ID A1DRD5_PSEU9 Unreviewed; 727 AA. AC A1DRD5; DT 23-JAN-2007, integrated into UniProtKB/TrEMBL. DT 23-JAN-2007, sequence version 1. DT 26-FEB-2020, entry version 100. DE SubName: Full=Secreted metalloprotease Mcp02 {ECO:0000313|EMBL:ABL06977.1}; GN Name=mcp02 {ECO:0000313|EMBL:ABL06977.1}; OS Pseudoalteromonas sp. (strain SM9913). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Pseudoalteromonadaceae; Pseudoalteromonas. OX NCBI_TaxID=234831 {ECO:0000313|EMBL:ABL06977.1}; RN [1] {ECO:0000313|EMBL:ABL06977.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SM9913 {ECO:0000313|EMBL:ABL06977.1}; RX PubMed=17464071; DOI=10.1099/mic.0.2006/003327-0; RA Qin G., Zhu L., Chen X., Wang P.G., Zhang Y.; RT "Structural characterization and ecological roles of a novel RT exopolysaccharide from the deep-sea psychrotolerant bacterium RT Pseudoalteromonas sp. SM9913."; RL Microbiology 153:1566-1572(2007). RN [2] {ECO:0000313|EMBL:ABL06977.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SM9913 {ECO:0000313|EMBL:ABL06977.1}; RX PubMed=19181663; DOI=10.1074/jbc.M808421200; RA Xie B.B., Bian F., Chen X.L., He H.L., Guo J., Gao X., Zeng Y.X., Chen B., RA Zhou B.C., Zhang Y.Z.; RT "Cold adaptation of zinc metalloproteases in the thermolysin family from RT deep sea and arctic sea ice bacteria revealed by catalytic and structural RT properties and molecular dynamics: new insights into relationship between RT conformational flexibility and hydrogen bonding."; RL J. Biol. Chem. 284:9257-9269(2009). RN [3] {ECO:0000213|PDB:3NQX, ECO:0000213|PDB:3NQY, ECO:0000213|PDB:3NQZ} RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 205-510 IN COMPLEX WITH CALCIUM RP AND ZINC, AND DISULFIDE BONDS. RX PubMed=20876133; DOI=10.1073/pnas.1005681107; RA Gao X., Wang J., Yu D.Q., Bian F., Xie B.B., Chen X.L., Zhou B.C., RA Lai L.H., Wang Z.X., Wu J.W., Zhang Y.Z.; RT "Structural basis for the autoprocessing of zinc metalloproteases in the RT thermolysin family."; RL Proc. Natl. Acad. Sci. U.S.A. 107:17569-17574(2010). 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; EF029091; ABL06977.1; -; Genomic_DNA. DR RefSeq; WP_013463300.1; NC_014800.1. DR PDB; 3NQX; X-ray; 1.70 A; A=205-510. DR PDB; 3NQY; X-ray; 2.60 A; A=25-204, B=205-519. DR PDB; 3NQZ; X-ray; 2.05 A; A=25-204, B=205-519. DR PDBsum; 3NQX; -. DR PDBsum; 3NQY; -. DR PDBsum; 3NQZ; -. DR SMR; A1DRD5; -. DR EnsemblBacteria; ADT70611; ADT70611; PSM_B0576. DR eggNOG; ENOG4105D4Y; Bacteria. DR eggNOG; COG2234; LUCA. DR eggNOG; COG3227; LUCA. DR OMA; SWYSGIG; -. DR OrthoDB; 1465483at2; -. DR BRENDA; 3.4.24.25; 12406. