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RS13_BACSU
ID   RS13_BACSU              Reviewed;         121 AA.
AC   P20282;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 152.
DE   RecName: Full=30S ribosomal protein S13 {ECO:0000255|HAMAP-Rule:MF_01315};
DE   AltName: Full=BS14;
GN   Name=rpsM {ECO:0000255|HAMAP-Rule:MF_01315}; OrderedLocusNames=BSU01410;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2496109; DOI=10.1128/jb.171.5.2553-2562.1989;
RA   Boylan S.A., Suh J.-W., Thomas S.M., Price C.W.;
RT   "Gene encoding the alpha core subunit of Bacillus subtilis RNA polymerase
RT   is cotranscribed with the genes for initiation factor 1 and ribosomal
RT   proteins B, S13, S11, and L17.";
RL   J. Bacteriol. 171:2553-2562(1989).
RN   [2]
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   [3]
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   [4]
RP   SEQUENCE REVISION TO 85.
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   [5]
RP   PROTEIN SEQUENCE OF 2-42.
RX   PubMed=6806564; DOI=10.1007/bf00330792;
RA   Higo K., Otaka E., Osawa S.;
RT   "Purification and characterization of 30S ribosomal proteins from Bacillus
RT   subtilis: correlation to Escherichia coli 30S proteins.";
RL   Mol. Gen. Genet. 185:239-244(1982).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 86-121.
RX   PubMed=3093467; DOI=10.1128/jb.168.1.65-71.1986;
RA   Suh J.-W., Boylan S.A., Price C.W.;
RT   "Gene for the alpha subunit of Bacillus subtilis RNA polymerase maps in the
RT   ribosomal protein gene cluster.";
RL   J. Bacteriol. 168:65-71(1986).
RN   [7] {ECO:0007744|PDB:6HA1, ECO:0007744|PDB:6HA8}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.10 ANGSTROMS) OF 1-121 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: Located at the top of the head of the 30S subunit, it
CC       contacts several helices of the 16S rRNA. In the 70S ribosome it
CC       contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit
CC       (bridge B1b), connecting the 2 subunits; these bridges are implicated
CC       in subunit movement. Contacts the tRNAs in the A and P-sites.
CC       {ECO:0000255|HAMAP-Rule:MF_01315}.
CC   -!- SUBUNIT: Part of the 30S ribosomal subunit (PubMed:30126986). Forms a
CC       loose heterodimer with protein S19. Forms two bridges to the 50S
CC       subunit in the 70S ribosome (By similarity). {ECO:0000255|HAMAP-
CC       Rule:MF_01315, ECO:0000269|PubMed:30126986}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS13 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01315}.
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DR   EMBL; L47971; AAB06824.1; -; Genomic_DNA.
DR   EMBL; M26414; AAA22215.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB11917.2; -; Genomic_DNA.
DR   EMBL; M13957; AAA22706.1; -; Genomic_DNA.
DR   PIR; C32307; R3BS13.
DR   RefSeq; NP_388022.2; NC_000964.3.
DR   RefSeq; WP_003235095.1; NZ_JNCM01000029.1.
DR   PDB; 3J9W; EM; 3.90 A; AM=1-121.
DR   PDB; 5NJT; EM; 3.80 A; M=2-112.
DR   PDB; 6HA1; EM; 3.10 A; m=1-121.
DR   PDB; 6HA8; EM; 3.50 A; m=1-121.
DR   PDB; 6HTQ; EM; 4.50 A; m=3-110.
DR   PDB; 7O5B; EM; 3.33 A; M=1-121.
DR   PDB; 7QV1; EM; 3.50 A; m=1-121.
DR   PDB; 7QV2; EM; 3.50 A; m=1-121.
DR   PDB; 7QV3; EM; 5.14 A; m=1-121.
DR   PDBsum; 3J9W; -.
DR   PDBsum; 5NJT; -.
DR   PDBsum; 6HA1; -.
DR   PDBsum; 6HA8; -.
DR   PDBsum; 6HTQ; -.
DR   PDBsum; 7O5B; -.
DR   PDBsum; 7QV1; -.
DR   PDBsum; 7QV2; -.
DR   PDBsum; 7QV3; -.
DR   AlphaFoldDB; P20282; -.
DR   SMR; P20282; -.
DR   STRING; 224308.BSU01410; -.
DR   jPOST; P20282; -.
DR   PaxDb; P20282; -.
DR   PRIDE; P20282; -.
DR   EnsemblBacteria; CAB11917; CAB11917; BSU_01410.
DR   GeneID; 938928; -.
DR   KEGG; bsu:BSU01410; -.
DR   PATRIC; fig|224308.179.peg.145; -.
DR   eggNOG; COG0099; Bacteria.
DR   InParanoid; P20282; -.
DR   OMA; YRGLRHK; -.
DR   PhylomeDB; P20282; -.
DR   BioCyc; BSUB:BSU01410-MON; -.
DR   PRO; PR:P20282; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0015935; C:small ribosomal subunit; 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-UniRule.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   Gene3D; 4.10.910.10; -; 1.
DR   HAMAP; MF_01315; Ribosomal_S13_S18; 1.
DR   InterPro; IPR027437; 30s_Rbsml_prot_S13_C.
DR   InterPro; IPR001892; Ribosomal_S13.
DR   InterPro; IPR010979; Ribosomal_S13-like_H2TH.
DR   InterPro; IPR019980; Ribosomal_S13_bac-type.
DR   InterPro; IPR018269; Ribosomal_S13_CS.
DR   PANTHER; PTHR10871:SF1; PTHR10871:SF1; 1.
DR   Pfam; PF00416; Ribosomal_S13; 1.
DR   PIRSF; PIRSF002134; Ribosomal_S13; 1.
DR   SUPFAM; SSF46946; SSF46946; 1.
DR   TIGRFAMs; TIGR03631; uS13_bact; 1.
DR   PROSITE; PS00646; RIBOSOMAL_S13_1; 1.
DR   PROSITE; PS50159; RIBOSOMAL_S13_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Reference proteome;
KW   Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding;
KW   tRNA-binding.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:6806564"
FT   CHAIN           2..121
FT                   /note="30S ribosomal protein S13"
FT                   /id="PRO_0000132065"
FT   REGION          93..121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        107..121
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        85
FT                   /note="S -> T (in Ref. 1; AAA22215)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   121 AA;  13787 MW;  86A03EE4EA9709EC CRC64;
     MARIAGVDIP RDKRVVISLT YIFGIGRTTA QQVLKEAGVS EDTRVRDLTE EELGKIRDII
     DKLKVEGDLR REVSLNIKRL IEIGSYRGIR HRRGLPVRGQ NSKNNARTRK GPRRTVANKK
     K
 
 
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