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Database: UniProt
Entry: B9E713_MACCJ
LinkDB: B9E713_MACCJ
Original site: B9E713_MACCJ 
ID   B9E713_MACCJ            Unreviewed;       374 AA.
AC   B9E713;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   RecName: Full=Peptidase M20 dimerisation domain-containing protein {ECO:0000259|Pfam:PF07687};
GN   OrderedLocusNames=MCCL_1274 {ECO:0000313|EMBL:BAH17981.1};
OS   Macrococcus caseolyticus (strain JCSC5402).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; Macrococcus.
OX   NCBI_TaxID=458233 {ECO:0000313|EMBL:BAH17981.1, ECO:0000313|Proteomes:UP000001383};
RN   [1] {ECO:0000313|EMBL:BAH17981.1, ECO:0000313|Proteomes:UP000001383}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC5402 {ECO:0000313|EMBL:BAH17981.1,
RC   ECO:0000313|Proteomes:UP000001383};
RX   PubMed=19074389; DOI=10.1128/JB.01058-08;
RA   Baba T., Kuwahara-Arai K., Uchiyama I., Takeuchi F., Ito T., Hiramatsu K.;
RT   "Complete genome sequence of Macrococcus caseolyticus strain JCSCS5402,
RT   reflecting the ancestral genome of the human-pathogenic staphylococci.";
RL   J. Bacteriol. 191:1180-1190(2009).
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DR   EMBL; AP009484; BAH17981.1; -; Genomic_DNA.
DR   AlphaFoldDB; B9E713; -.
DR   STRING; 458233.MCCL_1274; -.
DR   KEGG; mcl:MCCL_1274; -.
DR   eggNOG; COG1473; Bacteria.
DR   HOGENOM; CLU_023257_0_1_9; -.
DR   Proteomes; UP000001383; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
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:SF122; AMIDOHYDROLASE AMHX; 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:UP000001383}.
FT   DOMAIN          176..270
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   374 AA;  43113 MW;  BA82D9CE60F6B6AD CRC64;
     MKQMNSTTFK NEIHEINTEL NSIAEVSWKE QKTTEYLTTY LKDYTIERFN KTGFLLQIDG
     EIKDAIAFRT DIDALPYRLN NELKVLHACG HDVHMTILTG FILKLKEMDY KPKHTLKFIF
     QPAEELGEGA KYVVEHEQEV LEHVHYLFGM HVRPLNELKK GQFSASIQHG ASGTIYMDVI
     TKAGHAGRPW ESINSIDIVM EIYEHIKRIN MGSNRNYSIK MTKINTMNGQ DNSIPGHVSV
     TFDIRANYND MMDELIAVFN KMIDDRKVQY AEQDVFIDTR IDSYTVAAQI DTDAKEFLKK
     AIKSKGFEYV DTIYTPGAED FHNYTYALPN IKSTMLGIGC NMEHGLHHPD MKLDKSVIFD
     AIEIFYQLLI DIDK
//
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