IED ID |
IndEnz0002006917 |
Enzyme Type ID |
protease006917 |
Protein Name |
Hemagglutinin A
|
Gene Name |
hagA PG_1837 |
Organism |
Porphyromonas gingivalis (strain ATCC BAA-308 / W83) |
Taxonomic Lineage |
cellular organisms
Bacteria
FCB group
Bacteroidetes/Chlorobi group
Bacteroidetes
Bacteroidia
Bacteroidales
Porphyromonadaceae
Porphyromonas
Porphyromonas gingivalis
Porphyromonas gingivalis (strain ATCC BAA-308 / W83)
|
Enzyme Sequence |
MRKLNSLFSLAVLLSLLCWGQTAAAQGGPKTAPSVTHQAVQKGIRTSKAKDLRDPIPAGMARIILEAHDVWEDGTGYQMLWDADHNQYGASIPEESFWFANGTIPAGLYDPFEYKVPVNADASFSPTNFVLDGTASADIPAGTYDYVIINPNPGIIYIVGEGVSKGNDYVVEAGKTYHFTVQRQGPGDAASVVVTGEGGNEFAPVQNLQWSVSGQTVTLTWQAPASDKRTYVLNESFDTQTLPNGWTMIDADGDGHNWLSTINVYNTATHTGDGAMFSKSWTASSGAKIDLSPDNYLVTPKFTVPENGKLSYWVSSQEPWTNEHYGVFLSTTGNEAANFTIKLLEETLGSGKPAPMNLVKSEGVKAPAPYQERTIDLSAYAGQQVYLAFRHFGCTGIFRLYLDDVAVSGEGSSNDYTYTVYRDNVVIAQNLTATTFNQENVAPGQYNYCVEVKYTAGVSPKVCKDVTVEGSNEFAPVQNLTGSAVGQKVTLKWDAPNGTPNPNPGTTTLSESFENGIPASWKTIDADGDGNNWTTTPPPGGSSFAGHNSAICVSSASYINFEGPQNPDNYLVTPELSLPNGGTLTFWVCAQDANYASEHYAVYASSTGNDASNFANALLEEVLTAKTVVTAPEAIRGTRVQGTWYQKTVQLPAGTKYVAFRHFGCTDFFWINLDDVEIKANGKRADFTETFESSTHGEAPAEWTTIDADGDGQGWLCLSSGQLGWLTAHGGTNVVASFSWNGMALNPDNYLISKDVTGATKVKYYYAVNDGFPGDHYAVMISKTGTNAGDFTVVFEETPNGINKGGARFGLSTEANGAKPQSVWIERTVDLPAGTKYVAFRHYNCSDLNYILLDDIQFTMGGSPTPTDYTYTVYRDGTKIKEGLTETTFEEDGVATGNHEYCVEVKYTAGVSPKECVNVTVDPVQFNPVQNLTGSAVGQKVTLKWDAPNGTPNPNPGTTTLSESFENGIPASWKTIDADGDGNNWTTTPPPGGTSFAGHNSAICVSSASYINFEGPQNPDNYLVTPELSLPNGGTLTFWVCAQDANYASEHYAVYASSTGNDASNFANALLEEVLTAKTVVTAPEAIRGTRVQGTWYQKTVQLPAGTKYVAFRHFGCTDFFWINLDDVEIKANGKRADFTETFESSTHGEAPAEWTTIDADGDGQGWLCLSSGQLDWLTAHGGTNVVASFSWNGMALNPDNYLISKDVTGATKVKYYYAVNDGFPGDHYAVMISKTGTNAGDFTVVFEETPNGINKGGARFGLSTEANGAKPQSVWIERTVDLPAGTKYVAFRHYNCSDLNYILLDDIQFTMGGSPTPTDYTYTVYRDGTKIKEGLTETTFEEDGVATGNHEYCVEVKYTAGVSPKECVNVTVDPVQFNPVQNLTGSAVGQKVTLKWDAPNGTPNPNPGTTTLSESFENGIPASWKTIDADGDGNNWTTTPPPGGTSFAGHNSAICVSSASYINFEGPQNPDNYLVTPELSLPNGGTLTFWVCAQDANYASEHYAVYASSTGNDASNFANALLEEVLTAKTVVTAPEAIRGTRVQGTWYQKTVQLPAGTKYVAFRHFGCTDFFWINLDDVEIKANGKRADFTETFESSTHGEAPAEWTTIDADGDGQGWLCLSSGQLGWLTAHGGTNVVASFSWNGMALNPDNYLISKDVTGATKVKYYYAVNDGFPGDHYAVMISKTGTNAGDFTVVFEETPNGINKGGARFGLSTEANGAKPQSVWIERTVDLPAGTKYVAFRHYNCSDLNYILLDDIQFTMGGSPTPTDYTYTVYRDGTKIKEGLTETTFEEDGVATGNHEYCVEVKYTAGVSPKECVNVTINPTQFNPVQNLTAEQAPNSMDAILKWNAPASKRAEVLNEDFENGIPASWKTIDADGDGNNWTTTPPPGGSSFAGHNSAICVSSASYINFEGPQNPDNYLVTPELSLPGGGTLTFWVCAQDANYASEHYAVYASSTGNDASNFANALLEEVLTAKTVVTAPEAIRGTRVQGTWYQKTVQLPAGTKYVAFRHFGCTDFFWINLDDVVITSGNAPSYTYTIYRNNTQIASGVTETTYRDPDLATGFYTYGVKVVYPNGESAIETATLNITSLADVTAQKPYTLTVVGKTITVTCQGEAMIYDMNGRRLAAGRNTVVYTAQGGHYAVMVVVDGKSYVEKLAVK |
Enzyme Length |
2164 |
Uniprot Accession Number |
P59915 |
Absorption |
|
Active Site |
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Activity Regulation |
|
Binding Site |
|
Calcium Binding |
|
catalytic Activity |
|
DNA Binding |
|
EC Number |
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Enzyme Function |
FUNCTION: Agglutinates erythrocytes. {ECO:0000250}. |
Temperature Dependency |
|
PH Dependency |
|
Pathway |
|
nucleotide Binding |
|
Features |
Beta strand (12); Chain (1); Compositional bias (2); Erroneous initiation (1); Helix (1); Region (5); Signal peptide (1); Turn (1) |
Keywords |
3D-structure;Hemagglutinin;Hydrolase;Protease;Reference proteome;Repeat;Signal;Thiol protease;Virulence |
Interact With |
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Induction |
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Subcellular Location |
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Modified Residue |
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Post Translational Modification |
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Signal Peptide |
SIGNAL 1..25; /evidence=ECO:0000255 |
Structure 3D |
X-ray crystallography (1) |
Cross Reference PDB |
3KM5;
|
Mapped Pubmed ID |
20233299;
|
Motif |
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Gene Encoded By |
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Mass |
233,389 |
Kinetics |
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Metal Binding |
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Rhea ID |
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Cross Reference Brenda |
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