ID Q9L5A4_AERSO Unreviewed; 624 AA. AC Q9L5A4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 2. DT 03-AUG-2022, entry version 105. DE SubName: Full=Extracellular serine protease {ECO:0000313|EMBL:AAF64521.2}; OS Aeromonas sobria. OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales; OC Aeromonadaceae; Aeromonas. OX NCBI_TaxID=646 {ECO:0000313|EMBL:AAF64521.2}; RN [1] {ECO:0000313|EMBL:AAF64521.2, ECO:0007829|PDB:3HJR} RP NUCLEOTIDE SEQUENCE. RC STRAIN=288 {ECO:0000313|EMBL:AAF64521.2}; RX PubMed=19654332; DOI=10.1074/jbc.M109.006114; RA Kobayashi H., Utsunomiya H., Yamanaka H., Sei Y., Katunuma N., Okamoto K., RA Tsuge H.; RT "Structural basis for the kexin-like serine protease from Aeromonas sobria RT as sepsis-causing factor."; RL J. Biol. Chem. 284:27655-27663(2009). RN [2] {ECO:0007829|PDB:3WQB} RP X-RAY CRYSTALLOGRAPHY (1.41 ANGSTROMS) OF 25-624 IN COMPLEX WITH CALCIUM, RP AND DISULFIDE BONDS. RX PubMed=25784551; DOI=10.1074/jbc.M114.622852; RA Kobayashi H., Yoshida T., Miyakawa T., Tashiro M., Okamoto K., Yamanaka H., RA Tanokura M., Tsuge H.; RT "Structural Basis for Action of the External Chaperone for a Propeptide- RT deficient Serine Protease from Aeromonas sobria."; RL J. Biol. Chem. 290:11130-11143(2015). CC -!- SIMILARITY: Belongs to the peptidase S8 family. CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|RuleBase:RU003355}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF253471; AAF64521.2; -; Genomic_DNA. DR PDB; 3HJR; X-ray; 1.65 A; A=25-624. DR PDB; 3WQB; X-ray; 1.41 A; A=25-624. DR PDBsum; 3HJR; -. DR PDBsum; 3WQB; -. DR SMR; Q9L5A4; -. DR MEROPS; S08.125; -. DR KEGG; ag:AAF64521; -. DR BioCyc; MetaCyc:MON-17932; -. DR BRENDA; 3.4.21.121; 169. DR EvolutionaryTrace; Q9L5A4; -. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR CDD; cd04059; Peptidases_S8_Protein_convertases_Kexins_Furin-like; 1. DR Gene3D; 3.40.50.200; -; 1. DR InterPro; IPR008979; Galactose-bd-like_sf. DR InterPro; IPR034182; Kexin/furin. DR InterPro; IPR002884; P_dom. DR InterPro; IPR000209; Peptidase_S8/S53_dom. DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf. DR InterPro; IPR023827; Peptidase_S8_Asp-AS. DR InterPro; IPR022398; Peptidase_S8_His-AS. DR InterPro; IPR023828; Peptidase_S8_Ser-AS. DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel. DR Pfam; PF01483; P_proprotein; 1. DR Pfam; PF00082; Peptidase_S8; 1. DR PRINTS; PR00723; SUBTILISIN. DR SUPFAM; SSF49785; SSF49785; 1. DR SUPFAM; SSF52743; SSF52743; 1. DR PROSITE; PS51829; P_HOMO_B; 1. DR PROSITE; PS00136; SUBTILASE_ASP; 1. DR PROSITE; PS00137; SUBTILASE_HIS; 1. DR PROSITE; PS00138; SUBTILASE_SER; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:3HJR, ECO:0007829|PDB:3WQB}; KW Calcium {ECO:0007829|PDB:3HJR, ECO:0007829|PDB:3WQB}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003355}; KW Metal-binding {ECO:0007829|PDB:3HJR, ECO:0007829|PDB:3WQB}; KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003355}; KW Serine protease {ECO:0000256|ARBA:ARBA00022825, KW ECO:0000256|RuleBase:RU003355}; Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..24 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 25..624 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5004329932" FT