ID Q9L5A4_AERSO Unreviewed; 624 AA. AC Q9L5A4; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 2. DT 07-APR-2021, entry version 102. 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:MONOMER-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 CDD; cd04059; Peptidases_S8_Protein_convertases_Kexins_Furin-like; 1. DR Gene3D; 2.60.120.260; -; 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 ECO:0000313|EMBL:AAF64521.2}; 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" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT METAL 53 FT /note="Calcium 1" FT /evidence="ECO:0007829|PDB:3HJR, ECO:0007829|PDB:3WQB" FT METAL 111 FT /note="Calcium 1" FT /evidence="ECO:0007829|PDB:3WQB" FT METAL 150 FT /note="Calcium 1; via carbonyl oxygen" FT /evidence="ECO:0007829|PDB:3HJR, ECO:0007829|PDB:3WQB" FT METAL 152 FT /note="Calcium 1" FT /evidence="ECO:0007829|PDB:3HJR, ECO:0007829|PDB:3WQB" FT METAL 154 FT /note="Calcium 1; via carbonyl oxygen" FT /evidence="ECO:0007829|PDB:3HJR, ECO:0007829|PDB:3WQB" FT METAL 156 FT /note="Calcium 1; via carbonyl oxygen" FT /evidence="ECO:0007829|PDB:3HJR, ECO:0007829|PDB:3WQB" FT METAL 321 FT /note="Calcium 2" FT /evidence="ECO:0007829|PDB:3HJR, ECO:0007829|PDB:3WQB" FT METAL 322 FT /note="Calcium 2; via carbonyl oxygen" FT /evidence="ECO:0007829|PDB:3HJR, ECO:0007829|PDB:3WQB" FT METAL 324 FT /note="Calcium 2; via carbonyl oxygen" FT /evidence="ECO:0007829|PDB:3HJR, ECO:0007829|PDB:3WQB" FT METAL 327 FT /note="Calcium 2; via carbonyl oxygen" FT /evidence="ECO:0007829|PDB:3HJR, ECO:0007829|PDB:3WQB" FT METAL 330 FT /note="Calcium 2; via carbonyl oxygen" FT /evidence="ECO:0007829|PDB:3HJR, ECO:0007829|PDB:3WQB" FT METAL 350 FT /note="Calcium 2; via carbonyl oxygen" FT /evidence="ECO:0007829|PDB:3HJR, ECO:0007829|PDB:3WQB" FT METAL 478 FT /note="Calcium 3" FT /evidence="ECO:0007829|PDB:3HJR, ECO:0007829|PDB:3WQB" FT METAL 512 FT /note="Calcium 3" FT /evidence="ECO:0007829|PDB:3HJR, ECO:0007829|PDB:3WQB" FT METAL 577 FT /note="Calcium 3" FT /evidence="ECO:0007829|PDB:3HJR, ECO:0007829|PDB:3WQB" FT METAL 579 FT /note="Calcium 3; via carbonyl oxygen" FT /evidence="ECO:0007829|PDB:3WQB" FT METAL 602 FT /note="Calcium 3" FT /evidence="ECO:0007829|PDB:3HJR, ECO:0007829|PDB:3WQB" FT METAL 603 FT /note="Calcium 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 //