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR Gene3D; 1.10.390.10; -; 1. DR InterPro; IPR011096; FTP_domain. DR InterPro; IPR025711; PepSY. DR InterPro; IPR007280; Peptidase_C_arc/bac. DR InterPro; IPR023612; Peptidase_M4. DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf. DR InterPro; IPR001570; Peptidase_M4_C_domain. DR InterPro; IPR013856; Peptidase_M4_domain. DR Pfam; PF07504; FTP; 1. DR Pfam; PF03413; PepSY; 1. DR Pfam; PF01447; Peptidase_M4; 1. DR Pfam; PF02868; Peptidase_M4_C; 1. DR Pfam; PF04151; PPC; 2. DR PRINTS; PR00730; THERMOLYSIN. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:3NQX, ECO:0000213|PDB:3NQY, KW ECO:0000213|PDB:3NQZ}; KW Calcium {ECO:0000213|PDB:3NQY, ECO:0000213|PDB:3NQZ}; KW Hydrolase {ECO:0000313|EMBL:ABL06977.1}; KW Metal-binding {ECO:0000213|PDB:3NQY, ECO:0000213|PDB:3NQZ}; KW Metalloprotease {ECO:0000313|EMBL:ABL06977.1}; KW Protease {ECO:0000313|EMBL:ABL06977.1}; KW Zinc {ECO:0000213|PDB:3NQY, ECO:0000213|PDB:3NQZ}. FT METAL 345 FT /note="Zinc 1; via tele nitrogen" FT /evidence="ECO:0000213|PDB:3NQY" FT METAL 345 FT /note="Zinc 2; via tele nitrogen" FT /evidence="ECO:0000213|PDB:3NQZ" FT METAL 349 FT /note="Zinc 1; via tele nitrogen" FT /evidence="ECO:0000213|PDB:3NQY" FT METAL 349 FT /note="Zinc 2; via tele nitrogen" FT /evidence="ECO:0000213|PDB:3NQZ" FT METAL 369 FT /note="Zinc 1" FT /evidence="ECO:0000213|PDB:3NQY" FT METAL 377 FT /note="Calcium" FT /evidence="ECO:0000213|PDB:3NQY, ECO:0000213|PDB:3NQZ" FT METAL 380 FT /note="Calcium" FT /evidence="ECO:0000213|PDB:3NQY, ECO:0000213|PDB:3NQZ" FT METAL 388 FT /note="Calcium" FT /evidence="ECO:0000213|PDB:3NQY, ECO:0000213|PDB:3NQZ" FT METAL 390 FT /note="Calcium; via carbonyl oxygen" FT /evidence="ECO:0000213|PDB:3NQY, ECO:0000213|PDB:3NQZ" FT METAL 428 FT /note="Zinc 2; via tele nitrogen" FT /evidence="ECO:0000213|PDB:3NQZ" FT DISULFID 237..263 FT /evidence="ECO:0000213|PDB:3NQX, ECO:0000213|PDB:3NQY, FT ECO:0000213|PDB:3NQZ" FT DISULFID 482..510 FT /evidence="ECO:0000213|PDB:3NQY, ECO:0000213|PDB:3NQZ" SQ SEQUENCE 727 AA; 78276 MW; 8F5370995163F0E8 CRC64; MNLSKITIAT FAALTLVQAT NAVAANKKYL NQQPTINNMV QSNSASLLSV SPNQLIGLSV GNELVVLKEF TSNNGEVTRR YQQTYQGIPV IGDTVSLTFN NGMLKKAHGA AVYNIDEDLS DVSAKLTKKD AILKGSKTGI AAKSVGLKKH NEQSRLAIWV DDQNKAHLVY EVSYVTYGKS PSRPYLIIDA NTGEVLLSYD NLQHANATGP GGNLKTGKYL YGTDFDSLDV SQSGNTCSMN NANVRTINLN GGTSGSSAYS FTCPENTFKE INGAYSPLND AHFFGNVIFN MYNDWLGTAP LSFQLQMRVH YSSNYENAFW DGSAMTFGDG QNTFYPLVSL DVSAHEVSHG FTEQNSGLIY NGKPGGLNEA FSDMAGEAAE FYMKGSNDWL VGKDIFKGNG ALRYMNNPTQ DGRSIDNQSN YYSGMDVHYS SGVYNKAFYN LATTPGWDTQ KAFIVMARAN QLYWSAGVGW DLAGNGVMDA ACDLNYDPND VKAALAAVGV NSNLSSGSDC ATPQPPTDDE VLTNGVTRTG ISGAEKEQLF FTLEVPDGAT NLQFNTMGGS GDADLYVKFA SRPSLNNYDC NSTTSTSTES CNISNAQAGT YYVMVEAWSA ISGVLLTGSY SDGNGGVTPI NRTESNINVT TNNWSRFTQD LSEGYSTLNI SIAGGNGDAD LYVNFGSPSS TSSYLCRPYK NGNNEECTFD NPQAGTWYID LRGYSLASGV TLNVTAN //