ID Q9RKM4_STRCO Unreviewed; 423 AA.
AC Q9RKM4;
DT 01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 116.
DE SubName: Full=Peptidase {ECO:0000313|EMBL:CAB56384.1};
GN OrderedLocusNames=SCO4103 {ECO:0000313|EMBL:CAB56384.1};
GN ORFNames=SCD17.07c {ECO:0000313|EMBL:CAB56384.1};
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226 {ECO:0000313|EMBL:CAB56384.1, ECO:0000313|Proteomes:UP000001973};
RN [1] {ECO:0000313|EMBL:CAB56384.1, ECO:0000313|Proteomes:UP000001973}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145
RC {ECO:0000313|Proteomes:UP000001973};
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., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J., 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).
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DR EMBL; AL939118; CAB56384.1; -; Genomic_DNA.
DR RefSeq; NP_628283.1; NC_003888.3.
DR RefSeq; WP_011029435.1; NZ_VNID01000030.1.
DR AlphaFoldDB; Q9RKM4; -.
DR STRING; 100226.gene:17761743; -.
DR PaxDb; 100226-SCO4103; -.
DR PATRIC; fig|100226.15.peg.4162; -.
DR eggNOG; COG1473; Bacteria.
DR HOGENOM; CLU_023257_6_0_11; -.
DR InParanoid; Q9RKM4; -.
DR OrthoDB; 9777385at2; -.
DR PhylomeDB; Q9RKM4; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IBA:GO_Central.
DR CDD; cd05664; M20_Acy1-like; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR017439; Amidohydrolase.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR NCBIfam; TIGR01891; amidohydrolases; 1.
DR PANTHER; PTHR11014:SF63; METALLOPEPTIDASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G09600)-RELATED; 1.
DR PANTHER; PTHR11014; PEPTIDASE M20 FAMILY MEMBER; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000001973}.
FT DOMAIN 199..295
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 423 AA; 44795 MW; 0657D768E9BD3199 CRC64;
MSDTARTVLA GLGSVRSDLE DLYQDLHRHP ELGLREHRTA KKAAESLRRS GYDVTEGVGG
TGVIGVLANG DGPVVMARAD MDALPVRERT GLPYASTATV TDEDGREQPV MHACGHDVHV
TSLVGCARLL AGHRDDWRGT FVALFQPSEE NGAGARAMVE DGLTDRSPRP DVVLAQHVLP
YPAGYVGTRS GSFLSAADSL RVTVHGRGAH GSAPQASVDP VVIAASVVVR LQTVVSRELA
ATTPAVVTVG SIHAGSGPNV IPDRAVLELN VRTYDDATRT QVLDAIKRIV RAECEASRSP
REPEFERLST FPPTVNDEEP TRRVAEAFGV YFGDDAHTVE LQTASEDMSE IPGAFGVPFT
YWAIGGTDPD RYAEAARKGT VAQDIPVNHS AAFAPVVQPT LDTGVSALTV AALAWLGDGD
RAA
//
