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Database: UniProt
Entry: K8GK51_9CYAN
LinkDB: K8GK51_9CYAN
Original site: K8GK51_9CYAN 
ID   K8GK51_9CYAN            Unreviewed;       525 AA.
AC   K8GK51;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=Putative Zn-dependent peptidase {ECO:0000313|EMBL:EKQ69288.1};
DE   Flags: Precursor;
GN   ORFNames=OsccyDRAFT_1913 {ECO:0000313|EMBL:EKQ69288.1};
OS   Leptolyngbyaceae cyanobacterium JSC-12.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae.
OX   NCBI_TaxID=864702 {ECO:0000313|EMBL:EKQ69288.1, ECO:0000313|Proteomes:UP000001332};
RN   [1] {ECO:0000313|EMBL:EKQ69288.1, ECO:0000313|Proteomes:UP000001332}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JSC-12 {ECO:0000313|EMBL:EKQ69288.1,
RC   ECO:0000313|Proteomes:UP000001332};
RG   DOE Joint Genome Institute;
RA   Brown I., Huntemann M., Wei C.-L., Han J., Detter J.C., Han C., Tapia R.,
RA   Chen A., Kyrpides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA   Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L.,
RA   Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RT   "Improved high quality draft of Oscillatoriales sp. JSC-12.";
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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:EKQ69288.1}.
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DR   EMBL; AJUB01000010; EKQ69288.1; -; Genomic_DNA.
DR   AlphaFoldDB; K8GK51; -.
DR   STRING; 864702.OsccyDRAFT_1913; -.
DR   PATRIC; fig|864702.5.peg.2067; -.
DR   eggNOG; COG0612; Bacteria.
DR   HOGENOM; CLU_009902_1_2_3; -.
DR   Proteomes; UP000001332; 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:InterPro.
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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001332}.
FT   DOMAIN          75..119
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          171..269
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          278..455
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   525 AA;  58566 MW;  D1B6A7331E1DB017 CRC64;
     MVRLVSTRVG KLAGAIVLSL VLTIGCWGMV SESATAQTPP IAAQSPNPTS IQPYLDNVIQ
     NITEFRLENG MKFIVLERRK APVVSFVTYA DVGGADEPDG KTGVAHFLEH LAFKGTSRIG
     TVDYATEKPL LDRLDELSEQ IKIANASSQP DKAKQLQAEF AKVEAEAAKL VEQNEMGRIV
     EQAGGVGLNA TTSTDATRYF YSFPANKLEL WMSLESERFL DPVFREFYKE QNVILEERRL
     RTDNSPIGQM VEAFLDTAFK VHPYRRPVIG YNQDISGLTR QDVQQFFDRY YVPSNLTIAI
     VGDVRPAEVK RLATIYFGRY KAQPKPPQVT AVEPPQTETR EVTLKLKSQP WYLEGYHVPA
     FNDPDTVIYD MIGDILSSGR TSRLYKSLVE TKQLALSAQG FTGFPGNKFP NLMLFYALTA
     PGHTVEEVGT ALQAEIERLK TEPVTSEELE RVKTQARAGL LRSLNSNMGM AQALLEYEVK
     TGDWRNLFKQ LDRIAAVTPA DIQRVAKATF TSQNRTIGRI LPKEG
//
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