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Database: UniProt
Entry: C7MFV8_BRAFD
LinkDB: C7MFV8_BRAFD
Original site: C7MFV8_BRAFD 
ID   C7MFV8_BRAFD            Unreviewed;       403 AA.
AC   C7MFV8;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   RecName: Full=Peptidase M20 domain-containing protein 2 {ECO:0000256|PIRNR:PIRNR037226};
GN   OrderedLocusNames=Bfae_01980 {ECO:0000313|EMBL:ACU84076.1};
OS   Brachybacterium faecium (strain ATCC 43885 / DSM 4810 / JCM 11609 / LMG
OS   19847 / NBRC 14762 / NCIMB 9860 / 6-10).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermabacteraceae;
OC   Brachybacterium.
OX   NCBI_TaxID=446465 {ECO:0000313|EMBL:ACU84076.1, ECO:0000313|Proteomes:UP000001919};
RN   [1] {ECO:0000313|EMBL:ACU84076.1, ECO:0000313|Proteomes:UP000001919}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43885 / DSM 4810 / JCM 11609 / LMG 19847 / NBRC 14762 /
RC   NCIMB 9860 / 6-10 {ECO:0000313|Proteomes:UP000001919};
RX   PubMed=21304631; DOI=10.4056/sigs.492;
RA   Lapidus A., Pukall R., Labuttii K., Copeland A., Del Rio T.G., Nolan M.,
RA   Chen F., Lucas S., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S.,
RA   Rohde M., Goker M., Pati A., Ivanova N., Mavrommatis K., Chen A.,
RA   Palaniappan K., D'haeseleer P., Chain P., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Brachybacterium faecium type strain
RT   (Schefferle 6-10).";
RL   Stand. Genomic Sci. 1:3-11(2009).
CC   -!- SIMILARITY: Belongs to the peptidase M20A family.
CC       {ECO:0000256|PIRNR:PIRNR037226}.
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DR   EMBL; CP001643; ACU84076.1; -; Genomic_DNA.
DR   RefSeq; WP_012803852.1; NC_013172.1.
DR   RefSeq; YP_003153666.1; NC_013172.1.
DR   AlphaFoldDB; C7MFV8; -.
DR   STRING; 446465.Bfae_01980; -.
DR   KEGG; bfa:Bfae_01980; -.
DR   PATRIC; fig|446465.5.peg.197; -.
DR   eggNOG; COG1473; Bacteria.
DR   HOGENOM; CLU_031812_1_0_11; -.
DR   OrthoDB; 9781032at2; -.
DR   Proteomes; UP000001919; Chromosome.
DR   GO; GO:0016805; F:dipeptidase activity; IEA:InterPro.
DR   CDD; cd05672; M20_ACY1L2-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; IPR017144; Xaa-Arg_dipeptidase.
DR   NCBIfam; TIGR01891; amidohydrolases; 1.
DR   PANTHER; PTHR30575; PEPTIDASE M20; 1.
DR   PANTHER; PTHR30575:SF0; XAA-ARG DIPEPTIDASE; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   PIRSF; PIRSF037226; Amidohydrolase_ACY1L2_prd; 1.
DR   SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:ACU84076.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001919}.
SQ   SEQUENCE   403 AA;  42010 MW;  F3D01934F8F56C27 CRC64;
     MTVDDAALTA LTTAYASHRA PVRALARALH ADPETAFEEH RAHDRCADLL EQAGFTLERG
     IAELPTAFRA TAGSGSLVAA LCVEYDALPE IGHGCGHNLI AGASLGAALA LREQLAALDV
     TLQVIGTPAE EHGGGKQLLL DRGVFEGVHL ALMAHPTPHT DTYDVLGSTS QAVGRWRATY
     TGRGAHAAAN PTEGINANDA AVVAQVAAGL LRQRMHDGQR LALVPQQSGI TNIIPETAII
     DLECRALTMP AFEELRRQVF ACLEAGAVAT GAALEITTTE PIYEPLLQDA LLGAAWNAAM
     QQLGRPLEGS LGIMAASTDM GNVSQRVPSL HPFVGITGAG GALHTREFAA HADSEEGYRL
     MDDAAIALAA VIRDIAAEPA SRAVLRDRAA QLAEPVQGAS APL
//
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