ID   Y3971_NOSS1             Reviewed;         364 AA.
AC   Q8YQ64;
DT   15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Putative zinc metalloprotease all3971;
DE            EC=3.4.24.-;
GN   OrderedLocusNames=all3971;
OS   Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=103690;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX   PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA   Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA   Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT   "Complete genomic sequence of the filamentous nitrogen-fixing
RT   cyanobacterium Anabaena sp. strain PCC 7120.";
RL   DNA Res. 8:205-213(2001).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M50B family. {ECO:0000305}.
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DR   EMBL; BA000019; BAB75670.1; -; Genomic_DNA.
DR   PIR; AD2302; AD2302.
DR   RefSeq; WP_010998112.1; NZ_RSCN01000045.1.
DR   AlphaFoldDB; Q8YQ64; -.
DR   SMR; Q8YQ64; -.
DR   STRING; 103690.17133105; -.
DR   EnsemblBacteria; BAB75670; BAB75670; BAB75670.
DR   KEGG; ana:all3971; -.
DR   eggNOG; COG0750; Bacteria.
DR   OMA; QYMVGFG; -.
DR   OrthoDB; 1395197at2; -.
DR   Proteomes; UP000002483; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma 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   Gene3D; 2.30.42.10; -; 1.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR004387; Pept_M50_Zn.
DR   InterPro; IPR008915; Peptidase_M50.
DR   PANTHER; PTHR42837; PTHR42837; 1.
DR   Pfam; PF13180; PDZ_2; 1.
DR   Pfam; PF02163; Peptidase_M50; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF50156; SSF50156; 1.
DR   TIGRFAMs; TIGR00054; TIGR00054; 2.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Hydrolase; Membrane; Metal-binding;
KW   Metalloprotease; Protease; Reference proteome; Transmembrane;
KW   Transmembrane helix; Zinc.
FT   CHAIN           1..364
FT                   /note="Putative zinc metalloprotease all3971"
FT                   /id="PRO_0000088426"
FT   TRANSMEM        92..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        281..303
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        329..346
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          103..188
FT                   /note="PDZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   ACT_SITE        18
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         17
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         21
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ   SEQUENCE   364 AA;  38613 MW;  54F6AAE818AEFBEA CRC64;
     MSVLAAIAVL AVLILVHELG HFVAARSQGI HVNRFSLGFG PVLWKYQGAE TEYAIRAFPL
     GGFVGFPDDD PDSDIPPNDP NLLRNRPILD RAIVISAGVI ANLIFAYMLL LAQVGFVGIG
     QASQPGVSIQ QLAPEVSAVA TNAGLKPGDV ILSANQKEFG TSLQEIEALR DIIKNSPGKS
     IQLTVARGDE RLSVNVIPEA KPAGGSIGIG LAPNGKVERR PVSLSKAFSV GASEFQRIVV
     MTFKGFGQLV TNFGETASQV AGPIKIVEIG ANIAQNDTGS LFFFAALISI NLAVINILPL
     PALDGGQLAF LLIEGLRGKP LPNRIQEGVM QTGLVLLLGL GIFLIVKETT QLTTQLEWVQ
     KLFQ