RL2_BACSU
ID RL2_BACSU Reviewed; 277 AA.
AC P42919;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 3.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=50S ribosomal protein L2 {ECO:0000255|HAMAP-Rule:MF_01320};
DE Short=BL2;
GN Name=rplB {ECO:0000255|HAMAP-Rule:MF_01320}; OrderedLocusNames=BSU01190;
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=SG38;
RX PubMed=9371452; DOI=10.1128/jb.179.22.7046-7054.1997;
RA Li X., Lindahl L., Sha Y., Zengel J.M.;
RT "Analysis of the Bacillus subtilis S10 ribosomal protein gene cluster
RT identifies two promoters that may be responsible for transcription of the
RT entire 15-kilobase S10-spc-alpha cluster.";
RL J. Bacteriol. 179:7046-7054(1997).
RN [2]
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 [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 9; 256 AND 262.
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 2-9, AND SUBUNIT.
RC STRAIN=PY22;
RX PubMed=10781545; DOI=10.1128/jb.182.10.2771-2777.2000;
RA Scott J.M., Ju J., Mitchell T., Haldenwang W.G.;
RT "The Bacillus subtilis GTP binding protein obg and regulators of the
RT sigma(B) stress response transcription factor cofractionate with
RT ribosomes.";
RL J. Bacteriol. 182:2771-2777(2000).
RN [6] {ECO:0007744|PDB:6HA1, ECO:0007744|PDB:6HA8}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.10 ANGSTROMS) OF 1-277 WITH AND WITHOUT
RP VIRGINIAMYCIN M.
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: One of the primary rRNA binding proteins. Required for
CC association of the 30S and 50S subunits to form the 70S ribosome, for
CC tRNA binding and peptide bond formation. It has been suggested to have
CC peptidyltransferase activity; this is somewhat controversial. Makes
CC several contacts with the 16S rRNA in the 70S ribosome.
CC {ECO:0000255|HAMAP-Rule:MF_01320}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit (PubMed:10781545,
CC PubMed:30126986). Forms a bridge to the 30S subunit in the 70S ribosome
CC (By similarity). {ECO:0000255|HAMAP-Rule:MF_01320,
CC ECO:0000269|PubMed:10781545, ECO:0000269|PubMed:30126986}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL2 family.
CC {ECO:0000255|HAMAP-Rule:MF_01320}.
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DR EMBL; U43929; AAC45959.1; -; Genomic_DNA.
DR EMBL; D50302; BAA08834.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB11895.2; -; Genomic_DNA.
DR PIR; F69694; F69694.
DR RefSeq; NP_388000.2; NC_000964.3.
DR RefSeq; WP_003225795.1; NZ_JNCM01000029.1.
DR PDB; 3J3V; EM; 13.30 A; C=1-277.
DR PDB; 3J3W; EM; 10.70 A; C=1-277.
DR PDB; 3J9W; EM; 3.90 A; BD=1-277.
DR PDB; 5NJT; EM; 3.80 A; W=2-276.
DR PDB; 6HA1; EM; 3.10 A; C=1-277.
DR PDB; 6HA8; EM; 3.50 A; C=1-277.
DR PDB; 6HTQ; EM; 4.50 A; C=2-273.
DR PDB; 6PPF; EM; 3.40 A; C=1-277.
DR PDB; 6PPK; EM; 4.40 A; C=1-277.
DR PDB; 6PVK; EM; 3.40 A; C=1-277.
DR PDB; 6TNN; EM; 3.07 A; W=1-277.
DR PDB; 6TPQ; EM; 3.07 A; W=1-277.
DR PDB; 7AQC; EM; 2.99 A; C=1-277.
DR PDB; 7AQD; EM; 3.10 A; C=1-277.
DR PDB; 7AS8; EM; 2.90 A; E=1-277.
DR PDB; 7AS9; EM; 3.50 A; E=1-277.
DR PDB; 7O5B; EM; 3.33 A; Z=1-277.
DR PDB; 7OPE; EM; 3.20 A; E=1-277.
DR PDB; 7QV1; EM; 3.50 A; C=1-277.
DR PDB; 7QV2; EM; 3.50 A; C=1-277.
DR PDB; 7QV3; EM; 5.14 A; C=1-277.
DR PDBsum; 3J3V; -.
DR PDBsum; 3J3W; -.
DR PDBsum; 3J9W; -.
DR PDBsum; 5NJT; -.
DR PDBsum; 6HA1; -.
DR PDBsum; 6HA8; -.
DR PDBsum; 6HTQ; -.
DR PDBsum; 6PPF; -.
DR PDBsum; 6PPK; -.
DR PDBsum; 6PVK; -.
DR PDBsum; 6TNN; -.
DR PDBsum; 6TPQ; -.
DR PDBsum; 7AQC; -.
DR PDBsum; 7AQD; -.
