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BACAN:Q81QA6

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Species (Taxon ID) Bacillus anthracis. (1392)
Gene Name(s) yodJ (ECO:0000313 with EMBL:BAR76759.1)
Protein Name(s) D-alanyl-D-alanine carboxypeptidase (ECO:0000313 with EMBL:APT25987.1)

D-alanyl-D-alanine carboxypeptidase family protein (ECO:0000313 with EMBL:AAT31639.1) Putative carboxypeptidase yodJ (ECO:0000313 with EMBL:BAR76759.1)

External Links
UniProt Q81QA6
EMBL AE017334
CP009902
CP018903
CP019588
AP014833
MJAW01000040
RefSeq WP_001220642.1
PDB 4JID
4MPH
PDBsum 4JID
4MPH
STRING 198094.BA_2526
MEROPS M15.024
DNASU 1085538
EnsemblBacteria AAT31639
AJH88324
KOM61698
KOM66476
KOM74449
KOM80004
KOM85818
KOM90967
KON02983
KON17777
KON20449
KOR56617
KOR64877
KEGG banh:HYU01_12540
bar:GBAA_2526
eggNOG ENOG4108VXD
COG1876
HOGENOM HOG000038988
KO K07260
OMA ELSFANT
Proteomes UP000000594
UP000031920
UP000185489
UP000186718
UP000187792
GO GO:0016021
GO:0004180
GO:0046872
Gene3D 3.30.1380.10
InterPro IPR009045
IPR003709
Pfam PF02557
SUPFAM SSF55166

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0004180

carboxypeptidase activity

PMID:24909784[1]

ECO:0000314

F

This protein is carboxypeptidase activity because in the introduction of the paper, the terminal D-alanine of the nascent pentapeptide stem is hydrolyzed by DD-carboxypeptidases from the class C penicillin binding protein. Also membrane preparations of Bacillus subtilis have shown strong LD-carboxypeptidase against cell wall derived tetrapeptides.

complete
CACAO 12879

involved_in

GO:0006508

proteolysis

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR003709

P

Seeded From UniProt

complete

enables

GO:0008233

peptidase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR003709

F

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000038

ECO:0000323

imported automatically asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

enables

GO:0004180

carboxypeptidase activity

GO_REF:0000038

ECO:0000323

imported automatically asserted information used in automatic assertion

UniProtKB-KW:KW-0121

F

Seeded From UniProt

complete

Notes

References

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

  1. Hoyland, CN et al. (2014) Structure of the LdcB LD-carboxypeptidase reveals the molecular basis of peptidoglycan recognition. Structure 22 949-60 PubMed GONUTS page