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 03-AUG-2022, entry version 142.
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:0000255|PROSITE-
CC ProRule:PRU01050, ECO:0000305}.
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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 AlphaFoldDB; P42182; -.
DR SMR; P42182; -.
DR STRING; 224308.BSU25290; -.
DR PaxDb; P42182; -.
DR PRIDE; P42182; -.
DR EnsemblBacteria; CAB14458; CAB14458; BSU_25290.
DR GeneID; 937871; -.
DR KEGG; bsu:BSU25290; -.
DR PATRIC; fig|224308.179.peg.2749; -.
DR eggNOG; COG1159; Bacteria.
DR InParanoid; P42182; -.
DR OMA; WAEVDVI; -.
DR PhylomeDB; P42182; -.
DR BioCyc; BSUB:BSU25290-MON; -.
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-templated 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 Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00367; GTPase_Era; 1.
DR InterPro; IPR030388; G_ERA_dom.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR005662; GTP-bd_Era.
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 PANTHER; PTHR42698; PTHR42698; 1.
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;
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 /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT DOMAIN 205..282
FT /note="KH type-2"
FT REGION 15..22
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 41..45
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 62..65
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 124..127
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT REGION 153..155
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01050"
FT BINDING 15..22
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 62..66
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 124..127
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
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
