ID W6FJD2_NODSP Unreviewed; 518 AA.
AC W6FJD2;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Zinc protease {ECO:0000313|EMBL:AHJ27161.1};
DE EC=3.4.99.- {ECO:0000313|EMBL:AHJ27161.1};
GN ORFNames=NSP_8130 {ECO:0000313|EMBL:AHJ27161.1};
OS Nodularia spumigena CCY9414.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Aphanizomenonaceae;
OC Nodularia.
OX NCBI_TaxID=313624 {ECO:0000313|EMBL:AHJ27161.1, ECO:0000313|Proteomes:UP000019325};
RN [1] {ECO:0000313|EMBL:AHJ27161.1, ECO:0000313|Proteomes:UP000019325}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCY9414 {ECO:0000313|EMBL:AHJ27161.1};
RX PubMed=23555932;
RA Voss B., Bolhuis H., Fewer D.P., Kopf M., Moke F., Haas F., El-Shehawy R.,
RA Hayes P., Bergman B., Sivonen K., Dittmann E., Scanlan D.J., Hagemann M.,
RA Stal L.J., Hess W.R.;
RT "Insights into the physiology and ecology of the brackish-water-adapted
RT Cyanobacterium Nodularia spumigena CCY9414 based on a genome-transcriptome
RT analysis.";
RL PLoS ONE 8:E60224-E60224(2013).
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR EMBL; CP007203; AHJ27161.1; -; Genomic_DNA.
DR AlphaFoldDB; W6FJD2; -.
DR STRING; 313624.NSP_8130; -.
DR PATRIC; fig|313624.11.peg.816; -.
DR eggNOG; COG0612; Bacteria.
DR HOGENOM; CLU_009902_1_2_3; -.
DR Proteomes; UP000019325; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR001431; Pept_M16_Zn_BS.
DR InterPro; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR PANTHER; PTHR11851:SF229; PEPTIDASE M16 DOMAIN PROTEIN; 1.
DR Pfam; PF00675; Peptidase_M16; 2.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
DR PROSITE; PS00143; INSULINASE; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000313|EMBL:AHJ27161.1};
KW Protease {ECO:0000313|EMBL:AHJ27161.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..518
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004876902"
FT DOMAIN 67..115
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 165..263
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 270..448
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT COILED 119..165
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 518 AA; 58549 MW; 41FE2AC7CAAA6641 CRC64;
MVLVICWWGL LPNIAQAQAQ TQTANPLQRI RQFRQNPPEK TSIQPYLDRV IKQLTEFRLE
NGLKFIVLER HQAPVVSFLT YADVGGVDEP EGQTGVAHFL EHLAFKGTTR IGTKDYEAEK
LLLDRLEQLD AQIRTAKAND KQDDLAKLQT EFKQVESQAD TLVTQNEMGQ IVNQAGGVGL
NATTSSEATK YFYSFPSNKL KLWMSLESER FLEPVVRREF YKEKDVILEE RRMRVDNSPI
GMMVENLMDT AFTVHPYKRP VIGYEEDIRN LTPEDVQKFF DAHYVPSNLT IAVVGDVDPV
EVKKLAKIYF GRYQAKPKAT AKIPVEPPQA QTREFTLELA SQPWYLEGYH RPSVTHPDDA
VYQIIAGLLS NGRTSRLYKS LVEQQRLALN AQGFSGFPGD KYPNLMLFYA LTAPGHTVDE
VATALQQEIE KLKTEPVAEV DLQRVKTQAR ASLLLSLNSN MGMAQQLLEA EVKTGSWRNL
FKQLDDISAV TTADIQRVAK ATFTPENRTI GKLLSKQG
//
