ID A0A6P0Z9M2_9CYAN Unreviewed; 364 AA. AC A0A6P0Z9M2; DT 07-OCT-2020, integrated into UniProtKB/TrEMBL. DT 07-OCT-2020, sequence version 1. DT 22-FEB-2023, entry version 9. DE RecName: Full=Zinc metalloprotease {ECO:0000256|RuleBase:RU362031}; DE EC=3.4.24.- {ECO:0000256|RuleBase:RU362031}; GN Name=rseP {ECO:0000313|EMBL:NET70036.1}; GN ORFNames=F6K62_03005 {ECO:0000313|EMBL:NET70036.1}; OS Sphaerospermopsis sp. SIO1G2. OC Bacteria; Cyanobacteria; Nostocales; Aphanizomenonaceae; Sphaerospermopsis. OX NCBI_TaxID=2607815 {ECO:0000313|EMBL:NET70036.1, ECO:0000313|Proteomes:UP000471590}; RN [1] {ECO:0000313|EMBL:NET70036.1, ECO:0000313|Proteomes:UP000471590} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SIO1G2 {ECO:0000313|EMBL:NET70036.1}; RA Ferreira Leao T., Wang M., Moss N., Da Silva R., Sanders J., Nurk S., RA Gurevich A., Humphrey G., Reher R., Zhu Q., Belda-Ferre P., Glukhov E., RA Rex R., Dorrestein P.C., Knight R., Pevzner P., Gerwick W.H., Gerwick L.; RT "Insights into an expanded diversity of filamentous marine cyanobacterial RT genomes reveal an extraordinary biosynthetic potential."; RL Submitted (FEB-2020) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|ARBA:ARBA00001947, CC ECO:0000256|RuleBase:RU362031}; CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. CC -!- SIMILARITY: Belongs to the peptidase M50B family. CC {ECO:0000256|ARBA:ARBA00007931, ECO:0000256|RuleBase:RU362031}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:NET70036.1}. 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; JAAHFY010000018; NET70036.1; -; Genomic_DNA. DR AlphaFoldDB; A0A6P0Z9M2; -. DR Proteomes; UP000471590; Unassembled WGS sequence. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR CDD; cd00989; PDZ_metalloprotease; 1. DR CDD; cd06163; S2P-M50_PDZ_RseP-like; 1. DR Gene3D; 2.30.42.10; -; 1. DR InterPro; IPR001478; PDZ. DR InterPro; IPR041489; PDZ_6. DR InterPro; IPR036034; PDZ_sf. DR InterPro; IPR004387; Pept_M50_Zn. DR InterPro; IPR008915; Peptidase_M50. DR PANTHER; PTHR42837:SF2; MEMBRANE METALLOPROTEASE ARASP2, CHLOROPLASTIC-RELATED; 1. DR PANTHER; PTHR42837; REGULATOR OF SIGMA-E PROTEASE RSEP; 1. DR Pfam; PF17820; PDZ_6; 1. DR Pfam; PF02163; Peptidase_M50; 1. DR SMART; SM00228; PDZ; 1. DR SUPFAM; SSF50156; PDZ domain-like; 1. DR TIGRFAMs; TIGR00054; RIP metalloprotease RseP; 2. DR PROSITE; PS50106; PDZ; 1. PE 3: Inferred from homology; KW Hydrolase {ECO:0000256|RuleBase:RU362031}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362031}; KW Metal-binding {ECO:0000256|RuleBase:RU362031}; KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049, KW ECO:0000256|RuleBase:RU362031}; Protease {ECO:0000313|EMBL:NET70036.1}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, KW ECO:0000256|RuleBase:RU362031}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|RuleBase:RU362031}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU362031}. FT TRANSMEM 92..117 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362031" FT TRANSMEM 280..300 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362031" FT TRANSMEM 330..348 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362031" FT DOMAIN 128..159 FT /note="PDZ" FT /evidence="ECO:0000259|PROSITE:PS50106" SQ SEQUENCE 364 AA; 38999 MW; 3A4A176F8244D018 CRC64; MSVLAAIAVL AILILVHELG HFVAARSQGI YANRFSLGFG PTLLKYQGSE TEYTIRAFPL GGFVGFPDDD PDSEIPPNDP NLLRNRPILD RAIVISAGVI ANLIFAYLVL ALQIGIVGIP QEFQFKPGVV VKPISEQSVA YQAGIRAGDI ILSINGKELL ADKNAPALLT KEIQSHPLEE INLQVKHQDE IKPLTLTPTE NAEGKGLVGI ELVPNGKAIY RHPQNPIEIL TTAADRFQQL LVGTVKGFGQ LITNFQETAS QVSGPVNIVK IGAKLASDNI ANLLSFAAII SVNLAIINIL PLPALDGGQL AFLLIEGVLG KPLPAKIQEG VMQTGLVLLL GLGIFLIVKE TTQLDFVQQL IQGF //