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30S ribosomal protein S12 (BS12)

 RS12_BACSU              Reviewed;         138 AA.
P21472;
01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
16-JUN-2009, sequence version 5.
30-AUG-2017, entry version 140.
RecName: Full=30S ribosomal protein S12;
Short=BS12;
Name=rpsL; Synonyms=fun, strA; OrderedLocusNames=BSU01100;
Bacillus subtilis (strain 168).
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
NCBI_TaxID=224308;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168;
PubMed=8969501; DOI=10.1099/13500872-142-11-3039;
Yasumoto K., Liu H., Jeong S.M., Ohashi Y., Kakinuma S., Tanaka K.,
Kawamura F., Yoshikawa H., Takahashi H.;
"Sequence analysis of a 50 kb region between spo0H and rrnH on the
Bacillus subtilis chromosome.";
Microbiology 142:3039-3046(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
PubMed=9384377; DOI=10.1038/36786;
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G.,
Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
Yoshikawa H., Danchin A.;
"The complete genome sequence of the Gram-positive bacterium Bacillus
subtilis.";
Nature 390:249-256(1997).
[3]
SEQUENCE REVISION TO 102; 105 AND 128, AND LACK OF MODIFICATION.
STRAIN=168;
Ochi K., Takashi I., Forbes A., Kelleher N.L., Garavelli J.S.;
Unpublished observations (AUG-2002).
[4]
SEQUENCE REVISION TO 102 AND 105.
STRAIN=168 / BGSC1A1, and ATCC 21332 / IAM 1213;
PubMed=16484214; DOI=10.1128/JB.188.5.2020-2023.2006;
Carr J.F., Hamburg D.M., Gregory S.T., Limbach P.A., Dahlberg A.E.;
"Effects of streptomycin resistance mutations on posttranslational
modification of ribosomal protein S12.";
J. Bacteriol. 188:2020-2023(2006).
[5]
SEQUENCE REVISION TO 102; 105 AND 128, AND LACK OF MODIFICATION.
STRAIN=168;
PubMed=19653700; DOI=10.1021/pr801114k;
Lauber M.A., Running W.E., Reilly J.P.;
"B. subtilis ribosomal proteins: structural homology and post-
translational modifications.";
J. Proteome Res. 8:4193-4206(2009).
[6]
SEQUENCE REVISION TO 102; 105 AND 128.
PubMed=19383706; DOI=10.1099/mic.0.027839-0;
Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G.,
Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
"From a consortium sequence to a unified sequence: the Bacillus
subtilis 168 reference genome a decade later.";
Microbiology 155:1758-1775(2009).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-32.
STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 /
NCIMB 3610 / VKM B-501;
PubMed=7657605; DOI=10.1074/jbc.270.35.20329;
Boor K.J., Duncan M.L., Price C.W.;
"Genetic and transcriptional organization of the region encoding the
beta subunit of Bacillus subtilis RNA polymerase.";
J. Biol. Chem. 270:20329-20336(1995).
[8]
PROTEIN SEQUENCE OF 2-21.
PubMed=6806564; DOI=10.1007/BF00330792;
Higo K., Otaka E., Osawa S.;
"Purification and characterization of 30S ribosomal proteins from
Bacillus subtilis: correlation to Escherichia coli 30S proteins.";
Mol. Gen. Genet. 185:239-244(1982).
[9]
VARIANTS STREPTOMYCIN RESISTANT, AND ANTIBIOTIC PRODUCTION.
STRAIN=168;
PubMed=9687404;
Hosoya Y., Okamoto S., Muramatsu H., Ochi K.;
"Acquisition of certain streptomycin-resistant (str) mutations
enhances antibiotic production in bacteria.";
Antimicrob. Agents Chemother. 42:2041-2047(1998).
[10]
CHARACTERIZATION, MUTAGENESIS, AND VARIANTS STREPTOMYCIN RESISTANT.
STRAIN=168;
PubMed=11489846; DOI=10.1128/JB.183.17.4958-4963.2001;
Inaoka T., Kasai K., Ochi K.;
"Construction of an in vivo nonsense readthrough assay system and
functional analysis of ribosomal proteins S12, S4, and S5 in Bacillus
subtilis.";
J. Bacteriol. 183:4958-4963(2001).
-!- FUNCTION: With S4 and S5 plays an important role in translational
accuracy.
-!- FUNCTION: Interacts with and stabilizes bases of the 16S rRNA that
are involved in tRNA selection in the A site and with the mRNA
backbone. Located at the interface of the 30S and 50S subunits, it
traverses the body of the 30S subunit contacting proteins on the
other side and probably holding the rRNA structure together. The
combined cluster of proteins S8, S12 and S17 appears to hold
together the shoulder and platform of the 30S subunit (By
similarity). {ECO:0000250}.
