(data stored in ACNUC7421 zone)

SWISSPROT: RL23_BACSU

ID   RL23_BACSU              Reviewed;          95 AA.
AC   P42924;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 2.
DT   11-DEC-2019, entry version 123.
DE   RecName: Full=50S ribosomal protein L23 {ECO:0000255|HAMAP-Rule:MF_01369};
GN   Name=rplW {ECO:0000255|HAMAP-Rule:MF_01369}; OrderedLocusNames=BSU01180;
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 24 AND 39.
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).
CC   -!- FUNCTION: One of the early assembly proteins it binds 23S rRNA. One of
CC       the proteins that surrounds the polypeptide exit tunnel on the outside
CC       of the ribosome. Forms the main docking site for trigger factor binding
CC       to the ribosome. {ECO:0000255|HAMAP-Rule:MF_01369}.
CC   -!- SUBUNIT: Part of the 50S ribosomal subunit. Contacts protein L29, and
CC       trigger factor when it is bound to the ribosome. {ECO:0000255|HAMAP-
CC       Rule:MF_01369}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL23 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01369}.
DR   EMBL; U43929; AAC45958.1; -; Genomic_DNA.
DR   EMBL; D50302; BAA08833.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB11894.2; -; Genomic_DNA.
DR   PIR; A69697; A69697.
DR   RefSeq; NP_387999.2; NC_000964.3.
DR   RefSeq; WP_003156467.1; NZ_JNCM01000029.1.
DR   PDB; 3J3V; EM; 13.30 A; T=1-95.
DR   PDB; 3J3W; EM; 10.70 A; T=1-95.
DR   PDB; 3J9W; EM; 3.90 A; BW=1-95.
DR   PDB; 5NJT; EM; 3.80 A; m=1-93.
DR   PDB; 6HA1; EM; 3.10 A; T=1-95.
DR   PDB; 6HA8; EM; 3.50 A; T=1-95.
DR   PDBsum; 3J3V; -.
DR   PDBsum; 3J3W; -.
DR   PDBsum; 3J9W; -.
DR   PDBsum; 5NJT; -.
DR   PDBsum; 6HA1; -.
DR   PDBsum; 6HA8; -.
DR   SMR; P42924; -.
DR   IntAct; P42924; 2.
DR   STRING; 224308.BSU01180; -.
DR   jPOST; P42924; -.
DR   PaxDb; P42924; -.
DR   PRIDE; P42924; -.
DR   EnsemblBacteria; CAB11894; CAB11894; BSU01180.
DR   GeneID; 936820; -.
DR   GeneID; 9779966; -.
DR   KEGG; bsu:BSU01180; -.
DR   PATRIC; fig|224308.179.peg.121; -.
DR   eggNOG; ENOG41080UE; Bacteria.
DR   eggNOG; COG0089; LUCA.
DR   HOGENOM; HOG000231366; -.
DR   InParanoid; P42924; -.
DR   KO; K02892; -.
DR   OMA; FEVDHRA; -.
DR   PhylomeDB; P42924; -.
DR   BioCyc; BSUB:BSU01180-MONOMER; -.
DR   PRO; PR:P42924; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0022625; C:cytosolic large ribosomal subunit; 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:0000027; P:ribosomal large subunit assembly; IBA:GO_Central.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.70.330; -; 1.
DR   HAMAP; MF_01369_B; Ribosomal_L23_B; 1.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR012678; Ribosomal_L23/L15e_core_dom_sf.
DR   InterPro; IPR001014; Ribosomal_L23/L25_CS.
DR   InterPro; IPR013025; Ribosomal_L25/23.
DR   Pfam; PF00276; Ribosomal_L23; 1.
DR   SUPFAM; SSF54189; SSF54189; 1.
DR   PROSITE; PS00050; RIBOSOMAL_L23; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P42924.
DR   SWISS-2DPAGE; P42924.
KW   3D-structure; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW   RNA-binding; rRNA-binding.
FT   CHAIN           1..95
FT                   /note="50S ribosomal protein L23"
FT                   /id="PRO_0000129398"
FT   CONFLICT        24
FT                   /note="K -> E (in Ref. 1; AAC45958 and 2; BAA08833)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        39
FT                   /note="V -> A (in Ref. 1; AAC45958 and 2; BAA08833)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   95 AA;  10956 MW;  54272FBD14393AD6 CRC64;
     MKDPRDVLKR PVITERSADL MTEKKYTFEV DVRANKTEVK DAVESIFGVK VDKVNIMNYK
     GKSKRVGRYT GMTSRRRKAI VKLTADSKEI EIFEA
//

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