(data stored in ACNUC7421 zone)

SWISSPROT: 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   11-DEC-2019, entry version 123.
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}.
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   PDBsum; 3J9W; -.
DR   PDBsum; 5NJT; -.
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; BSU01040.
DR   GeneID; 936153; -.
DR   KEGG; bsu:BSU01040; -.
DR   PATRIC; fig|224308.179.peg.107; -.
DR   eggNOG; ENOG4108VZM; Bacteria.
DR   eggNOG; COG0244; LUCA.
DR   HOGENOM; HOG000004852; -.
DR   InParanoid; P42923; -.
DR   KO; K02864; -.
DR   OMA; VVVAHYS; -.
DR   PhylomeDB; P42923; -.
DR   BioCyc; BSUB:BSU01040-MONOMER; -.
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:0042254; P:ribosome biogenesis; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IBA:GO_Central.
DR   CDD; cd05797; Ribosomal_L10; 1.
DR   HAMAP; MF_00362; Ribosomal_L10; 1.
DR   InterPro; IPR022973; Ribosomal_L10.
DR   InterPro; IPR002363; Ribosomal_L10_eubac_CS.
DR   InterPro; IPR001790; Ribosomal_L10P.
DR   PANTHER; PTHR11560; PTHR11560; 1.
DR   Pfam; PF00466; Ribosomal_L10; 1.
DR   PROSITE; PS01109; RIBOSOMAL_L10; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P42923.
DR   SWISS-2DPAGE; P42923.
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"
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
//

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