(data stored in SCRATCH zone)

SWISSPROT: ERA_BACSU

ID   ERA_BACSU               Reviewed;         301 AA.
AC   P42182;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   11-DEC-2019, entry version 133.
DE   RecName: Full=GTPase Era;
DE   AltName: Full=Bex protein;
GN   Name=era; Synonyms=bex, yqfH; OrderedLocusNames=BSU25290;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, ABILITY TO COMPLEMENT E.COLI
RP   DISRUPTION MUTANT, AND DISRUPTION PHENOTYPE.
RC   STRAIN=168, 168 / BR151, and IS75;
RX   PubMed=12399511; DOI=10.1128/jb.184.22.6389-6394.2002;
RA   Minkovsky N., Zarimani A., Chary V.K., Johnstone B.H., Powell B.S.,
RA   Torrance P.D., Court D.L., Simons R.W., Piggot P.J.;
RT   "Bex, the Bacillus subtilis homolog of the essential Escherichia coli
RT   GTPase Era, is required for normal cell division and spore formation.";
RL   J. Bacteriol. 184:6389-6394(2002).
RN   [2]
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   [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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-106.
RC   STRAIN=168;
RX   PubMed=2526291; DOI=10.1007/bf00334391;
RA   Song B.-H., Neuhard J.;
RT   "Chromosomal location, cloning and nucleotide sequence of the Bacillus
RT   subtilis cdd gene encoding cytidine/deoxycytidine deaminase.";
RL   Mol. Gen. Genet. 216:462-468(1989).
RN   [5]
RP   GTP- AND GDP-BINDING, PROTEIN LEVELS, AND DISRUPTION PHENOTYPE.
RC   STRAIN=CRK6000;
RX   PubMed=12427945; DOI=10.1099/00221287-148-11-3539;
RA   Morimoto T., Loh P.C., Hirai T., Asai K., Kobayashi K., Moriya S.,
RA   Ogasawara N.;
RT   "Six GTP-binding proteins of the Era/Obg family are essential for cell
RT   growth in Bacillus subtilis.";
RL   Microbiology 148:3539-3552(2002).
CC   -!- FUNCTION: An essential GTPase that binds both GDP and GTP, with rapid
CC       nucleotide exchange. Plays a role in 16S rRNA processing and 30S
CC       ribosomal subunit biogenesis and possibly also in cell cycle regulation
CC       and energy metabolism (By similarity). Binds both GDP and GTP.
CC       Complements an E.coli era disruption mutant. {ECO:0000250}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}.
CC   -!- INDUCTION: Constitutively expressed, two-fold induced at the end of the
CC       exponential phase; this is under control of Spo0A, suggesting it may
CC       have a role in sporulation. {ECO:0000269|PubMed:12399511}.
CC   -!- DISRUPTION PHENOTYPE: Essential in some but not all strains; in 168 /
CC       BR151 the null mutation grows slowly and forms irregularly shaped
CC       colonies after several days. In liquid culture forms chains of
CC       elongated cells with diffuse nucleoids that occupy most of the cell.
CC       Sporulation in this disruption strain is severely impaired. Essential
CC       in strains CRK6000 and IS75, where it cannot be disrupted. In CRK600 in
CC       depletion experiments cells become 1.5 to 2-fold longer and nucleoid
CC       distribution is dispersed. The number of replication origins increases,
CC       suggesting an increase in chromosome replication.
CC       {ECO:0000269|PubMed:12399511, ECO:0000269|PubMed:12427945}.
CC   -!- MISCELLANEOUS: Estimated to be present at 3000 copies per cell.
CC   -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC       GTPase superfamily. Era GTPase family. {ECO:0000305}.
