GO term: cell wall-bounded periplasmic space Help



Ontology: Cellular Component (GO:0030287)

Definition: The region between the plasma membrane and the cell wall, as found in organisms such as yeast and Gram positive bacteria. The region is thinner than the equivalent in Gram negative bacteria.

Synonyms: cell wall bounded periplasmic space; cell wall-enclosed periplasmic space

View Ontology: GO Tree Graph (graph) | Amigo (text)

Annotation Summary


This table lists the methods used to annotate genes either directly to the term cell wall-bounded periplasmic space (8 genes) or to its variants containing one or more qualifiers (0 genes). Note that some genes may have been annotated by more than one method so the numbers in the table below may not add up to the totals given here.

Annotation Method GO Term # Yeast Genes Annotated
Manually curated (download data) cell wall-bounded periplasmic space 8
High-throughput none none
Computational none none

Links to Additional Annotations:
Genes Annotated with this Term
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Annotation details for genes that have been directly annotated to the term cell wall-bounded periplasmic space or its variants containing one or more qualifiers (NOT, contributes to, or colocalizes with).

cell wall-bounded periplasmic space
     8 genes directly annotated to this term
Locus Evidence Annotation Method Reference Assigned By
APE2/YKL157W IDA: Inferred from Direct Assay
Assigned on 2008-08-19
manually curated Frey J and Rohm KH  (1979) External and internal forms of yeast aminopeptidase II. Eur J Biochem 97(1):169-73 SGD
ASP3-1/YLR155C IDA: Inferred from Direct Assay
Assigned on 2013-03-14
manually curated Dunlop PC and Roon RJ  (1975) L-Asparaginase of Saccharomyces cerevisiae: an extracellular Enzyme. J Bacteriol 122(3):1017-24 SGD
ASP3-2/YLR157C IDA: Inferred from Direct Assay
Assigned on 2013-03-14
manually curated Dunlop PC and Roon RJ  (1975) L-Asparaginase of Saccharomyces cerevisiae: an extracellular Enzyme. J Bacteriol 122(3):1017-24 SGD
ASP3-3/YLR158C IDA: Inferred from Direct Assay
Assigned on 2013-03-14
manually curated Dunlop PC and Roon RJ  (1975) L-Asparaginase of Saccharomyces cerevisiae: an extracellular Enzyme. J Bacteriol 122(3):1017-24 SGD
ASP3-4/YLR160C IDA: Inferred from Direct Assay
Assigned on 2013-03-14
manually curated Dunlop PC and Roon RJ  (1975) L-Asparaginase of Saccharomyces cerevisiae: an extracellular Enzyme. J Bacteriol 122(3):1017-24 SGD
ATH1/YPR026W IDA: Inferred from Direct Assay
Assigned on 2005-08-12
manually curated Jules M, et al.  (2004) Two distinct pathways for trehalose assimilation in the yeast Saccharomyces cerevisiae. Appl Environ Microbiol 70(5):2771-8 SGD
BAR1/YIL015W TAS: Traceable Author Statement
Assigned on 2007-09-19
manually curated Ballensiefen W and Schmitt HD  (1997) Periplasmic Bar1 protease of Saccharomyces cerevisiae is active before reaching its extracellular destination. Eur J Biochem 247(1):142-7 SGD
PHO3/YBR092C IMP: Inferred from Mutant Phenotype
Assigned on 2001-09-24
manually curated Nosaka K, et al.  (1989) A possible role for acid phosphatase with thiamin-binding activity encoded by PHO3 in yeast. FEMS Microbiol Lett 51(1):55-9 SGD