GONUTS has been updated to MW1.31 Most things seem to be working but be sure to report problems.

Have any questions? Please email us at ecoliwiki@gmail.com

MYCTU:CLPX

From GONUTS
Jump to: navigation, search
Species (Taxon ID) Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv). (83332)
Gene Name(s) clpX (ECO:0000255 with HAMAP-Rule:MF_00175)
Protein Name(s) ATP-dependent Clp protease ATP-binding subunit ClpX (ECO:0000255 with HAMAP-Rule:MF_00175)
External Links
UniProt P9WPB9
EMBL AL123456
PIR H70864
RefSeq NP_216973.1
YP_006515894.1
ProteinModelPortal P9WPB9
SMR P9WPB9
GeneID 13319167
888167
KEGG mtu:Rv2457c
mtv:RVBD_2457c
TubercuList Rv2457c
KO K03544
OMA HYKRINT
PhylomeDB P9WPB9
Proteomes UP000001584
GO GO:0005618
GO:0005524
GO:0008270
GO:0040007
GO:0006457
Gene3D 3.40.50.300
HAMAP MF_00175
InterPro IPR003593
IPR003959
IPR019489
IPR004487
IPR027417
IPR010603
Pfam PF07724
PF10431
PF06689
SMART SM00382
SM01086
SM00994
SUPFAM SSF52540
TIGRFAMs TIGR00382

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0051302

regulation of cell division

PMID:20625433[1]

ECO:0000314

P

Figure 2A is a light scatter assay that shows the amount of FtsZ polymerization. FtsZ polymerization is necessary for FtsZ ring formation and cell division. Figure 2A shows that for M. tuberculosis mutant without a function ClpX gene has a higher level of FtsZ polymerization than the wild type strain. This indicates that ClpX inhibits cell division.

complete
CACAO 4941

GO:0032272

negative regulation of protein polymerization

PMID:20625433[1]

ECO:0000314

P

Figure 2 show that ClpX inhibits FtsZ polymerization activity. Ftsz interacts directly with Clpx. And ClpX inhibition of FtsZ assembly is independent of the GTP hydrolysis activity of FtsZ

complete
CACAO 6909

GO:0051301

cell division

PMID:20625433[1]

ECO:0000315

P

Fig 6C

complete
CACAO 6910

involved_in

GO:0051301

cell division

PMID:20625433[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0032272

negative regulation of protein polymerization

PMID:20625433[1]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005618

cell wall

PMID:15525680[2]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0051301

cell division

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10159
PANTHER:PTN000137358
UniProtKB:P9WPB9

P

Seeded From UniProt

complete

involved_in

GO:0030163

protein catabolic process

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000137292
UniProtKB:P50866

P

Seeded From UniProt

complete

part_of

GO:0005759

mitochondrial matrix

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000137292
SGD:S000000431
TAIR:locus:2154257
UniProtKB:O76031

C

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10159
MGI:MGI:1346017
PANTHER:PTN000137292
SGD:S000000431

F

Seeded From UniProt

complete

enables

GO:0004176

ATP-dependent peptidase activity

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10159
PANTHER:PTN000137292
UniProtKB:O76031

F

Seeded From UniProt

complete

involved_in

GO:0006508

proteolysis

GO_REF:0000108

ECO:0000364

evidence based on logical inference from manual annotation used in automatic assertion

GO:0004176

P

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR003959
InterPro:IPR004487

F

Seeded From UniProt

complete

involved_in

GO:0006457

protein folding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR004487

P

Seeded From UniProt

complete

enables

GO:0008270

zinc ion binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR010603

F

Seeded From UniProt

complete

enables

GO:0046983

protein dimerization activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR010603

F

Seeded From UniProt

complete

enables

GO:0051082

unfolded protein binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR004487

F

Seeded From UniProt

complete

involved_in

GO:0006457

protein folding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000001454

P

Seeded From UniProt

complete

enables

GO:0051082

unfolded protein binding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000001454

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000001454

F

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0067

F

Seeded From UniProt

complete

enables

GO:0000166

nucleotide binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0547

F

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 1.2 1.3 1.4 Dziedzic, R et al. (2010) Mycobacterium tuberculosis ClpX interacts with FtsZ and interferes with FtsZ assembly. PLoS ONE 5 e11058 PubMed GONUTS page
  2. Mawuenyega, KG et al. (2005) Mycobacterium tuberculosis functional network analysis by global subcellular protein profiling. Mol. Biol. Cell 16 396-404 PubMed GONUTS page
  3. 3.0 3.1 3.2 3.3 3.4 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page