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ECO27:B7UJR0

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Species (Taxon ID) Escherichia coli O127:H6 (strain E2348/69 / EPEC). (574521)
Gene Name(s) No Information Provided.
Protein Name(s) ATP-dependent Clp protease proteolytic subunit (ECO:0000256 with HAMAP-Rule:MF_00444, ECO:0000256 with RuleBase:RU003567)

Endopeptidase Clp (ECO:0000256 with HAMAP-Rule:MF_00444)

External Links
UniProt B7UJR0
EMBL FM180568
RefSeq YP_002327949.1
ProteinModelPortal B7UJR0
SMR B7UJR0
STRING 574521.E2348C_0372
PRIDE B7UJR0
EnsemblBacteria CAS07920
GeneID 7061803
KEGG ecg:E2348C_0372
PATRIC 18339710
eggNOG COG0740
HOGENOM HOG000285833
KO K01358
OMA ARMNELM
OrthoDB EOG6Z3KQ0
BioCyc ECOL574521:GJAO-384-MONOMER
Proteomes UP000008205
GO GO:0005737
GO:0004252
Gene3D 3.90.226.10
HAMAP MF_00444
InterPro IPR001907
IPR029045
IPR023562
IPR018215
PANTHER PTHR10381
Pfam PF00574
PRINTS PR00127
SUPFAM SSF52096
TIGRFAMs TIGR00493
PROSITE PS00382
PS00381

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:1901800

positive regulation of proteasomal protein catabolic process

PMID:21529717[1]

ECO:0000314

P

Figure 6 - With ClpP in complex with ClpX, slippage of the protein occurs much less and thus the ClpP works to positively regulate the catabolic process of GFP.

complete
CACAO 9055

GO:0010498

proteasomal protein catabolic process

PMID:9573050[2]

ECO:0000314

P

Figure 4 - ClpP works with ClpA and ClpX in vitro to degrate SsrA-tagged proteins.

complete
CACAO 9056

enables

GO:0004252

serine-type endopeptidase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001907

F

Seeded From UniProt

complete

GO:1901800

positive regulation of proteasomal protein catabolic process

PMID:9573050[2]

ECO:0000315

P

Figure 5 shows ClpP- strains degrade the SsrA-tagged proteins more slowly than wild type strain, in vivo.

complete
CACAO 9057

involved_in

GO:0006508

proteolysis

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001907

P

Seeded From UniProt

complete

enables

GO:0016787

hydrolase activity

GO_REF:0000038

ECO:0000323

imported automatically asserted information used in automatic assertion

UniProtKB-KW:KW-0378

F

Seeded From UniProt

complete

enables

GO:0008233

peptidase activity

GO_REF:0000038

ECO:0000323

imported automatically asserted information used in automatic assertion

UniProtKB-KW:KW-0645

F

Seeded From UniProt

complete

involved_in

GO:0006508

proteolysis

GO_REF:0000038

ECO:0000323

imported automatically asserted information used in automatic assertion

UniProtKB-KW:KW-0645

P

Seeded From UniProt

complete

enables

GO:0008236

serine-type peptidase activity

GO_REF:0000038

ECO:0000323

imported automatically asserted information used in automatic assertion

UniProtKB-KW:KW-0720

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000038

ECO:0000323

imported automatically asserted information used in automatic assertion

UniProtKB-KW:KW-0963

C

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000040

ECO:0000323

imported automatically asserted information used in automatic assertion

UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000089051

C

Seeded From UniProt

complete

enables

GO:0004252

serine-type endopeptidase activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000089051

F

Seeded From UniProt

complete

involved_in

GO:0006508

proteolysis

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000089051

P

Seeded From UniProt

complete

Notes

References

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

  1. Maillard, RA et al. (2011) ClpX(P) generates mechanical force to unfold and translocate its protein substrates. Cell 145 459-69 PubMed GONUTS page
  2. 2.0 2.1 Gottesman, S et al. (1998) The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging system. Genes Dev. 12 1338-47 PubMed GONUTS page