ID K9Z1P5_CYAAP Unreviewed; 515 AA.
AC K9Z1P5;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Processing peptidase {ECO:0000313|EMBL:AFZ52278.1};
DE EC=3.4.24.64 {ECO:0000313|EMBL:AFZ52278.1};
GN OrderedLocusNames=Cyan10605_0120 {ECO:0000313|EMBL:AFZ52278.1};
OS Cyanobacterium aponinum (strain PCC 10605).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Geminocystaceae; Cyanobacterium.
OX NCBI_TaxID=755178 {ECO:0000313|EMBL:AFZ52278.1, ECO:0000313|Proteomes:UP000010480};
RN [1] {ECO:0000313|Proteomes:UP000010480}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 10605 {ECO:0000313|Proteomes:UP000010480};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR EMBL; CP003947; AFZ52278.1; -; Genomic_DNA.
DR RefSeq; WP_015218010.1; NC_019776.1.
DR AlphaFoldDB; K9Z1P5; -.
DR STRING; 755178.Cyan10605_0120; -.
DR KEGG; can:Cyan10605_0120; -.
DR PATRIC; fig|755178.3.peg.123; -.
DR eggNOG; COG0612; Bacteria.
DR HOGENOM; CLU_009902_1_2_3; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000010480; 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:UniProtKB-EC.
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.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000313|EMBL:AFZ52278.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010480}.
FT DOMAIN 64..108
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 161..258
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 266..444
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT COILED 113..162
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 515 AA; 58889 MW; 226D9C531C2A888D CRC64;
MFFRPLYKAF IFGLIIFFAW TNNCELALAK ISLNESNQSI EPYLNQVKED ITEFTLSNGI
HFIVLENHQA PVISFNTYVD VGGANEPEGK TGVAHFLEHL AFKGTKEIGT INYEKEKQIL
EELDKTFQQI KEAKKENNQE QLTELENKFE QLNNQAHNLV KQNEFGQIIE LEGGVGLNAA
TSADSTVYFY NFPSNKLELW MYLESDRFLN PVFREFYQEK QVILEERKLR TDNSPVGKMV
EAFLDSAFTT HPYKRPVIGY EEDIINLTRE DVQNFFDSYY GGNNITIAIV GDVDPKEVKQ
MANKYFGRFP SSTKPAKLNI VEPKQTETRE VAIEYPSQPW YLEGYHIPNI NDPDYVVYDI
ISSILSSGRT SRLYQSLVDE QKIALSAAGF NGFPGDKYPN LMLFYAMLAP ERQLEDLEVA
LHEQIEKLKS DLVTEEELQR VKTQARASLL RSLNSNAGMA KLLAEYQAKT GDWRNLFLSL
DKISAVTAQD IQRVAQNTFT SDNKTVGRLI TKPMN
//
