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Database: UniProt
Entry: K9PPH0_9CYAN
LinkDB: K9PPH0_9CYAN
Original site: K9PPH0_9CYAN 
ID   K9PPH0_9CYAN            Unreviewed;       290 AA.
AC   K9PPH0;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Peptidase M48 Ste24p {ECO:0000313|EMBL:AFY34432.1};
GN   ORFNames=Cal7507_4048 {ECO:0000313|EMBL:AFY34432.1};
OS   Calothrix sp. PCC 7507.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC   Calothrix.
OX   NCBI_TaxID=99598 {ECO:0000313|EMBL:AFY34432.1, ECO:0000313|Proteomes:UP000010390};
RN   [1] {ECO:0000313|EMBL:AFY34432.1, ECO:0000313|Proteomes:UP000010390}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7507 {ECO:0000313|EMBL:AFY34432.1,
RC   ECO:0000313|Proteomes:UP000010390};
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., Teshima H., Chen A.,
RA   Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA   Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L., Pitluck S.,
RA   Woyke T., Kerfeld C.;
RT   "Finished genome of Calothrix sp. PCC 7507.";
RL   Submitted (APR-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; CP003943; AFY34432.1; -; Genomic_DNA.
DR   RefSeq; WP_015130235.1; NC_019682.1.
DR   AlphaFoldDB; K9PPH0; -.
DR   STRING; 99598.Cal7507_4048; -.
DR   MEROPS; M48.021; -.
DR   KEGG; calo:Cal7507_4048; -.
DR   PATRIC; fig|99598.3.peg.4561; -.
DR   eggNOG; COG0501; Bacteria.
DR   HOGENOM; CLU_052979_1_0_3; -.
DR   OrthoDB; 9810445at2; -.
DR   Proteomes; UP000010390; 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:UP000010390};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003983}.
FT   DOMAIN          65..261
FT                   /note="Peptidase M48"
FT                   /evidence="ECO:0000259|Pfam:PF01435"
SQ   SEQUENCE   290 AA;  32087 MW;  A9CE3AF16841DBA5 CRC64;
     MSFLKTPLLG LKADSFRHPL DLEATKALKQ IPGLDMVVRN WLGPMAEQIF YVENIAASVL
     VGEKQLPDLH NLLLEACKIL DIEPPQLYIR QHPAPNAYTF AMRGKQPFIV VHTSLIDILT
     PAEIQAVIAH ELGHLKCDHS VYLTPVNVLI LAAAALPNVG TFVAQAIQAQ LLEWVRCAEF
     TCDRAALLAT QDPKVVMSVL MKLAGGSPRL APQLNLDAFV DQARAYDDIS KTELGEMVKV
     ARTAQLTHPV PVLRAREIDR WSSSQEYQLL LQSQGNSTSE VSSQGGWRNW
//
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