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P50743

- DER_BACSU

UniProt

P50743 - DER_BACSU

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Protein

GTPase Der

Gene

der

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

Functioni

GTPase that plays an essential role in the late steps of ribosome biogenesis.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi10 – 178GTP 1Sequence Analysis
Nucleotide bindingi57 – 615GTP 1Sequence Analysis
Nucleotide bindingi119 – 1224GTP 1Sequence Analysis
Nucleotide bindingi182 – 1898GTP 2Sequence Analysis
Nucleotide bindingi229 – 2335GTP 2Sequence Analysis
Nucleotide bindingi294 – 2974GTP 2Sequence Analysis

GO - Molecular functioni

  1. GTP binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. ribosome biogenesis Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Ribosome biogenesis

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciBSUB:BSU22840-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
GTPase Der
Alternative name(s):
GTP-binding protein EngA
Gene namesi
Name:der
Synonyms:engA, yphC
Ordered Locus Names:BSU22840
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU22840. [Micado]

Pathology & Biotechi

Disruption phenotypei

Essential for growth, it cannot be disrupted. Depletion experiments show that cells become longer and abnormally curved, with nucleoid condensation. Cells have many fewer 70S ribosomes; the large ribosomal subunit is 45S and is missing proteins L16, L27, L36 and interacts with 2 large non-ribosomal proteins.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 436436GTPase DerPRO_0000178964Add
BLAST

Proteomic databases

PaxDbiP50743.

Interactioni

Subunit structurei

Cofractionates with the 70S ribosome; association is stabilized by the non-hydrolyzable GTP analog GMPPNP, and inhibited by GTP or GDP.

Protein-protein interaction databases

STRINGi224308.BSU22840.

Structurei

Secondary structure

1
436
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 96Combined sources
Beta strandi11 – 155Combined sources
Helixi16 – 238Combined sources
Beta strandi24 – 263Combined sources
Beta strandi42 – 487Combined sources
Beta strandi51 – 577Combined sources
Helixi58 – 603Combined sources
Helixi68 – 8215Combined sources
Beta strandi84 – 918Combined sources
Turni92 – 943Combined sources
Helixi98 – 10710Combined sources
Beta strandi114 – 1196Combined sources
Helixi124 – 13613Combined sources
Beta strandi137 – 1393Combined sources
Beta strandi141 – 1433Combined sources
Turni146 – 1494Combined sources
Helixi152 – 1609Combined sources
Helixi161 – 1655Combined sources
Beta strandi176 – 1816Combined sources
Helixi188 – 1969Combined sources
Beta strandi201 – 2033Combined sources
Beta strandi215 – 2206Combined sources
Beta strandi223 – 2275Combined sources
Helixi230 – 2323Combined sources
Turni233 – 2353Combined sources
Turni236 – 2383Combined sources
Helixi245 – 25713Combined sources
Beta strandi259 – 2668Combined sources
Turni267 – 2693Combined sources
Helixi273 – 28412Combined sources
Beta strandi288 – 2947Combined sources
Helixi296 – 2983Combined sources
Helixi305 – 31612Combined sources
Helixi318 – 3203Combined sources
Beta strandi325 – 3273Combined sources
Turni330 – 3323Combined sources
Helixi336 – 3383Combined sources
Helixi339 – 35012Combined sources
Helixi356 – 36914Combined sources
Beta strandi374 – 3774Combined sources
Beta strandi382 – 3898Combined sources
Turni390 – 3934Combined sources
Beta strandi394 – 4007Combined sources
Helixi402 – 4043Combined sources
Helixi407 – 42115Combined sources
Beta strandi429 – 4335Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HJGX-ray2.50A1-436[»]
4DCSX-ray2.25A1-436[»]
4DCTX-ray2.30A1-436[»]
4DCUX-ray2.00A1-436[»]
4DCVX-ray2.60A1-436[»]
4KYUX-ray1.70A/B1-163[»]
ProteinModelPortaliP50743.
SMRiP50743. Positions 3-436.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP50743.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 167164EngA-type G 1Add
BLAST
Domaini176 – 351176EngA-type G 2Add
BLAST
Domaini352 – 43685KH-likeAdd
BLAST

Sequence similaritiesi

Contains 1 KH-like domain.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG1160.
HOGENOMiHOG000242861.
InParanoidiP50743.
KOiK03977.
OMAiSQGRGIN.
OrthoDBiEOG6DC6K1.
PhylomeDBiP50743.