DR PDBsum; 7AS8; -.
DR PDBsum; 7AS9; -.
DR PDBsum; 7O5B; -.
DR PDBsum; 7OPE; -.
DR PDBsum; 7QV1; -.
DR PDBsum; 7QV2; -.
DR PDBsum; 7QV3; -.
DR AlphaFoldDB; P42919; -.
DR SMR; P42919; -.
DR IntAct; P42919; 2.
DR MINT; P42919; -.
DR STRING; 224308.BSU01190; -.
DR jPOST; P42919; -.
DR PaxDb; P42919; -.
DR PRIDE; P42919; -.
DR EnsemblBacteria; CAB11895; CAB11895; BSU_01190.
DR GeneID; 50135140; -.
DR GeneID; 64301957; -.
DR GeneID; 936817; -.
DR KEGG; bsu:BSU01190; -.
DR PATRIC; fig|224308.179.peg.122; -.
DR eggNOG; COG0090; Bacteria.
DR InParanoid; P42919; -.
DR OMA; SCIELRP; -.
DR PhylomeDB; P42919; -.
DR BioCyc; BSUB:BSU01190-MON; -.
DR PRO; PR:P42919; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0016740; F:transferase activity; IEA:InterPro.
DR GO; GO:0002181; P:cytoplasmic translation; IBA:GO_Central.
DR Gene3D; 2.30.30.30; -; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 4.10.950.10; -; 1.
DR HAMAP; MF_01320_B; Ribosomal_L2_B; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR022666; Rbsml_prot_L2_RNA-bd_dom.
DR InterPro; IPR014722; Rib_L2_dom2.
DR InterPro; IPR002171; Ribosomal_L2.
DR InterPro; IPR005880; Ribosomal_L2_bac/org-type.
DR InterPro; IPR022669; Ribosomal_L2_C.
DR InterPro; IPR022671; Ribosomal_L2_CS.
DR InterPro; IPR014726; Ribosomal_L2_dom3.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR PANTHER; PTHR13691; PTHR13691; 1.
DR Pfam; PF00181; Ribosomal_L2; 1.
DR Pfam; PF03947; Ribosomal_L2_C; 1.
DR PIRSF; PIRSF002158; Ribosomal_L2; 1.
DR SMART; SM01383; Ribosomal_L2; 1.
DR SMART; SM01382; Ribosomal_L2_C; 1.
DR SUPFAM; SSF50104; SSF50104; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR TIGRFAMs; TIGR01171; rplB_bact; 1.
DR PROSITE; PS00467; RIBOSOMAL_L2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10781545"
FT CHAIN 2..277
FT /note="50S ribosomal protein L2"
FT /id="PRO_0000129529"
FT REGION 219..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..277
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 9
FT /note="T -> S (in Ref. 1; AAC45959 and 2; BAA08834)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="I -> V (in Ref. 1; AAC45959)"
FT /evidence="ECO:0000305"
FT CONFLICT 256
FT /note="G -> E (in Ref. 2; BAA08834)"
FT /evidence="ECO:0000305"
FT CONFLICT 262
FT /note="K -> Q (in Ref. 2; BAA08834)"
FT /evidence="ECO:0000305"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:7AS8"
FT TURN 11..15
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:7AS8"
FT TURN 31..33
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:7AQC"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:6TNN"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:6PVK"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:7AQC"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:7AQC"
FT STRAND 76..83
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 87..96
FT /evidence="ECO:0007829|PDB:7AS8"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:6TNN"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:6PVK"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:7AS8"
FT TURN 132..134
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:6PPF"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 162..167
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 169..176
FT /evidence="ECO:0007829|PDB:7AS8"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 180..185
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 189..193
FT /evidence="ECO:0007829|PDB:7AS8"
FT HELIX 198..202
FT /evidence="ECO:0007829|PDB:7AQC"
FT HELIX 208..213
FT /evidence="ECO:0007829|PDB:7AS8"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:7AQC"
FT TURN 227..229
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:7AQC"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:7AS9"
FT TURN 266..269
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:7AQC"
SQ SEQUENCE 277 AA; 30274 MW; E126BCA251035A96 CRC64;
MAIKKYKPTS NGRRGMTTSD FAEITTDKPE KSLLAPLHKK GGRNNQGKLT VRHQGGGHKR
QYRVIDFKRD KDGIPGRVAT VEYDPNRSAN IALINYADGE KRYILAPKGI QVGTEIMSGP
EADIKVGNAL PLINIPVGTV VHNIELKPGK GGQLVRSAGT SAQVLGKEGK YVLVRLNSGE
VRMILSACRA SIGQVGNEQH ELINIGKAGR SRWKGIRPTV RGSVMNPNDH PHGGGEGRAP
IGRKSPMSPW GKPTLGFKTR KKKNKSDKFI VRRRKNK
