIAFSTEDVV APAKVLNDFA KNHEALEIKA GVIEGKVSTV
EEVKALAELP SREGLLSMLL SVLQAPVRNL ALAAKAVAEQ KEEQGA
