(data stored in SCRATCH zone)

SWISSPROT: RL7_BACSU

ID   RL7_BACSU               Reviewed;         123 AA.
AC   P02394;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   11-DEC-2019, entry version 146.
DE   RecName: Full=50S ribosomal protein L7/L12 {ECO:0000255|HAMAP-Rule:MF_00368};
DE   AltName: Full=BL9;
DE   AltName: Full=Vegetative protein 341;
DE            Short=VEG341;
GN   Name=rplL {ECO:0000255|HAMAP-Rule:MF_00368}; OrderedLocusNames=BSU01050;
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   PRELIMINARY PROTEIN SEQUENCE OF 2-123.
RX   PubMed=103754; DOI=10.1016/0014-5793(78)80445-1;
RA   Itoh T., Wittmann-Liebold B.;
RT   "The primary structure of Bacillus subtilis acidic ribosomal protein B-L9
RT   and its comparison with Escherichia coli proteins L7/L12.";
RL   FEBS Lett. 96:392-394(1978).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-123.
RC   STRAIN=ATCC 6633 / PCI 219 / NRS 231;
RX   PubMed=6771249;
RA   Itoh T., Wittmann-Liebold B.;
RT   "The primary structure of Bacillus subtilis acidic ribonsomal protein B-L9.
RT   Isolation and characterization of peptides and the complete amino acid
RT   sequence.";
RL   J. Biochem. 87:1185-1201(1980).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-85.
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 76-123.
RC   STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC   3610 / VKM B-501;
RX   PubMed=7657605; DOI=10.1074/jbc.270.35.20329;
RA   Boor K.J., Duncan M.L., Price C.W.;
RT   "Genetic and transcriptional organization of the region encoding the beta
RT   subunit of Bacillus subtilis RNA polymerase.";
RL   J. Biol. Chem. 270:20329-20336(1995).
RN   [6]
RP   PROTEIN SEQUENCE OF 2-31.
RC   STRAIN=168 / JH642;
RX   PubMed=8755892; DOI=10.1128/jb.178.15.4611-4619.1996;
RA   Graumann P., Schroeder K., Schmid R., Marahiel M.A.;
RT   "Cold shock stress-induced proteins in Bacillus subtilis.";
RL   J. Bacteriol. 178:4611-4619(1996).
RN   [7]
RP   PROTEIN SEQUENCE OF 2-27.
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   [8]
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   [9]
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 which helps the ribosome
CC       interact with GTP-bound translation factors. Is thus essential for
CC       accurate translation. {ECO:0000255|HAMAP-Rule:MF_00368}.
CC   -!- SUBUNIT: Homodimer. Part of the 50S ribosomal subunit; present in 4
CC       copies per ribosome. Forms part of the ribosomal stalk which helps the
CC       ribosome interact with GTP-bound translation factors. Forms a
CC       pentameric L10(L12)2(L12)2 complex, where L10 forms an elongated spine
CC       to which 2 L12 dimers bind in a sequential fashion.
CC       {ECO:0000269|PubMed:15923259, ECO:0000269|PubMed:20467040}.
CC   -!- INTERACTION:
CC       P38424:engB; NbExp=2; IntAct=EBI-6401150, EBI-6401087;
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=12623.1; Mass_error=0.15; 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=12623; Mass_error=1; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:15923259};
CC   -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL12 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00368}.
DR   EMBL; AL009126; CAB11881.1; -; Genomic_DNA.
DR   EMBL; D50303; BAA08841.1; -; Genomic_DNA.
DR   EMBL; L24376; AAB00970.1; -; Genomic_DNA.
DR   PIR; F69695; R5BS9.
DR   RefSeq; NP_387986.1; NC_000964.3.
DR   RefSeq; WP_003156436.1; NZ_JNCM01000029.1.
DR   SMR; P02394; -.
DR   IntAct; P02394; 2.
DR   MINT; P02394; -.
DR   STRING; 224308.BSU01050; -.
DR   jPOST; P02394; -.
DR   PaxDb; P02394; -.
DR   PRIDE; P02394; -.
DR   EnsemblBacteria; CAB11881; CAB11881; BSU01050.
DR   GeneID; 935952; -.
DR   GeneID; 9779972; -.
DR   KEGG; bsu:BSU01050; -.
DR   PATRIC; fig|224308.179.peg.108; -.
DR   eggNOG; ENOG4105KBC; Bacteria.
DR   eggNOG; COG0222; LUCA.
DR   HOGENOM; HOG000248813; -.
DR   InParanoid; P02394; -.
DR   KO; K02935; -.
DR   OMA; VDNAPKP; -.
DR   PhylomeDB; P02394; -.
DR   BioCyc; BSUB:BSU01050-MONOMER; -.
DR   PRO; PR:P02394; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   CDD; cd00387; Ribosomal_L7_L12; 1.
DR   Gene3D; 1.20.5.710; -; 1.
DR   Gene3D; 3.30.1390.10; -; 1.
DR   HAMAP; MF_00368; Ribosomal_L7_L12; 1.
DR   InterPro; IPR000206; Ribosomal_L7/12.
DR   InterPro; IPR014719; Ribosomal_L7/12_C/ClpS-like.
DR   InterPro; IPR013823; Ribosomal_L7/L12_C.
DR   InterPro; IPR008932; Ribosomal_L7/L12_oligo.
DR   InterPro; IPR036235; Ribosomal_L7/L12_oligo_N_sf.
DR   Pfam; PF00542; Ribosomal_L12; 1.
DR   Pfam; PF16320; Ribosomal_L12_N; 1.
DR   SUPFAM; SSF48300; SSF48300; 1.
DR   SUPFAM; SSF54736; SSF54736; 1.
DR   TIGRFAMs; TIGR00855; L12; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P02394.
DR   SWISS-2DPAGE; P02394.
KW   Direct protein sequencing; Reference proteome; Ribonucleoprotein;
KW   Ribosomal protein.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:6771249,
FT                   ECO:0000269|PubMed:8755892, ECO:0000269|PubMed:9298659"
FT   CHAIN           2..123
FT                   /note="50S ribosomal protein L7/L12"
FT                   /id="PRO_0000157505"
FT   CONFLICT        54..55
FT                   /note="Missing (in Ref. 2; AA sequence and 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        97
FT                   /note="L -> LEV (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   123 AA;  12751 MW;  8BFE1B168292FAEC CRC64;
     MALNIEEIIA SVKEATVLEL NDLVKAIEEE FGVTAAAPVA VAGGAAAGGA AEEQSEFDLI
     LAGAGSQKIK VIKVVREITG LGLKEAKELV DNTPKPLKEG IAKEEAEELK AKLEEVGASV
     EVK
//

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