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Database: UniProt
Entry: A0A2S6CX83_9CYAN
LinkDB: A0A2S6CX83_9CYAN
Original site: A0A2S6CX83_9CYAN 
ID   A0A2S6CX83_9CYAN        Unreviewed;       495 AA.
AC   A0A2S6CX83;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Site-2 protease family protein {ECO:0000313|EMBL:PPJ64384.1};
GN   ORFNames=CUN59_04875 {ECO:0000313|EMBL:PPJ64384.1};
OS   Cuspidothrix issatschenkoi CHARLIE-1.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Aphanizomenonaceae;
OC   Cuspidothrix.
OX   NCBI_TaxID=2052836 {ECO:0000313|EMBL:PPJ64384.1, ECO:0000313|Proteomes:UP000239589};
RN   [1] {ECO:0000313|EMBL:PPJ64384.1, ECO:0000313|Proteomes:UP000239589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CHARLIE-1 {ECO:0000313|EMBL:PPJ64384.1,
RC   ECO:0000313|Proteomes:UP000239589};
RA   Kust A., Mares J., Jokela J., Urajova P., Hajek J., Saurav K., Voracova K.,
RA   Fewer D.P., Haapaniemi E., Permi P., Rehakova K., Sivonen K., Hrouzek P.;
RT   "Discovery of a pederin family compound in a non-symbiotic bloom-forming
RT   cyanobacterium.";
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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}.
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:PPJ64384.1}.
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DR   EMBL; PGEM01000028; PPJ64384.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S6CX83; -.
DR   OrthoDB; 494312at2; -.
DR   Proteomes; UP000239589; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd06160; S2P-M50_like_2; 1.
DR   InterPro; IPR044838; EGY1-like.
DR   InterPro; IPR008915; Peptidase_M50.
DR   PANTHER; PTHR31412; ZINC METALLOPROTEASE EGY1; 1.
DR   PANTHER; PTHR31412:SF5; ZINC METALLOPROTEASE EGY2, CHLOROPLASTIC-RELATED; 1.
DR   Pfam; PF02163; Peptidase_M50; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:PPJ64384.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000313|EMBL:PPJ64384.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000239589};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        36..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        60..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        218..241
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        253..275
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        282..299
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        311..338
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        376..398
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        419..445
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        465..488
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          258..423
FT                   /note="Peptidase M50"
FT                   /evidence="ECO:0000259|Pfam:PF02163"
SQ   SEQUENCE   495 AA;  53382 MW;  FD696B5907535CFD CRC64;
     MFTSSETPII AAIVLIASGI LGWGFYRARP FGKLGILAWL QSVVLMTPWL LFFGLFAAGI
     YINIVGILFL VVASAGLYIF LGRKLRAAGQ DAILKQRATE RLAAEGLSQG DKTSPVIVAE
     LKLEPTPIPE ADLNLIKGIF GIETFFATET IPYQEGVVFK GNLRGEPETV HNRLTQSLQA
     RLEDKYRLFL VENTDGKPVV IVLPSRTDPR PAQVGQKVFA VILLIATIAT SLEVGGILQN
     FDLFSNPERF AEALPIGLGL SAILLSHEIG HWLLARRHQV KLSWPFFLPA VQIGSFGAIT
     RFESLVPSRK ALFDIALAGP AFGGITSLLL LVIGLLLSHP GSLFQLPNQF FQGSILVGSL
     ARVVLGSALQ SPVVNIHPLV IIGWLGLVIT ALNLMPAGQL DGGRIVQAIY GRKTAGRTTF
     ATIVLLAIVS LGNPLAMYWA IVILFLQRDL ERPSLNEISE PDDARAALCL LALFLMIATL
     LPLTPALAGR LGIGS
//
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