RL27_BACSU
ID RL27_BACSU Reviewed; 94 AA.
AC P05657;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=50S ribosomal protein L27;
DE AltName: Full=BL24;
DE AltName: Full=BL30;
GN Name=rpmA; OrderedLocusNames=BSU27940;
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=3918016; DOI=10.1128/jb.161.2.556-562.1985;
RA Ferrari F.A., Trach K.A., Hoch J.A.;
RT "Sequence analysis of the spo0B locus reveals a polycistronic transcription
RT unit.";
RL J. Bacteriol. 161:556-562(1985).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26.
RC STRAIN=168;
RX PubMed=1942049; DOI=10.1016/0022-2836(91)90931-u;
RA Cutting S.M., Roels S., Losick R.;
RT "Sporulation operon spoIVF and the characterization of mutations that
RT uncouple mother-cell from forespore gene expression in Bacillus subtilis.";
RL J. Mol. Biol. 221:1237-1256(1991).
RN [4]
RP DISRUPTION PHENOTYPE, AND ROLE IN SPORULATION.
RC STRAIN=168;
RX PubMed=14586115; DOI=10.1271/bbb.67.2245;
RA Ohashi Y., Inaoka T., Kasai K., Ito Y., Okamoto S., Satsu H., Tozawa Y.,
RA Kawamura F., Ochi K.;
RT "Expression profiling of translation-associated genes in sporulating
RT Bacillus subtilis and consequence of sporulation by gene inactivation.";
RL Biosci. Biotechnol. Biochem. 67:2245-2253(2003).
RN [5] {ECO:0007744|PDB:6HA1, ECO:0007744|PDB:6HA8}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.10 ANGSTROMS) OF 1-94 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: Plays a role in sporulation at high temperatures.
CC {ECO:0000269|PubMed:14586115}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit.
CC {ECO:0000269|PubMed:30126986}.
CC -!- DISRUPTION PHENOTYPE: No effect on sporulation at 37 degrees Celsius,
CC however sporulation decreases at 47 degrees Celsius.
CC {ECO:0000269|PubMed:14586115}.
CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL27 family.
CC {ECO:0000305}.
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DR EMBL; X02656; CAA26492.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14754.1; -; Genomic_DNA.
DR EMBL; X59528; CAA42110.1; -; Genomic_DNA.
DR PIR; C21895; C21895.
DR RefSeq; NP_390672.1; NC_000964.3.
DR RefSeq; WP_003222623.1; NZ_JNCM01000036.1.
DR PDB; 3J9W; EM; 3.90 A; BZ=1-94.
DR PDB; 5NJT; EM; 3.80 A; o=11-92.
DR PDB; 6HA1; EM; 3.10 A; W=1-94.
DR PDB; 6HA8; EM; 3.50 A; W=1-94.
DR PDB; 6HTQ; EM; 4.50 A; V=11-92.
DR PDB; 6PPF; EM; 3.40 A; V=1-94.
DR PDB; 6PPK; EM; 4.40 A; V=1-94.
DR PDB; 6TNN; EM; 3.07 A; o=1-94.
DR PDB; 6TPQ; EM; 3.07 A; o=1-94.
DR PDB; 7AQC; EM; 2.99 A; V=1-94.
DR PDB; 7AQD; EM; 3.10 A; V=1-94.
DR PDB; 7AS8; EM; 2.90 A; a=1-94.
DR PDB; 7AS9; EM; 3.50 A; a=1-94.
DR PDB; 7O5B; EM; 3.33 A; u=1-94.
DR PDB; 7OPE; EM; 3.20 A; a=1-94.
DR PDB; 7QV1; EM; 3.50 A; W=1-94.
DR PDB; 7QV2; EM; 3.50 A; W=1-94.
DR PDB; 7QV3; EM; 5.14 A; W=1-94.
DR PDBsum; 3J9W; -.
DR PDBsum; 5NJT; -.
DR PDBsum; 6HA1; -.
DR PDBsum; 6HA8; -.
DR PDBsum; 6HTQ; -.
DR PDBsum; 6PPF; -.
DR PDBsum; 6PPK; -.
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; P05657; -.
DR SMR; P05657; -.
DR IntAct; P05657; 1.
DR STRING; 224308.BSU27940; -.
DR jPOST; P05657; -.
DR PaxDb; P05657; -.
DR PRIDE; P05657; -.
DR EnsemblBacteria; CAB14754; CAB14754; BSU_27940.
DR GeneID; 50136748; -.
DR GeneID; 64304517; -.
DR GeneID; 937511; -.
DR KEGG; bsu:BSU27940; -.
DR PATRIC; fig|224308.179.peg.3036; -.
DR eggNOG; COG0211; Bacteria.
DR InParanoid; P05657; -.
DR OMA; GKDHTLH; -.
DR PhylomeDB; P05657; -.
DR BioCyc; BSUB:BSU27940-MON; -.
DR PRO; PR:P05657; -.
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; IBA:GO_Central.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00539; Ribosomal_L27; 1.
DR InterPro; IPR001684; Ribosomal_L27.
DR InterPro; IPR018261; Ribosomal_L27_CS.
DR PANTHER; PTHR15893; PTHR15893; 1.
DR Pfam; PF01016; Ribosomal_L27; 1.
DR PRINTS; PR00063; RIBOSOMALL27.
DR TIGRFAMs; TIGR00062; L27; 1.
DR PROSITE; PS00831; RIBOSOMAL_L27; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1..94
FT /note="50S ribosomal protein L27"
FT /id="PRO_0000181044"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 67..83
FT /evidence="ECO:0007829|PDB:7AS8"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:7AS8"
SQ SEQUENCE 94 AA; 10372 MW; AFB2D90836B6AABD CRC64;
MLRLDLQFFA SKKGVGSTKN GRDSEAKRLG AKRADGQFVT GGSILYRQRG TKIYPGENVG
RGGDDTLFAK IDGTVKFERF GRDRKKVSVY PVAQ