-!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts proteins S8
and S17. May interact with IF1 in the 30S initiation complex (By
similarity). {ECO:0000250}.
-!- MISCELLANEOUS: Many streptomycin resistant B.subtilis with
mutations in this protein produce increased quantities of a
natural (but uncharacterized) antibiotic.
-!- MISCELLANEOUS: A number of substitutions and deletions can promote
streptomycin resistance, dependence or pseudodependence; all but
one of these (K55R) are associated with hyperaccurate translation.
-!- SIMILARITY: Belongs to the universal ribosomal protein uS12
family. {ECO:0000305}.
-!- CAUTION: The enzyme that would modify Asp-102 to 3-
methylthioaspartic acid has not been found in the proteome of this
organism, and that modification does not occur. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; D64127; BAA11001.1; -; Genomic_DNA.
EMBL; AL009126; CAB11886.2; -; Genomic_DNA.
EMBL; L43593; AAB59114.1; -; Genomic_DNA.
PIR; C69700; C69700.
RefSeq; NP_387991.2; NC_000964.3.
RefSeq; WP_003225781.1; NZ_JNCM01000029.1.
PDB; 3J9W; EM; 3.90 A; AL=1-138.
PDB; 5NJT; EM; 3.80 A; L=2-138.
PDBsum; 3J9W; -.
PDBsum; 5NJT; -.
ProteinModelPortal; P21472; -.
SMR; P21472; -.
STRING; 224308.Bsubs1_010100000570; -.
PaxDb; P21472; -.
PRIDE; P21472; -.
EnsemblBacteria; CAB11886; CAB11886; BSU01100.
GeneID; 936616; -.
KEGG; bsu:BSU01100; -.
PATRIC; fig|224308.179.peg.113; -.
eggNOG; ENOG4108UKE; Bacteria.
eggNOG; COG0048; LUCA.
HOGENOM; HOG000040063; -.
InParanoid; P21472; -.
KO; K02950; -.
OMA; KRGVCTA; -.
PhylomeDB; P21472; -.
BioCyc; BSUB:BSU01100-MONOMER; -.
PRO; PR:P21472; -.
Proteomes; UP000001570; Chromosome.
GO; GO:0005840; C:ribosome; IBA:GO_Central.
GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro.
GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
GO; GO:0006412; P:translation; IBA:GO_Central.
CDD; cd03368; Ribosomal_S12; 1.
HAMAP; MF_00403_B; Ribosomal_S12_B; 1.
InterPro; IPR012340; NA-bd_OB-fold.
InterPro; IPR006032; Ribosomal_S12/S23.
InterPro; IPR005679; Ribosomal_S12_bac.
PANTHER; PTHR11652; PTHR11652; 1.
Pfam; PF00164; Ribosom_S12_S23; 1.
PIRSF; PIRSF002133; Ribosomal_S12/S23; 1.
PRINTS; PR01034; RIBOSOMALS12.
SUPFAM; SSF50249; SSF50249; 1.
TIGRFAMs; TIGR00981; rpsL_bact; 1.
PROSITE; PS00055; RIBOSOMAL_S12; 1.
1: Evidence at protein level;
3D-structure; Antibiotic resistance; Complete proteome;
Direct protein sequencing; Reference proteome; Ribonucleoprotein;
Ribosomal protein; RNA-binding; rRNA-binding; tRNA-binding.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:6806564}.
CHAIN 2 138 30S ribosomal protein S12.
/FTId=PRO_0000146178.
SITE 102 102 Not modified.
{ECO:0000269|PubMed:19653700,
ECO:0000269|Ref.3}.
VARIANT 56 56 K -> I (in RPSL4 (STRA1); confers
streptomycin resistance and hyperaccurate
translation, has no effect on natural
antibiotic production).
VARIANT 56 56 K -> R (in RPSL1 (KO-267); confers
streptomycin resistance but not
hyperaccurate translation, increases
natural antibiotic production 10-fold).
MUTAGEN 56 56 K->D: Confers streptomycin resistance and
very poor growth in rich medium.
{ECO:0000269|PubMed:11489846}.
CONFLICT 102 102 D -> N (in Ref. 1; BAA11001).
{ECO:0000305}.
CONFLICT 105 105 G -> R (in Ref. 1; BAA11001).
{ECO:0000305}.
CONFLICT 128 128 S -> P (in Ref. 1; BAA11001).
{ECO:0000305}.
SEQUENCE 138 AA; 15216 MW; 1E8EDCEC75B75648 CRC64;
MPTINQLIRK GRVSKVENSK SPALNKGYNS FKKEHTNVSS PQKRGVCTRV GTMTPKKPNS
ALRKYARVRL TNGIEVTAYI PGIGHNLQEH SVVLIRGGRV KDLPGVRYHI VRGALDTAGV
ENRAQGRSKY GTKKPKAK


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