ID   Y6489_STRCO             Reviewed;         310 AA.
AC   Q9ZBI5;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Putative carboxypeptidase SCO6489;
DE            EC=3.4.16.-;
GN   OrderedLocusNames=SCO6489; ORFNames=SC9C7.25;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
CC   -!- SIMILARITY: Belongs to the peptidase S66 family. {ECO:0000305}.
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DR   EMBL; AL939128; CAA22737.1; -; Genomic_DNA.
DR   PIR; T35976; T35976.
DR   RefSeq; NP_630572.1; NC_003888.3.
DR   RefSeq; WP_011030959.1; NC_003888.3.
DR   AlphaFoldDB; Q9ZBI5; -.
DR   SMR; Q9ZBI5; -.
DR   STRING; 100226.SCO6489; -.
DR   MEROPS; S66.001; -.
DR   PRIDE; Q9ZBI5; -.
DR   GeneID; 1101928; -.
DR   KEGG; sco:SCO6489; -.
DR   PATRIC; fig|100226.15.peg.6590; -.
DR   eggNOG; COG1619; Bacteria.
DR   HOGENOM; CLU_034346_3_1_11; -.
DR   InParanoid; Q9ZBI5; -.
DR   OMA; MLTQWRL; -.
DR   PhylomeDB; Q9ZBI5; -.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.10740; -; 1.
DR   Gene3D; 3.50.30.60; -; 1.
DR   InterPro; IPR027461; Carboxypeptidase_A_C_sf.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR027478; LdcA_N.
DR   InterPro; IPR040449; Peptidase_S66_N.
DR   InterPro; IPR040921; Peptidase_S66C.
DR   InterPro; IPR003507; S66_fam.
DR   PANTHER; PTHR30237; PTHR30237; 1.
DR   Pfam; PF02016; Peptidase_S66; 1.
DR   Pfam; PF17676; Peptidase_S66C; 1.
DR   PIRSF; PIRSF028757; LD-carboxypeptidase; 1.
DR   SUPFAM; SSF141986; SSF141986; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase; Hydrolase; Protease; Reference proteome; Serine protease.
FT   CHAIN           1..310
FT                   /note="Putative carboxypeptidase SCO6489"
FT                   /id="PRO_0000172845"
FT   ACT_SITE        116
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        212
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        277
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   310 AA;  32764 MW;  6E2C587F3AE8E615 CRC64;
     MRELVRPARL APGARVAVVA PSGPVPEERL QAGLDVLRGW DLDPVVAPHV LDRHDTFDYL
     AGTDADRAAD LQAAWCDPAV DAVLCARGGY GVQRMADLLD WEAMRAAGPK VFVGFSDITA
     LHEAFATRLG LVTLHGPMAA GIDFIKNARA QEHLRATLFA PETVRVITSG GTPLVPGRAR
     GVTLGGCLAL LAADLGTPHA RPGARGGLLC LEDVGEETYR IDRYLTQLLR SGWLDGVGGV
     LLGSWAQCEP YERLRPLLAD RLGGLGVPVV EDFGFGHCEG ALTVPFGVPA ELDADTGTLT
     LDRPALCSPG