ID   K9T9Q6_9CYAN            Unreviewed;       291 AA.
AC   K9T9Q6;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=Zn-dependent protease with chaperone function {ECO:0000313|EMBL:AFY78836.1};
GN   ORFNames=Ple7327_3641 {ECO:0000313|EMBL:AFY78836.1};
OS   Pleurocapsa sp. PCC 7327.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Pleurocapsales; Hyellaceae;
OC   Pleurocapsa.
OX   NCBI_TaxID=118163 {ECO:0000313|EMBL:AFY78836.1, ECO:0000313|Proteomes:UP000010382};
RN   [1] {ECO:0000313|EMBL:AFY78836.1, ECO:0000313|Proteomes:UP000010382}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7327 {ECO:0000313|EMBL:AFY78836.1,
RC   ECO:0000313|Proteomes:UP000010382};
RG   US DOE Joint Genome Institute;
RA   Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA   Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., Kyrpides N.,
RA   Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA   Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT   "Finished genome of Pleurocapsa sp. PCC 7327.";
RL   Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU003983};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU003983};
CC   -!- SIMILARITY: Belongs to the peptidase M48 family.
CC       {ECO:0000256|RuleBase:RU003983}.
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DR   EMBL; CP003590; AFY78836.1; -; Genomic_DNA.
DR   RefSeq; WP_015145135.1; NC_019689.1.
DR   AlphaFoldDB; K9T9Q6; -.
DR   STRING; 118163.Ple7327_3641; -.
DR   MEROPS; M48.021; -.
DR   KEGG; plp:Ple7327_3641; -.
DR   eggNOG; COG0501; Bacteria.
DR   HOGENOM; CLU_052979_1_0_3; -.
DR   Proteomes; UP000010382; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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   CDD; cd07325; M48_Ste24p_like; 1.
DR   Gene3D; 3.30.2010.10; Metalloproteases ('zincins'), catalytic domain; 1.
DR   InterPro; IPR001915; Peptidase_M48.
DR   PANTHER; PTHR10120; CAAX PRENYL PROTEASE 1; 1.
DR   PANTHER; PTHR10120:SF26; PLASTOGLOBULE-LOCALIZED METALLOPEPTIDASE 48, CHLOROPLASTIC; 1.
DR   Pfam; PF01435; Peptidase_M48; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003983};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU003983};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003983};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010382};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003983}.
FT   DOMAIN          68..261
FT                   /note="Peptidase M48"
FT                   /evidence="ECO:0000259|Pfam:PF01435"
SQ   SEQUENCE   291 AA;  32755 MW;  5C434A7048E87D92 CRC64;
     MGFSKTQLIG LRADDFRHPL DLQATTALKQ LPGLDMLVRS LLGPVAEQFF YLNNIASSIL
     VGENQLPHLH KLLLEACQIL DLEPPQLYVQ QNPIPNAYTF AMRGKQPFMV LHTSLIEMLT
     PEEIQAVMAH ELGHLKCEHG VYLTLVNIVV LAAGLLPSWG TVIAQSLREQ MLQWVRCAEF
     SCDRAALLAI QDPKVVMSVL MKLTGGSPTL APQLNLDAFI EQARAYDAIS ETELGQMLKT
     AQTAQLTHPV PVLRAREIDR WASSQDYQRL LQRRQIEYNR KADPKGGWRN W
//