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GTPase Era (Bex protein)

 ERA_BACSU               Reviewed;         301 AA.
P42182;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 1.
10-OCT-2018, entry version 128.
RecName: Full=GTPase Era;
AltName: Full=Bex protein;
Name=era; Synonyms=bex, yqfH; OrderedLocusNames=BSU25290;
Bacillus subtilis (strain 168).
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
NCBI_TaxID=224308;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, ABILITY TO COMPLEMENT
E.COLI DISRUPTION MUTANT, AND DISRUPTION PHENOTYPE.
STRAIN=168, 168 / BR151, and IS75;
PubMed=12399511; DOI=10.1128/JB.184.22.6389-6394.2002;
Minkovsky N., Zarimani A., Chary V.K., Johnstone B.H., Powell B.S.,
Torrance P.D., Court D.L., Simons R.W., Piggot P.J.;
"Bex, the Bacillus subtilis homolog of the essential Escherichia coli
GTPase Era, is required for normal cell division and spore
formation.";
J. Bacteriol. 184:6389-6394(2002).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168 / JH642;
PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
Kobayashi Y.;
"Systematic sequencing of the 283 kb 210 degrees-232 degrees region of
the Bacillus subtilis genome containing the skin element and many
sporulation genes.";
Microbiology 142:3103-3111(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
PubMed=9384377; DOI=10.1038/36786;
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G.,
Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
Yoshikawa H., Danchin A.;
"The complete genome sequence of the Gram-positive bacterium Bacillus
subtilis.";
Nature 390:249-256(1997).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-106.
STRAIN=168;
PubMed=2526291; DOI=10.1007/BF00334391;
Song B.-H., Neuhard J.;
"Chromosomal location, cloning and nucleotide sequence of the Bacillus
subtilis cdd gene encoding cytidine/deoxycytidine deaminase.";
Mol. Gen. Genet. 216:462-468(1989).
[5]
GTP- AND GDP-BINDING, PROTEIN LEVELS, AND DISRUPTION PHENOTYPE.
STRAIN=CRK6000;
PubMed=12427945;
Morimoto T., Loh P.C., Hirai T., Asai K., Kobayashi K., Moriya S.,
Ogasawara N.;
"Six GTP-binding proteins of the Era/Obg family are essential for cell
growth in Bacillus subtilis.";
Microbiology 148:3539-3552(2002).
-!- FUNCTION: An essential GTPase that binds both GDP and GTP, with
rapid nucleotide exchange. Plays a role in 16S rRNA processing and
30S ribosomal subunit biogenesis and possibly also in cell cycle
regulation and energy metabolism (By similarity). Binds both GDP
and GTP. Complements an E.coli era disruption mutant.
{ECO:0000250}.
-!- SUBUNIT: Monomer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane {ECO:0000250};
Peripheral membrane protein {ECO:0000250}.
-!- INDUCTION: Constitutively expressed, two-fold induced at the end
of the exponential phase; this is under control of Spo0A,
suggesting it may have a role in sporulation.
{ECO:0000269|PubMed:12399511}.
-!- DISRUPTION PHENOTYPE: Essential in some but not all strains; in
168 / BR151 the null mutation grows slowly and forms irregularly
shaped colonies after several days. In liquid culture forms chains
of elongated cells with diffuse nucleoids that occupy most of the
cell. Sporulation in this disruption strain is severely impaired.
Essential in strains CRK6000 and IS75, where it cannot be
disrupted. In CRK600 in depletion experiments cells become 1.5 to
2-fold longer and nucleoid distribution is dispersed. The number
of replication origins increases, suggesting an increase in
chromosome replication. {ECO:0000269|PubMed:12399511,
ECO:0000269|PubMed:12427945}.
-!- MISCELLANEOUS: Estimated to be present at 3000 copies per cell.
-!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-
like GTPase superfamily. Era GTPase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U18532; AAB59994.1; -; Genomic_DNA.
EMBL; D84432; BAA12482.1; -; Genomic_DNA.
EMBL; AL009126; CAB14458.1; -; Genomic_DNA.
EMBL; X17430; -; NOT_ANNOTATED_CDS; Genomic_DNA.
PIR; B69593; B69593.
RefSeq; NP_390407.1; NC_000964.3.
RefSeq; WP_003230051.1; NZ_JNCM01000036.1.
ProteinModelPortal; P42182; -.
SMR; P42182; -.
STRING; 224308.Bsubs1_010100013831; -.
PaxDb; P42182; -.
PRIDE; P42182; -.
EnsemblBacteria; CAB14458; CAB14458; BSU25290.
GeneID; 937871; -.
KEGG; bsu:BSU25290; -.
PATRIC; fig|224308.179.peg.2749; -.
eggNOG; ENOG4105CWT; Bacteria.
eggNOG; COG1159; LUCA.
HOGENOM; HOG000245596; -.
InParanoid; P42182; -.
KO; K03595; -.
OMA; KVAKDWQ; -.
PhylomeDB; P42182; -.
BioCyc; BSUB:BSU25290-MONOMER; -.
Proteomes; UP000001570; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
GO; GO:0070181; F:small ribosomal subunit rRNA binding; IEA:UniProtKB-UniRule.
GO; GO:0032297; P:negative regulation of DNA-dependent DNA replication initiation; IDA:CACAO.
GO; GO:0051781; P:positive regulation of cell division; IMP:CACAO.
GO; GO:0042274; P:ribosomal small subunit biogenesis; IEA:UniProtKB-UniRule.
CDD; cd04163; Era; 1.
Gene3D; 3.30.300.20; -; 1.
HAMAP; MF_00367; GTPase_Era; 1.
InterPro; IPR030388; G_ERA_dom.
InterPro; IPR005662; GTP-bd_Era.
InterPro; IPR006073; GTP_binding_domain.
InterPro; IPR015946; KH_dom-like_a/b.
InterPro; IPR004044; KH_dom_type_2.
InterPro; IPR009019; KH_sf_prok-type.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR005225; Small_GTP-bd_dom.
Pfam; PF07650; KH_2; 1.
Pfam; PF01926; MMR_HSR1; 1.
PRINTS; PR00326; GTP1OBG.
SUPFAM; SSF52540; SSF52540; 1.
SUPFAM; SSF54814; SSF54814; 1.
TIGRFAMs; TIGR00436; era; 1.
TIGRFAMs; TIGR00231; small_GTP; 1.
PROSITE; PS51713; G_ERA; 1.
PROSITE; PS50823; KH_TYPE_2; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Cytoplasm; GTP-binding; Membrane;
Nucleotide-binding; Reference proteome; Ribosome biogenesis;
RNA-binding; rRNA-binding.
CHAIN 1 301 GTPase Era.
/FTId=PRO_0000179997.
DOMAIN 7 174 Era-type G.
DOMAIN 205 282 KH type-2.
NP_BIND 15 22 GTP. {ECO:0000255}.
NP_BIND 62 66 GTP. {ECO:0000255}.
NP_BIND 124 127 GTP. {ECO:0000255}.
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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