(data stored in SCRATCH zone)

SWISSPROT: EFP_BACSU

ID   EFP_BACSU               Reviewed;         185 AA.
AC   P49778;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 2.
DT   11-DEC-2019, entry version 128.
DE   RecName: Full=Elongation factor P;
DE            Short=EF-P;
GN   Name=efp; Synonyms=yqgF, yqhU; OrderedLocusNames=BSU24450;
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=168 / JH642;
RX   PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA   Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA   Kobayashi Y.;
RT   "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT   Bacillus subtilis genome containing the skin element and many sporulation
RT   genes.";
RL   Microbiology 142:3103-3111(1996).
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   SEQUENCE REVISION TO 14.
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   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 139-185.
RC   STRAIN=168 / JH642;
RA   Guerout-Fleury A.M., Gonzy-Treboul G., Stragier P.;
RL   Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
RN   [5]
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).
CC   -!- FUNCTION: Involved in peptide bond synthesis. Stimulates efficient
CC       translation and peptide-bond synthesis on native or reconstituted 70S
CC       ribosomes in vitro. Probably functions indirectly by altering the
CC       affinity of the ribosome for aminoacyl-tRNA, thus increasing their
CC       reactivity as acceptors for peptidyl transferase (By similarity).
CC       {ECO:0000250}.
CC   -!- FUNCTION: Plays a role in sporulation. {ECO:0000269|PubMed:14586115}.
CC   -!- PATHWAY: Protein biosynthesis; polypeptide chain elongation.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: No sporulation at 37 or 47 degrees Celsius.
CC       {ECO:0000269|PubMed:14586115}.
CC   -!- SIMILARITY: Belongs to the elongation factor P family. {ECO:0000305}.
DR   EMBL; D84432; BAA12558.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14376.2; -; Genomic_DNA.
DR   EMBL; U35252; AAA76718.1; -; Genomic_DNA.
DR   PIR; A69620; A69620.
DR   RefSeq; NP_390325.2; NC_000964.3.
DR   RefSeq; WP_003226377.1; NZ_JNCM01000036.1.
DR   SMR; P49778; -.
DR   STRING; 224308.BSU24450; -.
DR   jPOST; P49778; -.
DR   PaxDb; P49778; -.
DR   PRIDE; P49778; -.
DR   EnsemblBacteria; CAB14376; CAB14376; BSU24450.
DR   GeneID; 938558; -.
DR   KEGG; bsu:BSU24450; -.
DR   PATRIC; fig|224308.179.peg.2663; -.
DR   eggNOG; ENOG4105DRH; Bacteria.
DR   eggNOG; COG0231; LUCA.
DR   HOGENOM; HOG000010048; -.
DR   InParanoid; P49778; -.
DR   KO; K02356; -.
DR   OMA; NTFSAGH; -.
DR   PhylomeDB; P49778; -.
DR   BioCyc; BSUB:BSU24450-MONOMER; -.
DR   UniPathway; UPA00345; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central.
DR   CDD; cd04470; S1_EF-P_repeat_1; 1.
DR   CDD; cd05794; S1_EF-P_repeat_2; 1.
DR   Gene3D; 2.30.30.30; -; 1.
DR   HAMAP; MF_00141; EF_P; 1.
DR   InterPro; IPR015365; Elong-fact-P_C.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR014722; Rib_L2_dom2.
DR   InterPro; IPR020599; Transl_elong_fac_P/YeiP.
DR   InterPro; IPR013185; Transl_elong_KOW-like.
DR   InterPro; IPR001059; Transl_elong_P/YeiP_cen.
DR   InterPro; IPR013852; Transl_elong_P/YeiP_CS.
DR   InterPro; IPR011768; Transl_elongation_fac_P.
DR   InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR   PANTHER; PTHR30053; PTHR30053; 1.
DR   Pfam; PF01132; EFP; 1.
DR   Pfam; PF08207; EFP_N; 1.
DR   Pfam; PF09285; Elong-fact-P_C; 1.
DR   PIRSF; PIRSF005901; EF-P; 1.
DR   SMART; SM01185; EFP; 1.
DR   SMART; SM00841; Elong-fact-P_C; 1.
DR   SUPFAM; SSF50104; SSF50104; 1.
DR   SUPFAM; SSF50249; SSF50249; 2.
DR   TIGRFAMs; TIGR00038; efp; 1.
DR   PROSITE; PS01275; EFP; 1.
PE   3: Inferred from homology;
DR   PRODOM; P49778.
DR   SWISS-2DPAGE; P49778.
KW   Cytoplasm; Elongation factor; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..185
FT                   /note="Elongation factor P"
FT                   /id="PRO_0000094199"
FT   CONFLICT        14
FT                   /note="E -> D (in Ref. 1; BAA12558)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   185 AA;  20468 MW;  7CB27F646B3DF28D CRC64;
     MISVNDFRTG LTIEVDGGIW RVVDFQHVKP GKGAAFVRSK LRNLRTGAIQ EKTFRAGEKV
     AKAQIETKTM QYLYANGDQH VFMDTSSYEQ LELSATQIEE ELKYLLENMS VHIMMYQDET
     LGIELPNTVE LKVVETEPGI KGDTASGGTK PAKTETGLVV NVPFFVNEGD TLVVNTSDGS
     YVSRA
//

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