ID Q9L5A4_AERSO Unreviewed; 624 AA. AC Q9L5A4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 2. DT 04-MAR-2015, entry version 73. 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:0000213|PDB:3HJR, ECO:0000313|EMBL:AAF64521.2} 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., RA Okamoto K., Tsuge H.; RT "Structural basis for the kexin-like serine protease from Aeromonas RT sobria as sepsis-causing factor."; RL J. Biol. Chem. 284:27655-27663(2009). CC -!- SIMILARITY: Belongs to the peptidase S8 family. CC {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 PDBsum; 3HJR; -. DR BioCyc; MetaCyc:MONOMER-17932; -. 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 Gene3D; 2.60.120.260; -; 1. DR Gene3D; 3.40.50.200; -; 1. DR InterPro; IPR008979; Galactose-bd-like. DR InterPro; IPR000209; Peptidase_S8/S53_dom. 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 InterPro; IPR002884; PrprotnconvertsP. DR PANTHER; PTHR10795; PTHR10795; 1. 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; 2. 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:0000213|PDB:3HJR}; Calcium {ECO:0000213|PDB:3HJR}; KW Hydrolase {ECO:0000256|RuleBase:RU004261}; KW Metal-binding {ECO:0000213|PDB:3HJR}; KW Protease {ECO:0000256|RuleBase:RU004261, ECO:0000313|EMBL:AAF64521.2}; KW Serine protease {ECO:0000256|RuleBase:RU004261}. 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 //