ID K9PQB0_9CYAN Unreviewed; 345 AA.
AC K9PQB0;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE SubName: Full=Peptidase S51 dipeptidase E {ECO:0000313|EMBL:AFY35298.1};
GN ORFNames=Cal7507_4947 {ECO:0000313|EMBL:AFY35298.1};
OS Calothrix sp. PCC 7507.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC Calothrix.
OX NCBI_TaxID=99598 {ECO:0000313|EMBL:AFY35298.1, ECO:0000313|Proteomes:UP000010390};
RN [1] {ECO:0000313|EMBL:AFY35298.1, ECO:0000313|Proteomes:UP000010390}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7507 {ECO:0000313|EMBL:AFY35298.1,
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 -!- SIMILARITY: Belongs to the peptidase S51 family.
CC {ECO:0000256|ARBA:ARBA00006534}.
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DR EMBL; CP003943; AFY35298.1; -; Genomic_DNA.
DR RefSeq; WP_015131093.1; NC_019682.1.
DR AlphaFoldDB; K9PQB0; -.
DR STRING; 99598.Cal7507_4947; -.
DR MEROPS; S51.003; -.
DR KEGG; calo:Cal7507_4947; -.
DR PATRIC; fig|99598.3.peg.5548; -.
DR eggNOG; COG4242; Bacteria.
DR HOGENOM; CLU_051822_0_0_3; -.
DR OrthoDB; 9799980at2; -.
DR Proteomes; UP000010390; Chromosome.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd03145; GAT1_cyanophycinase; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR005320; Peptidase_S51.
DR PANTHER; PTHR36175; CYANOPHYCINASE; 1.
DR PANTHER; PTHR36175:SF1; CYANOPHYCINASE; 1.
DR Pfam; PF03575; Peptidase_S51; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000010390};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
SQ SEQUENCE 345 AA; 38868 MW; 1F802CFD2BAA03B0 CRC64;
MTDAFPKIAK CWRTVRNRLS DIRDYLRSYL TVESTPYFEQ KTAYEEKTTY IAPALAGPAL
AFGGGGPDVD DAIQWMINQV RGCTNCATKV DVVVIRAAGD YEYNRLIKAM KGVSSVETLL
ISNRQDANKA EIVEKVRNAD VIFFAGGDQC RYIRNWKDTK LENAVQSVYA KGGGIGGTSA
GAMILSEYVY DACASSEKGI ETRDALEDPY RDITFTYNFF RWHNLQGTIV DTHFDRRERM
GRIMTFIARQ IKDGVSKSVL GIAVSESTSV VVDKNGLAKV MGRGAAYFIL GDHMPEVCER
RTPLTFSNYK IWKLRSGETF NLKNRPTSGY YLRNVKRGRI DYNPY
//