DR   EMBL; U18532; AAB59994.1; -; Genomic_DNA.
DR   EMBL; D84432; BAA12482.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14458.1; -; Genomic_DNA.
DR   EMBL; X17430; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; B69593; B69593.
DR   RefSeq; NP_390407.1; NC_000964.3.
DR   RefSeq; WP_003230051.1; NZ_JNCM01000036.1.
DR   SMR; P42182; -.
DR   STRING; 224308.BSU25290; -.
DR   PaxDb; P42182; -.
DR   PRIDE; P42182; -.
DR   EnsemblBacteria; CAB14458; CAB14458; BSU25290.
DR   GeneID; 937871; -.
DR   KEGG; bsu:BSU25290; -.
DR   PATRIC; fig|224308.179.peg.2749; -.
DR   eggNOG; ENOG4105CWT; Bacteria.
DR   eggNOG; COG1159; LUCA.
DR   HOGENOM; HOG000245596; -.
DR   InParanoid; P42182; -.
DR   KO; K03595; -.
DR   OMA; HVKVAKD; -.
DR   PhylomeDB; P42182; -.
DR   BioCyc; BSUB:BSU25290-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0043024; F:ribosomal small subunit binding; IBA:GO_Central.
DR   GO; GO:0019843; F:rRNA binding; IBA:GO_Central.
DR   GO; GO:0070181; F:small ribosomal subunit rRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0032297; P:negative regulation of DNA-dependent DNA replication initiation; IDA:CACAO.
DR   GO; GO:0051781; P:positive regulation of cell division; IMP:CACAO.
DR   GO; GO:0000028; P:ribosomal small subunit assembly; IBA:GO_Central.
DR   CDD; cd04163; Era; 1.
DR   Gene3D; 3.30.300.20; -; 1.
DR   HAMAP; MF_00367; GTPase_Era; 1.
DR   InterPro; IPR030388; G_ERA_dom.
DR   InterPro; IPR005662; GTP-bd_Era.
DR   InterPro; IPR006073; GTP_binding_domain.
DR   InterPro; IPR015946; KH_dom-like_a/b.
DR   InterPro; IPR004044; KH_dom_type_2.
DR   InterPro; IPR009019; KH_sf_prok-type.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   Pfam; PF07650; KH_2; 1.
DR   Pfam; PF01926; MMR_HSR1; 1.
DR   PRINTS; PR00326; GTP1OBG.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF54814; SSF54814; 1.
DR   TIGRFAMs; TIGR00436; era; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51713; G_ERA; 1.
DR   PROSITE; PS50823; KH_TYPE_2; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P42182.
DR   SWISS-2DPAGE; P42182.
KW   Cell membrane; Cytoplasm; GTP-binding; Membrane; Nucleotide-binding;
KW   Reference proteome; Ribosome biogenesis; RNA-binding; rRNA-binding.
FT   CHAIN           1..301
FT                   /note="GTPase Era"
FT                   /id="PRO_0000179997"
FT   DOMAIN          7..174
FT                   /note="Era-type G"
FT   DOMAIN          205..282
FT                   /note="KH type-2"
FT   NP_BIND         15..22
FT                   /note="GTP"
FT                   /evidence="ECO:0000255"
FT   NP_BIND         62..66
FT                   /note="GTP"
FT                   /evidence="ECO:0000255"
FT   NP_BIND         124..127
FT                   /note="GTP"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   301 AA;  34074 MW;  64B2D58FABA4264F CRC64;
     MTNESFKSGF VSIIGRPNVG KSTFLNRVIG QKIAIMSDKP QTTRNKVQGV LTTGTSQTIF
     IDTPGIHKPK HKLGDFMMKV AQNTLKEVDL ILFMINAEEG YGKGDEFIIE KLQTMSTPVF
     LIVNKIDKIH PDQLLLLIDE YRKRYPFKEI VPISALEGNN IETLLAQIEA YLPEGPQFYP
     SDQVTDHPER FIISELIREK VLHLTREEIP HSIAVAIESI KGQDNGSVHV AATIVVERDS
     QKGIVIGKKG SLLKEVGKRA RADIEALLGS RVYLELWVKV QKDWRNKMSQ LRDFGFKEDE
     Y
//

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