DOMAIN 456..622 FT /note="P/Homo B" FT /evidence="ECO:0000259|PROSITE:PS51829" FT REGION 116..140 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 120..140 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 53 FT /ligand="Calcium" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:3HJR, ECO:0007829|PDB:3WQB" FT BINDING 111 FT /ligand="Calcium" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:3WQB" FT BINDING 150 FT /ligand="Calcium" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:3HJR, ECO:0007829|PDB:3WQB" FT BINDING 152 FT /ligand="Calcium" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:3HJR, ECO:0007829|PDB:3WQB" FT BINDING 154 FT /ligand="Calcium" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:3HJR, ECO:0007829|PDB:3WQB" FT BINDING 156 FT /ligand="Calcium" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:3HJR, ECO:0007829|PDB:3WQB" FT BINDING 321 FT /ligand="Calcium" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:3HJR, ECO:0007829|PDB:3WQB" FT BINDING 322 FT /ligand="Calcium" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:3HJR, ECO:0007829|PDB:3WQB" FT BINDING 324 FT /ligand="Calcium" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:3HJR, ECO:0007829|PDB:3WQB" FT BINDING 327 FT /ligand="Calcium" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:3HJR, ECO:0007829|PDB:3WQB" FT BINDING 330 FT /ligand="Calcium" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:3HJR, ECO:0007829|PDB:3WQB" FT BINDING 350 FT /ligand="Calcium" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:3HJR, ECO:0007829|PDB:3WQB" FT BINDING 478 FT /ligand="Calcium" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:3HJR, ECO:0007829|PDB:3WQB" FT BINDING 512 FT /ligand="Calcium" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:3HJR, ECO:0007829|PDB:3WQB" FT BINDING 577 FT /ligand="Calcium" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:3HJR, ECO:0007829|PDB:3WQB" FT BINDING 579 FT /ligand="Calcium" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:3WQB" FT BINDING 602 FT /ligand="Calcium" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:3HJR, ECO:0007829|PDB:3WQB" FT BINDING 603 FT /ligand="Calcium" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:3HJR, ECO:0007829|PDB:3WQB" FT DISULFID 28..48 FT /evidence="ECO:0007829|PDB:3HJR, ECO:0007829|PDB:3WQB" FT DISULFID 325..350 FT /evidence="ECO:0007829|PDB:3HJR, ECO:0007829|PDB:3WQB" SQ SEQUENCE 624 AA; 66635 MW; 6B6F2DC8DE639531 CRC64; MKQTSLALAI TALLSTLPSA LVQANEGCAP LTGKESGMDI GRSSTERCLP GANPLQDQQW YLLNSGQDGF SARGGIAGND LNLWWAHRTG VLGQGVNVAV VDDGLAIAHP DLADNVRPGS KNVVTGSDDP TPTDPDTAHG TSVSGIIAAV DNAIGTKGIA PRAQLQGFNL LDDNSQQLQK DWLYALGDSN ASRDNRVFNQ SYGMSVVDPR SANSLDQSQL DRLFEQQTLK AQGAAYIKAA GNGFNKIAAG GYVLNRTGNG PKLPFENSNL DPSNSNFWNL VVSALNADGV RSSYSSVGSN IFLSATGGEY GTDTPAMVTT DLPGCDMGYN RTDDPSTNRL HGNSQLDASC DYNGVMNGTS SATPSTSGAM ALLMSAYPDL SVRDLRDLLA RSATRVDAKH QPVMVSYTSS TGKVRDVKGL EGWERNAAGM WFSPTYGFGL IDVNKALELA ANHQPLPPLV QLPWQKINVT GSAAAIADVG NSPTSSTTRI ATPLTVEAVQ VMVSLDHQRL PDLLIELVSP AGTRSILLSP FNSLVGQSLD QQQLGFVRTK GLRDMRMLSN KFYGESAQGT WRLEVTDVAN GTRQVSLLNR ETRERTTLTE RNNRQPGKLI SWSLRVLGHD ANRS //