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
//