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4WVJ

Crystal structure of the Type-I signal peptidase from Staphylococcus aureus (SpsB) in complex with an inhibitor peptide (pep3).

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0005515molecular_functionprotein binding
A0006465biological_processsignal peptide processing
A0006508biological_processproteolysis
A0006974biological_processDNA damage response
A0008236molecular_functionserine-type peptidase activity
A0008643biological_processcarbohydrate transport
A0015144molecular_functioncarbohydrate transmembrane transporter activity
A0015768biological_processmaltose transport
A0016020cellular_componentmembrane
A0030288cellular_componentouter membrane-bounded periplasmic space
A0034219biological_processcarbohydrate transmembrane transport
A0034289biological_processdetection of maltose stimulus
A0042597cellular_componentperiplasmic space
A0042956biological_processmaltodextrin transmembrane transport
A0043190cellular_componentATP-binding cassette (ABC) transporter complex
A0055052cellular_componentATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing
A0055085biological_processtransmembrane transport
A0060326biological_processcell chemotaxis
A0071702biological_processobsolete organic substance transport
A1901982molecular_functionmaltose binding
A1990060cellular_componentmaltose transport complex
Functional Information from PROSITE/UniProt
site_idPS00501
Number of Residues8
DetailsSPASE_I_1 Signal peptidases I serine active site. GESMDPTL
ChainResidueDetails
AGLY385-LEU392

site_idPS00760
Number of Residues13
DetailsSPASE_I_2 Signal peptidases I lysine active site. KRVIGvPGDkVeY
ChainResidueDetails
ALYS428-TYR440

site_idPS00761
Number of Residues14
DetailsSPASE_I_3 Signal peptidases I signature 3. YLVLGDNRevSkdS
ChainResidueDetails
ATYR493-SER506

site_idPS01037
Number of Residues18
DetailsSBP_BACTERIAL_1 Bacterial extracellular solute-binding proteins, family 1 signature. PIAvEalSLIYNkdlLpN
ChainResidueDetails
APRO113-ASN130

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000250
ChainResidueDetails
ASER387
ALYS428

221716

PDB entries from 2024-06-26

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