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-NOV-2018, entry version 93. 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). RN [2] {ECO:0000213|PDB:3WQB} RP X-RAY CRYSTALLOGRAPHY (1.41 ANGSTROMS) OF 25-624 IN COMPLEX WITH RP CALCIUM, AND DISULFIDE BONDS. RX DOI=10.1074/jbc.M114.622852; RA Kobayashi H., Yoshida T., Miyakawa T., Tashiro M., Okamoto K., RA Yamanaka H., Tanokura M., Tsuge H.; RT "Structural basis for action of the external chaperone for a RT propeptide-deficient serine protease from Aeromonas sobria."; RL J. Biol. Chem. 0:0-0(2015). 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 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 KO; K20755; -. 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_converta; 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:0000213|PDB:3HJR, ECO:0000213|PDB:3WQB}; KW Calcium {ECO:0000213|PDB:3HJR, ECO:0000213|PDB:3WQB}; KW Hydrolase {ECO:0000256|RuleBase:RU003355}; KW Metal-binding {ECO:0000213|PDB:3HJR, ECO:0000213|PDB:3WQB}; KW Protease {ECO:0000256|RuleBase:RU003355, ECO:0000313|EMBL:AAF64521.2}; KW Serine protease {ECO:0000256|RuleBase:RU003355}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 24 {ECO:0000256|SAM:SignalP}. FT CHAIN 25 624 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004329932. FT DOMAIN 456 622 P/Homo B. {ECO:0000259|PROSITE:PS51829}. FT METAL 53 53 Calcium 1. {ECO:0000213|PDB:3HJR, FT ECO:0000213|PDB:3WQB}. FT METAL 111 111 Calcium 1. {ECO:0000213|PDB:3WQB}. FT METAL 150 150 Calcium 1; via carbonyl oxygen. FT {ECO:0000213|PDB:3HJR, ECO:0000213|PDB: FT 3WQB}. FT METAL 152 152 Calcium 1. {ECO:0000213|PDB:3HJR, FT ECO:0000213|PDB:3WQB}. FT METAL 154 154 Calcium 1; via carbonyl oxygen. FT {ECO:0000213|PDB:3HJR, ECO:0000213|PDB: FT 3WQB}. FT METAL 156 156 Calcium 1; via carbonyl oxygen. FT {ECO:0000213|PDB:3HJR, ECO:0000213|PDB: FT 3WQB}. FT METAL 321 321 Calcium 2. {ECO:0000213|PDB:3HJR, FT ECO:0000213|PDB:3WQB}. FT METAL 322 322 Calcium 2; via carbonyl oxygen. FT {ECO:0000213|PDB:3HJR, ECO:0000213|PDB: FT 3WQB}. FT METAL 324 324 Calcium 2; via carbonyl oxygen. FT {ECO:0000213|PDB:3HJR, ECO:0000213|PDB: FT 3WQB}. FT METAL 327 327 Calcium 2; via carbonyl oxygen. FT {ECO:0000213|PDB:3HJR, ECO:0000213|PDB: FT 3WQB}. FT METAL 330 330 Calcium 2; via carbonyl oxygen. FT {ECO:0000213|PDB:3HJR, ECO:0000213|PDB: FT 3WQB}. FT METAL 350 350 Calcium 2; via carbonyl oxygen. FT {ECO:0000213|PDB:3HJR, ECO:0000213|PDB: FT 3WQB}. FT METAL 478 478 Calcium 3. {ECO:0000213|PDB:3HJR, FT ECO:0000213|PDB:3WQB}. FT METAL 512 512 Calcium 3. {ECO:0000213|PDB:3HJR, FT ECO:0000213|PDB:3WQB}. FT METAL 577 577 Calcium 3. {ECO:0000213|PDB:3HJR, FT ECO:0000213|PDB:3WQB}. FT METAL 579 579 Calcium 3; via carbonyl oxygen. FT {ECO:0000213|PDB:3WQB}. FT METAL 602 602 Calcium 3. {ECO:0000213|PDB:3HJR, FT ECO:0000213|PDB:3WQB}. FT METAL 603 603 Calcium 3. {ECO:0000213|PDB:3HJR, FT ECO:0000213|PDB:3WQB}. FT DISULFID 28 48 {ECO:0000213|PDB:3HJR, ECO:0000213|PDB: FT 3WQB}. FT DISULFID 325 350 {ECO:0000213|PDB:3HJR, ECO:0000213|PDB: FT 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 //