| IED ID | IndEnz0002003227 |
| Enzyme Type ID | protease003227 |
| Protein Name |
Hemoglobin-binding protease hbp autotransporter EC 3.4.21.- Cleaved into: Hemoglobin-binding protease hbp; Hemoglobin-binding protease hbp translocator Helper peptide |
| Gene Name | hbp |
| Organism | Escherichia coli |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli |
| Enzyme Sequence | MNRIYSLRYSAVARGFIAVSEFARKCVHKSVRRLCFPVLLLIPVLFSAGSLAGTVNNELGYQLFRDFAENKGMFRPGATNIAIYNKQGEFVGTLDKAAMPDFSAVDSEIGVATLINPQYIASVKHNGGYTNVSFGDGENRYNIVDRNNAPSLDFHAPRLDKLVTEVAPTAVTAQGAVAGAYLDKERYPVFYRLGSGTQYIKDSNGQLTKMGGAYSWLTGGTVGSLSSYQNGEMISTSSGLVFDYKLNGAMPIYGEAGDSGSPLFAFDTVQNKWVLVGVLTAGNGAGGRGNNWAVIPLDFIGQKFNEDNDAPVTFRTSEGGALEWSFNSSTGAGALTQGTTTYAMHGQQGNDLNAGKNLIFQGQNGQINLKDSVSQGAGSLTFRDNYTVTTSNGSTWTGAGIVVDNGVSVNWQVNGVKGDNLHKIGEGTLTVQGTGINEGGLKVGDGKVVLNQQADNKGQVQAFSSVNIASGRPTVVLTDERQVNPDTVSWGYRGGTLDVNGNSLTFHQLKAADYGAVLANNVDKRATITLDYALRADKVALNGWSESGKGTAGNLYKYNNPYTNTTDYFILKQSTYGYFPTDQSSNATWEFVGHSQGDAQKLVADRFNTAGYLFHGQLKGNLNVDNRLPEGVTGALVMDGAADISGTFTQENGRLTLQGHPVIHAYNTQSVADKLAASGDHSVLTQPTSFSQEDWENRSFTFDRLSLKNTDFGLGRNATLNTTIQADNSSVTLGDSRVFIDKNDGQGTAFTLEEGTSVATKDADKSVFNGTVNLDNQSVLNINDIFNGGIQANNSTVNISSDSAVLGNSTLTSTALNLNKGANALASQSFVSDGPVNISDATLSLNSRPDEVSHTLLPVYDYAGSWNLKGDDARLNVGPYSMLSGNINVQDKGTVTLGGEGELSPDLTLQNQMLYSLFNGYRNIWSGSLNAPDATVSMTDTQWSMNGNSTAGNMKLNRTIVGFNGGTSPFTTLTTDNLDAVQSAFVMRTDLNKADKLVINKSATGHDNSIWVNFLKKPSNKDTLDIPLVSAPEATADNLFRASTRVVGFSDVTPILSVRKEDGKKEWVLDGYQVARNDGQGKAAATFMHISYNNFITEVNNLNKRMGDLRDINGEAGTWVRLLNGSGSADGGFTDHYTLLQMGADRKHELGSMDLFTGVMATYTDTDASADLYSGKTKSWGGGFYASGLFRSGAYFDVIAKYIHNENKYDLNFAGAGKQNFRSHSLYAGAEVGYRYHLTDTTFVEPQAELVWGRLQGQTFNWNDSGMDVSMRRNSVNPLVGRTGVVSGKTFSGKDWSLTARAGLHYEFDLTDSADVHLKDAAGEHQINGRKDSRMLYGVGLNARFGDNTRLGLEVERSAFGKYNTDDAINANIRYSF |
| Enzyme Length | 1377 |
| Uniprot Accession Number | O88093 |
| Absorption | |
| Active Site | ACT_SITE 125; /note=Charge relay system; ACT_SITE 153; /note=Charge relay system; ACT_SITE 259; /note=Charge relay system |
| Activity Regulation | ACTIVITY REGULATION: Protease activity is inhibited by 3,4-dichloroisocoumarin. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Interacts with hemoglobin, degrades it and subsequently binds the released heme. Could make heme accessible not only for E.coli, but also for B.fragilis during mixed intra-abdominal infections. Has a role in abscess formation. {ECO:0000269|PubMed:11748157, ECO:0000269|PubMed:9743528}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0. {ECO:0000269|PubMed:9743528}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (97); Chain (3); Domain (2); Helix (16); Signal peptide (1); Site (1); Turn (9) |
| Keywords | 3D-structure;Cell outer membrane;Direct protein sequencing;Hydrolase;Membrane;Periplasm;Plasmid;Protease;Secreted;Serine protease;Signal;Transmembrane;Transmembrane beta strand;Virulence;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: [Hemoglobin-binding protease hbp autotransporter]: Periplasm {ECO:0000250}.; SUBCELLULAR LOCATION: [Hemoglobin-binding protease hbp]: Secreted. Cell surface.; SUBCELLULAR LOCATION: [Hemoglobin-binding protease hbp translocator]: Cell outer membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=The cleaved C-terminal fragment (autotransporter domain) is localized in the outer membrane. {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | PTM: Cleaved to release the mature protein from the outer membrane. |
| Signal Peptide | SIGNAL 1..52; /evidence=ECO:0000269|PubMed:9743528 |
| Structure 3D | X-ray crystallography (3) |
| Cross Reference PDB | 1WXR; 3AEH; 3AK5; |
| Mapped Pubmed ID | 20615416; 21123869; |
| Motif | |
| Gene Encoded By | Plasmid IncFI ColV3-K30 |
| Mass | 148,257 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |