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MYCTU:FTSZ

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Species (Taxon ID) Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv). (83332)
Gene Name(s) ftsZ (ECO:0000255 with HAMAP-Rule:MF_00909)
Protein Name(s) Cell division protein FtsZ (ECO:0000255 with HAMAP-Rule:MF_00909)
External Links
UniProt P9WN95
EMBL AL123456
PIR B70579
RefSeq NP_216666.1
YP_006515569.1
PDB 1RLU
1RQ2
1RQ7
2Q1X
2Q1Y
4KWE
PDBsum 1RLU
1RQ2
1RQ7
2Q1X
2Q1Y
4KWE
ProteinModelPortal P9WN95
SMR P9WN95
BindingDB P9WN95
ChEMBL CHEMBL4213
GeneID 13316961
888369
KEGG mtu:Rv2150c
mtv:RVBD_2150c
TubercuList Rv2150c
KO K03531
OMA IHVTVIA
PhylomeDB P9WN95
Proteomes UP000001584
GO GO:0032153
GO:0005737
GO:0005886
GO:0043234
GO:0005525
GO:0003924
GO:0000287
GO:0000917
GO:0007049
GO:0043093
GO:0040007
GO:0006184
GO:0051258
Gene3D 3.30.1330.20
3.40.50.1440
HAMAP MF_00909
InterPro IPR000158
IPR020805
IPR024757
IPR008280
IPR018316
IPR003008
Pfam PF12327
PF00091
PRINTS PR00423
SMART SM00864
SM00865
SUPFAM SSF52490
SSF55307
TIGRFAMs TIGR00065
PROSITE PS01134
PS01135

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0022607

cellular component assembly

PMID:18436955[1]

ECO:0000314

P

Figure 2. Hg2Cl chelation of Cysteine residue impedes protein function and causes aggregation

complete
CACAO 9094

part_of

GO:0005886

plasma membrane

PMID:14532352[2]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0051258

protein polymerization

PMID:17644520[3]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0051258

protein polymerization

PMID:10869082[4]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0045787

positive regulation of cell cycle

PMID:11932443[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0003924

GTPase activity

PMID:17644520[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0003924

GTPase activity

PMID:10869082[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0000921

septin ring assembly

PMID:11932443[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0000287

magnesium ion binding

PMID:10869082[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0051301

cell division

PMID:21873635[6]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10347
PANTHER:PTN000768275
UniProtKB:P17865
UniProtKB:P47466

P

Seeded From UniProt

complete

part_of

GO:0032153

cell division site

PMID:21873635[6]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10347
PANTHER:PTN000768275

C

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

PMID:21873635[6]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10347
PANTHER:PTN000768275

C

Seeded From UniProt

complete

enables

GO:0005525

GTP binding

PMID:21873635[6]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10347
PANTHER:PTN000768275

F

Seeded From UniProt

complete

enables

GO:0003924

GTPase activity

PMID:21873635[6]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10347
PANTHER:PTN000768275
TAIR:locus:2049455
TAIR:locus:2161610
UniProtKB:P17865
UniProtKB:P9WN95

F

Seeded From UniProt

complete

enables

GO:0003924

GTPase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR003008

F

Seeded From UniProt

complete

enables

GO:0005525

GTP binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000158
InterPro:IPR020805

F

Seeded From UniProt

complete

part_of

GO:0032153

cell division site

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000100343

C

Seeded From UniProt

complete

involved_in

GO:0090529

cell septum assembly

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000100343

P

Seeded From UniProt

complete

enables

GO:0005525

GTP binding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000100343

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000100343

C

Seeded From UniProt

complete

enables

GO:0003924

GTPase activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000100343

F

Seeded From UniProt

complete

involved_in

GO:0043093

FtsZ-dependent cytokinesis

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000100343

P

Seeded From UniProt

complete

involved_in

GO:0051258

protein polymerization

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000100343

P

Seeded From UniProt

complete

enables

GO:0005525

GTP binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0342

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

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

involved_in

GO:0000917

division septum assembly

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0717

P

Seeded From UniProt

complete

involved_in

GO:0007049

cell cycle

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0131

P

Seeded From UniProt

complete

involved_in

GO:0051301

cell division

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0132

P

Seeded From UniProt

complete

Notes

References

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

  1. Jaiswal, R & Panda, D (2008) Cysteine 155 plays an important role in the assembly of Mycobacterium tuberculosis FtsZ. Protein Sci. 17 846-54 PubMed GONUTS page
  2. Gu, S et al. (2003) Comprehensive proteomic profiling of the membrane constituents of a Mycobacterium tuberculosis strain. Mol. Cell Proteomics 2 1284-96 PubMed GONUTS page
  3. 3.0 3.1 Chen, Y et al. (2007) Assembly dynamics of Mycobacterium tuberculosis FtsZ. J. Biol. Chem. 282 27736-43 PubMed GONUTS page
  4. 4.0 4.1 4.2 White, EL et al. (2000) Slow polymerization of Mycobacterium tuberculosis FtsZ. J. Bacteriol. 182 4028-34 PubMed GONUTS page
  5. 5.0 5.1 Dziadek, J et al. (2002) Physiological consequences associated with overproduction of Mycobacterium tuberculosis FtsZ in mycobacterial hosts. Microbiology (Reading, Engl.) 148 961-71 PubMed GONUTS page
  6. 6.0 6.1 6.2 6.3 6.4 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page