Family and domain databases

Gene3Di3.30.300.20. 1 hit.
3.40.50.300. 2 hits.
HAMAPiMF_00195. GTPase_Der.
InterProiIPR016484. GTP-bd_EngA.
IPR006073. GTP_binding_domain.
IPR015946. KH_dom-like_a/b.
IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
[Graphical view]
PANTHERiPTHR11649:SF5. PTHR11649:SF5. 1 hit.
PfamiPF01926. MMR_HSR1. 2 hits.
[Graphical view]
PIRSFiPIRSF006485. GTP-binding_EngA. 1 hit.
SUPFAMiSSF52540. SSF52540. 2 hits.
TIGRFAMsiTIGR03594. GTPase_EngA. 1 hit.
TIGR00231. small_GTP. 2 hits.
PROSITEiPS51712. G_ENGA. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P50743-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGKPVVAIVG RPNVGKSTIF NRIAGERISI VEDTPGVTRD RIYSSAEWLN
60 70 80 90 100
YDFNLIDTGG IDIGDEPFLA QIRQQAEIAM DEADVIIFMV NGREGVTAAD
110 120 130 140 150
EEVAKILYRT KKPVVLAVNK LDNTEMRANI YDFYSLGFGE PYPISGTHGL
160 170 180 190 200
GLGDLLDAVA EHFKNIPETK YNEEVIQFCL IGRPNVGKSS LVNAMLGEER
210 220 230 240 250
VIVSNVAGTT RDAVDTSFTY NQQEFVIVDT AGMRKKGKVY ETTEKYSVLR
260 270 280 290 300
ALKAIDRSEV VAVVLDGEEG IIEQDKRIAG YAHEAGKAVV IVVNKWDAVD
310 320 330 340 350
KDESTMKEFE ENIRDHFQFL DYAPILFMSA LTKKRIHTLM PAIIKASENH
360 370 380 390 400
SLRVQTNVLN DVIMDAVAMN PTPTHNGSRL KIYYATQVSV KPPSFVVFVN
410 420 430
DPELMHFSYE RFLENRIRDA FGFEGTPIKI FARARK
Length:436
Mass (Da):48,770
Last modified:October 1, 1996 - v1
Checksum:iA5CC7028FFB5A442
GO

Sequence cautioni

The sequence U32164 differs from that shown. Reason: Frameshift at position 208. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti186 – 1872VG → CR(PubMed:9384377)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L47648 Genomic DNA. Translation: AAC83966.1.
AL009126 Genomic DNA. Translation: CAB14200.1.
U32164 Genomic DNA. No translation available.
PIRiA69936.
RefSeqiNP_390165.1. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB14200; CAB14200; BSU22840.
GeneIDi938988.
KEGGibsu:BSU22840.
PATRICi18976379. VBIBacSub10457_2380.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L47648 Genomic DNA. Translation: AAC83966.1 .
AL009126 Genomic DNA. Translation: CAB14200.1 .
U32164 Genomic DNA. No translation available.
PIRi A69936.
RefSeqi NP_390165.1. NC_000964.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2HJG X-ray 2.50 A 1-436 [» ]
4DCS X-ray 2.25 A 1-436 [» ]
4DCT X-ray 2.30 A 1-436 [» ]
4DCU X-ray 2.00 A 1-436 [» ]
4DCV X-ray 2.60 A 1-436 [» ]
4KYU X-ray 1.70 A/B 1-163 [» ]
ProteinModelPortali P50743.
SMRi P50743. Positions 3-436.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 224308.BSU22840.

Proteomic databases

PaxDbi P50743.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB14200 ; CAB14200 ; BSU22840 .
GeneIDi 938988.
KEGGi bsu:BSU22840.
PATRICi 18976379. VBIBacSub10457_2380.

Organism-specific databases

GenoListi BSU22840. [Micado ]

Phylogenomic databases

eggNOGi COG1160.
HOGENOMi HOG000242861.
InParanoidi P50743.
KOi K03977.
OMAi SQGRGIN.
OrthoDBi EOG6DC6K1.
PhylomeDBi P50743.

Enzyme and pathway databases

BioCyci BSUB:BSU22840-MONOMER.

Miscellaneous databases

EvolutionaryTracei P50743.

Family and domain databases

Gene3Di 3.30.300.20. 1 hit.
3.40.50.300. 2 hits.
HAMAPi MF_00195. GTPase_Der.
InterProi IPR016484. GTP-bd_EngA.
IPR006073. GTP_binding_domain.
IPR015946. KH_dom-like_a/b.
IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
[Graphical view ]
PANTHERi PTHR11649:SF5. PTHR11649:SF5. 1 hit.
Pfami PF01926. MMR_HSR1. 2 hits.
[Graphical view ]
PIRSFi PIRSF006485. GTP-binding_EngA. 1 hit.
SUPFAMi SSF52540. SSF52540. 2 hits.
TIGRFAMsi TIGR03594. GTPase_EngA. 1 hit.
TIGR00231. small_GTP. 2 hits.
PROSITEi PS51712. G_ENGA. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence analysis of the Bacillus subtilis chromosome region between the serA and kdg loci cloned in a yeast artificial chromosome."
    Sorokin A.V., Azevedo V., Zumstein E., Galleron N., Ehrlich S.D., Serror P.
    Microbiology 142:2005-2016(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / VKM B-501.
  2. "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.
  3. "Synthesis of sn-glycerol 3-phosphate, a key precursor of membrane lipids, in Bacillus subtilis."
    Morbidoni H.R., de Mendoza D., Cronan J.E. Jr.
    J. Bacteriol. 177:5899-5905(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 185-436.
    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.
  5. "Multiple GTPases participate in the assembly of the large ribosomal subunit in Bacillus subtilis."
    Schaefer L., Uicker W.C., Wicker-Planquart C., Foucher A.-E., Jault J.-M., Britton R.A.
    J. Bacteriol. 188:8252-8258(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH THE 50S RIBOSOMAL SUBUNIT, FUNCTION IN 50S RIBOSOMAL SUBUNIT BIOGENESIS.
    Strain: RB247.
  6. "The essential GTPase YphC displays a major domain rearrangement associated with nucleotide binding."
    Muench S.P., Xu L., Sedelnikova S.E., Rice D.W.
    Proc. Natl. Acad. Sci. U.S.A. 103:12359-12364(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) BOUND TO GDP IN THE PROBABLE OFF STATE.

Entry informationi

Entry nameiDER_BACSU
AccessioniPrimary (citable) accession number: P50743
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: October 29, 2014
This is version 108 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 7000 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

External Data

Dasty 3