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Protein

Probable GTP-binding protein EngB

Gene

engB

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Necessary for normal cell division and for the maintenance of normal septation.UniRule annotation
Binds GTP and GDP.

Cofactori

Mg2+UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi37 – 371MagnesiumUniRule annotation
Metal bindingi59 – 591MagnesiumUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi30 – 378GTPUniRule annotation
Nucleotide bindingi57 – 615GTPUniRule annotation
Nucleotide bindingi75 – 784GTPUniRule annotation
Nucleotide bindingi142 – 1454GTPUniRule annotation
Nucleotide bindingi174 – 1763GTPUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Septation

Keywords - Ligandi

GTP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciBSUB:BSU28190-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable GTP-binding protein EngBUniRule annotation
Gene namesi
Name:engBUniRule annotation
Synonyms:ysxC
Ordered Locus Names:BSU28190
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Disruption phenotypei

Essential for growth, it cannot be disrupted. In depletion experiments cells become over 3-fold longer, are abnormally curved and nucleoids condense.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 195195Probable GTP-binding protein EngBPRO_0000157736Add
BLAST

Proteomic databases

PaxDbiP38424.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
rplAQ067973EBI-6401087,EBI-6401093
rplFP468982EBI-6401087,EBI-6401129
rplLP023942EBI-6401087,EBI-6401150

Protein-protein interaction databases

IntActiP38424. 7 interactions.
STRINGi224308.Bsubs1_010100015401.

Structurei

Secondary structure

1
195
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 149Combined sources
Helixi15 – 173Combined sources
Beta strandi25 – 317Combined sources
Helixi36 – 449Combined sources
Beta strandi47 – 504Combined sources
Beta strandi54 – 563Combined sources
Beta strandi62 – 676Combined sources
Turni68 – 703Combined sources
Beta strandi71 – 755Combined sources
Beta strandi79 – 813Combined sources
Helixi86 – 10217Combined sources
Beta strandi106 – 1149Combined sources
Helixi121 – 13212Combined sources
Beta strandi137 – 1426Combined sources
Helixi144 – 1463Combined sources
Helixi149 – 1513Combined sources
Helixi152 – 16312Combined sources
Beta strandi169 – 1735Combined sources
Turni176 – 1783Combined sources
Helixi182 – 19312Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SULX-ray2.00A/B1-195[»]
1SVIX-ray1.95A1-195[»]
1SVWX-ray2.80A/B1-195[»]
ProteinModelPortaliP38424.
SMRiP38424. Positions 1-195.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP38424.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 195174EngB-type GUniRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. EngB GTPase family.UniRule annotation
Contains 1 EngB-type G (guanine nucleotide-binding) domain.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105WHM. Bacteria.
COG0218. LUCA.
HOGENOMiHOG000009833.
InParanoidiP38424.
KOiK03978.
OMAiNKHESMV.
OrthoDBiEOG6ND0NG.
PhylomeDBiP38424.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00321. GTPase_EngB.
InterProiIPR030393. G_ENGB_dom.
IPR019987. GTP-bd_ribosome_bio_YsxC.
IPR006073. GTP_binding_domain.
IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
[Graphical view]
PfamiPF01926. MMR_HSR1. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR03598. GTPase_YsxC. 1 hit.
TIGR00231. small_GTP. 1 hit.
PROSITEiPS51706. G_ENGB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P38424-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKVTKSEIVI SAVKPEQYPE GGLPEIALAG RSNVGKSSFI NSLINRKNLA
60 70 80 90 100
RTSSKPGKTQ TLNFYIINDE LHFVDVPGYG FAKVSKSERE AWGRMIETYI
110 120 130 140 150
TTREELKAVV QIVDLRHAPS NDDVQMYEFL KYYGIPVIVI ATKADKIPKG
160 170 180 190
KWDKHAKVVR QTLNIDPEDE LILFSSETKK GKDEAWGAIK KMINR
Length:195
Mass (Da):22,026
Last modified:October 1, 1994 - v1
Checksum:i12EC561C1806FFE3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X76424 Genomic DNA. Translation: CAA53985.1.
Z75208 Genomic DNA. Translation: CAA99541.1.
AL009126 Genomic DNA. Translation: CAB14779.1.
PIRiI40422.
RefSeqiNP_390697.1. NC_000964.3.
WP_003229621.1. NZ_JNCM01000036.1.

Genome annotation databases

EnsemblBacteriaiCAB14779; CAB14779; BSU28190.
GeneIDi938009.
KEGGibsu:BSU28190.
PATRICi18977514. VBIBacSub10457_2946.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X76424 Genomic DNA. Translation: CAA53985.1.
Z75208 Genomic DNA. Translation: CAA99541.1.
AL009126 Genomic DNA. Translation: CAB14779.1.
PIRiI40422.
RefSeqiNP_390697.1. NC_000964.3.
WP_003229621.1. NZ_JNCM01000036.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SULX-ray2.00A/B1-195[»]
1SVIX-ray1.95A1-195[»]
1SVWX-ray2.80A/B1-195[»]
ProteinModelPortaliP38424.
SMRiP38424. Positions 1-195.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP38424. 7 interactions.
STRINGi224308.Bsubs1_010100015401.

Proteomic databases

PaxDbiP38424.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB14779; CAB14779; BSU28190.
GeneIDi938009.
KEGGibsu:BSU28190.
PATRICi18977514. VBIBacSub10457_2946.

Phylogenomic databases

eggNOGiENOG4105WHM. Bacteria.
COG0218. LUCA.
HOGENOMiHOG000009833.
InParanoidiP38424.
KOiK03978.
OMAiNKHESMV.
OrthoDBiEOG6ND0NG.
PhylomeDBiP38424.

Enzyme and pathway databases

BioCyciBSUB:BSU28190-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP38424.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00321. GTPase_EngB.
InterProiIPR030393. G_ENGB_dom.
IPR019987. GTP-bd_ribosome_bio_YsxC.
IPR006073. GTP_binding_domain.
IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
[Graphical view]
PfamiPF01926. MMR_HSR1. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR03598. GTPase_YsxC. 1 hit.
TIGR00231. small_GTP. 1 hit.
PROSITEiPS51706. G_ENGB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, nucleotide sequence, and expression of the Bacillus subtilis lon gene."
    Riethdorf S., Voelker U., Gerth U., Winkler A., Engelmann S., Hecker M.
    J. Bacteriol. 176:6518-6527(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168 / IS58.
  2. "The dnaB-pheA (256 degrees-240 degrees) region of the Bacillus subtilis chromosome containing genes responsible for stress responses, the utilization of plant cell walls and primary metabolism."
    Wipat A., Carter N., Brignell C.S., Guy J.B., Piper K., Sanders J., Emmerson P.T., Harwood C.R.
    Microbiology 142:3067-3078(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168.
  3. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    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.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  4. "Six GTP-binding proteins of the Era/Obg family are essential for cell growth in Bacillus subtilis."
    Morimoto T., Loh P.C., Hirai T., Asai K., Kobayashi K., Moriya S., Ogasawara N.
    Microbiology 148:3539-3552(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: GTP- AND GDP-BINDING, PROTEIN LEVELS, DISRUPTION PHENOTYPE.
    Strain: CRK6000.

Entry informationi

Entry nameiENGB_BACSU
AccessioniPrimary (citable) accession number: P38424
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: July 6, 2016
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Estimated to be present at 1000 copies per cell.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.