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Database: UniProt
Entry: A0A1J0PED7_9SYNE
LinkDB: A0A1J0PED7_9SYNE
Original site: A0A1J0PED7_9SYNE 
ID   A0A1J0PED7_9SYNE        Unreviewed;       425 AA.
AC   A0A1J0PED7;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Zinc metalloprotease {ECO:0000256|PIRNR:PIRNR006404};
GN   ORFNames=BM449_13805 {ECO:0000313|EMBL:APD49639.1};
OS   Synechococcus sp. SynAce01.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=1916956 {ECO:0000313|EMBL:APD49639.1, ECO:0000313|Proteomes:UP000182608};
RN   [1] {ECO:0000313|Proteomes:UP000182608}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SynAce01 {ECO:0000313|Proteomes:UP000182608};
RA   Tang J., Daroch M., Liang Y., Jiang D., Shah M.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRNR:PIRNR006404,
CC         ECO:0000256|PIRSR:PIRSR006404-2};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR006404,
CC       ECO:0000256|PIRSR:PIRSR006404-2};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|PIRNR:PIRNR006404};
CC       Multi-pass membrane protein {ECO:0000256|PIRNR:PIRNR006404}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the peptidase M50B family.
CC       {ECO:0000256|ARBA:ARBA00007931, ECO:0000256|PIRNR:PIRNR006404}.
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DR   EMBL; CP018091; APD49639.1; -; Genomic_DNA.
DR   RefSeq; WP_071802332.1; NZ_CP018091.1.
DR   AlphaFoldDB; A0A1J0PED7; -.
DR   STRING; 1916956.BM449_13805; -.
DR   KEGG; syny:BM449_13805; -.
DR   OrthoDB; 166377at2; -.
DR   Proteomes; UP000182608; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd06164; S2P-M50_SpoIVFB_CBS; 1.
DR   InterPro; IPR046342; CBS_dom_sf.
DR   InterPro; IPR008915; Peptidase_M50.
DR   InterPro; IPR016483; UCP006404_Pept_M50_CBS.
DR   PANTHER; PTHR39188; MEMBRANE-ASSOCIATED ZINC METALLOPROTEASE M50B; 1.
DR   PANTHER; PTHR39188:SF3; ZINC METALLOPROTEASE SLR1821-RELATED; 1.
DR   Pfam; PF02163; Peptidase_M50; 2.
DR   PIRSF; PIRSF006404; UCP006404_Pept_M50_CBS; 1.
DR   SUPFAM; SSF54631; CBS-domain pair; 1.
PE   3: Inferred from homology;
KW   CBS domain {ECO:0000256|ARBA:ARBA00023122};
KW   Cell membrane {ECO:0000256|PIRNR:PIRNR006404};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR006404};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR006404};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRNR:PIRNR006404};
KW   Metalloprotease {ECO:0000256|PIRNR:PIRNR006404};
KW   Protease {ECO:0000256|PIRNR:PIRNR006404};
KW   Reference proteome {ECO:0000313|Proteomes:UP000182608};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|PIRNR:PIRNR006404};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|PIRNR:PIRNR006404};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRNR:PIRNR006404}.
FT   TRANSMEM        15..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT   TRANSMEM        44..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT   TRANSMEM        72..94
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT   TRANSMEM        106..127
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT   TRANSMEM        147..174
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT   TRANSMEM        213..232
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT   DOMAIN          56..128
FT                   /note="Peptidase M50"
FT                   /evidence="ECO:0000259|Pfam:PF02163"
FT   DOMAIN          140..196
FT                   /note="Peptidase M50"
FT                   /evidence="ECO:0000259|Pfam:PF02163"
FT   REGION          405..425
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        68
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006404-1"
FT   BINDING         67
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006404-2"
FT   BINDING         71
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006404-2"
FT   BINDING         164
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006404-2"
SQ   SEQUENCE   425 AA;  45377 MW;  AD237F014C86B9FC CRC64;
     MGEGWLLLKI RGIPLRIHPS WFVILGLATV SFEQQYGARF AGQASVLGLW LMALLTALLL
     FVSVLLHELG HSFVAMAYGV KVRSITLFLL GGVATVEREC STALSALQVA AAGPLVSLVL
     ASVLLLGSHS VSHAWPLAGE VVQQLGVLNL VLGLFNLLPG LPLDGGLIVK ALVWQFTGSQ
     RRGIQVAAGI GRFLSLMAIG MGTLFVLRGG GFGAFWLILL GWFGLGASRN QLQQLSLEEA
     MRELKVGDAA ARRFRVLESD ASLRDLSQLR LSDDSSLPAD WVLICDRGRW QGVIDDQALQ
     SLPVQRWDGE RVGDHHQPLD SLPSITSGEP LWQAALKLDA DGVNRLLVLS NAGLPSGTIE
     RPELSDAVLK RLGLRLPAPL IEAARRQGAY PLGLALGQVA RSMANAAPAD PDPEPLTAAK
     QAPLG
//
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