ENGB_BACSU
ID ENGB_BACSU Reviewed; 195 AA.
AC P38424;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Probable GTP-binding protein EngB {ECO:0000255|HAMAP-Rule:MF_00321};
GN Name=engB {ECO:0000255|HAMAP-Rule:MF_00321}; Synonyms=ysxC;
GN OrderedLocusNames=BSU28190;
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 / IS58;
RX PubMed=7961402; DOI=10.1128/jb.176.21.6518-6527.1994;
RA Riethdorf S., Voelker U., Gerth U., Winkler A., Engelmann S., Hecker M.;
RT "Cloning, nucleotide sequence, and expression of the Bacillus subtilis lon
RT gene.";
RL J. Bacteriol. 176:6518-6527(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8969504; DOI=10.1099/13500872-142-11-3067;
RA Wipat A., Carter N., Brignell C.S., Guy J.B., Piper K., Sanders J.,
RA Emmerson P.T., Harwood C.R.;
RT "The dnaB-pheA (256 degrees-240 degrees) region of the Bacillus subtilis
RT chromosome containing genes responsible for stress responses, the
RT utilization of plant cell walls and primary metabolism.";
RL Microbiology 142:3067-3078(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 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: Necessary for normal cell division and for the maintenance of
CC normal septation. {ECO:0000255|HAMAP-Rule:MF_00321}.
CC -!- FUNCTION: Binds GTP and GDP.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00321};
CC -!- INTERACTION:
CC P38424; Q06797: rplA; NbExp=3; IntAct=EBI-6401087, EBI-6401093;
CC P38424; P46898: rplF; NbExp=2; IntAct=EBI-6401087, EBI-6401129;
CC P38424; P02394: rplL; NbExp=2; IntAct=EBI-6401087, EBI-6401150;
CC -!- DISRUPTION PHENOTYPE: Essential for growth, it cannot be disrupted. In
CC depletion experiments cells become over 3-fold longer, are abnormally
CC curved and nucleoids condense. {ECO:0000269|PubMed:12427945}.
CC -!- MISCELLANEOUS: Estimated to be present at 1000 copies per cell.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. EngB GTPase family. {ECO:0000255|HAMAP-
CC Rule:MF_00321}.
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DR EMBL; X76424; CAA53985.1; -; Genomic_DNA.
DR EMBL; Z75208; CAA99541.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14779.1; -; Genomic_DNA.
DR PIR; I40422; I40422.
DR RefSeq; NP_390697.1; NC_000964.3.
DR RefSeq; WP_003229621.1; NZ_JNCM01000036.1.
DR PDB; 1SUL; X-ray; 2.00 A; A/B=1-195.
DR PDB; 1SVI; X-ray; 1.95 A; A=1-195.
DR PDB; 1SVW; X-ray; 2.80 A; A/B=1-195.
DR PDBsum; 1SUL; -.
DR PDBsum; 1SVI; -.
DR PDBsum; 1SVW; -.
DR AlphaFoldDB; P38424; -.
DR SMR; P38424; -.
DR IntAct; P38424; 7.
DR STRING; 224308.BSU28190; -.
DR DrugBank; DB04315; Guanosine-5'-Diphosphate.
DR DrugBank; DB04137; Guanosine-5'-Triphosphate.
DR PaxDb; P38424; -.
DR PRIDE; P38424; -.
DR EnsemblBacteria; CAB14779; CAB14779; BSU_28190.
DR GeneID; 938009; -.
DR KEGG; bsu:BSU28190; -.
DR PATRIC; fig|224308.179.peg.3062; -.
DR eggNOG; COG0218; Bacteria.
DR InParanoid; P38424; -.
DR OMA; LMMDIRH; -.
DR PhylomeDB; P38424; -.
DR BioCyc; BSUB:BSU28190-MON; -.
DR EvolutionaryTrace; P38424; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR CDD; cd01876; YihA_EngB; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00321; GTPase_EngB; 1.
DR InterPro; IPR030393; G_ENGB_dom.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR019987; GTP-bd_ribosome_bio_YsxC.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR Pfam; PF01926; MMR_HSR1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR03598; GTPase_YsxC; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51706; G_ENGB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; GTP-binding; Magnesium;
KW Metal-binding; Nucleotide-binding; Reference proteome; Septation.
FT CHAIN 1..195
FT /note="Probable GTP-binding protein EngB"
FT /id="PRO_0000157736"
FT DOMAIN 22..195
FT /note="EngB-type G"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT BINDING 30..37
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT BINDING 37
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT BINDING 57..61
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT BINDING 59
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT BINDING 75..78
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT BINDING 142..145
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT BINDING 174..176
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00321"
FT STRAND 6..14
FT /evidence="ECO:0007829|PDB:1SVI"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:1SVI"
FT STRAND 25..31
FT /evidence="ECO:0007829|PDB:1SVI"
FT HELIX 36..44
FT /evidence="ECO:0007829|PDB:1SVI"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:1SVW"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:1SVW"
FT STRAND 62..67
FT /evidence="ECO:0007829|PDB:1SVI"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:1SVI"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:1SVI"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:1SVW"
FT HELIX 86..102
FT /evidence="ECO:0007829|PDB:1SVI"
FT STRAND 106..114
FT /evidence="ECO:0007829|PDB:1SVI"
FT HELIX 121..132
FT /evidence="ECO:0007829|PDB:1SVI"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:1SVI"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:1SVI"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:1SVI"
FT HELIX 152..163
FT /evidence="ECO:0007829|PDB:1SVI"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:1SVI"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:1SVI"
FT HELIX 182..193
FT /evidence="ECO:0007829|PDB:1SVI"
SQ SEQUENCE 195 AA; 22026 MW; 12EC561C1806FFE3 CRC64;
MKVTKSEIVI SAVKPEQYPE GGLPEIALAG RSNVGKSSFI NSLINRKNLA RTSSKPGKTQ
TLNFYIINDE LHFVDVPGYG FAKVSKSERE AWGRMIETYI TTREELKAVV QIVDLRHAPS
NDDVQMYEFL KYYGIPVIVI ATKADKIPKG KWDKHAKVVR QTLNIDPEDE LILFSSETKK
GKDEAWGAIK KMINR
