ID K9YK64_CYASC Unreviewed; 406 AA.
AC K9YK64;
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=Peptidase S13 D-Ala-D-Ala carboxypeptidase C {ECO:0000313|EMBL:AFZ47244.1};
GN OrderedLocusNames=Cyast_1279 {ECO:0000313|EMBL:AFZ47244.1};
OS Cyanobacterium stanieri (strain ATCC 29140 / PCC 7202).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Geminocystaceae; Cyanobacterium.
OX NCBI_TaxID=292563 {ECO:0000313|EMBL:AFZ47244.1, ECO:0000313|Proteomes:UP000010483};
RN [1] {ECO:0000313|Proteomes:UP000010483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29140 / PCC 7202 {ECO:0000313|Proteomes:UP000010483};
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 S13 family.
CC {ECO:0000256|ARBA:ARBA00006096}.
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DR EMBL; CP003940; AFZ47244.1; -; Genomic_DNA.
DR AlphaFoldDB; K9YK64; -.
DR STRING; 292563.Cyast_1279; -.
DR KEGG; csn:Cyast_1279; -.
DR PATRIC; fig|292563.3.peg.1339; -.
DR eggNOG; COG2027; Bacteria.
DR HOGENOM; CLU_047821_0_0_3; -.
DR BioCyc; CSTA292563:G1353-1287-MONOMER; -.
DR Proteomes; UP000010483; Chromosome.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.50.80.20; D-Ala-D-Ala carboxypeptidase C, peptidase S13; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR000667; Peptidase_S13.
DR PANTHER; PTHR30023; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR30023:SF0; PENICILLIN-SENSITIVE CARBOXYPEPTIDASE A; 1.
DR Pfam; PF02113; Peptidase_S13; 2.
DR PRINTS; PR00922; DADACBPTASE3.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:AFZ47244.1};
KW Hydrolase {ECO:0000313|EMBL:AFZ47244.1};
KW Protease {ECO:0000313|EMBL:AFZ47244.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010483}.
SQ SEQUENCE 406 AA; 45152 MW; 26DCC78EAEC5259F CRC64;
MFFSTLLTIF SGWFNFALTP QEVPLIPWHE NPIFQLPTEG DEEVERILEQ YLEGLANRNV
PINQQGVWIQ THWATLGDNR GTIPAPAASI TKVATTLGAL DKWSVDHRFL TNIYTTGDIL
GGVLQGDLIV EAGNDPFFVW EDAIALGDEI RKLGIERVRG NLIIVGDWQM NFKENNLTSG
DDLRRALNSD NWNYTVETQY QGMENPPPRP QLVIEGENIF RDGLPPASNL LYTHSSKPLH
QILRAMNLYS NNFIADHLAQ QIGGGDQLGA IASKLSNVPP EEIQLINGSG LGVDNRISPR
AACRMLIAIE QKIANHNITI ADLFPVSGID EGTLKERNIP FGVPVKTGSL AVVSALSGVI
DTEERETVYF AIMNYANGLD DLRNRQDQLL TDLDNHWQTR PILPMP
//
