ID C5C632_BEUC1 Unreviewed; 409 AA.
AC C5C632;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=Peptidase M20 domain-containing protein 2 {ECO:0000256|PIRNR:PIRNR037226};
GN OrderedLocusNames=Bcav_4151 {ECO:0000313|EMBL:ACQ82390.1};
OS Beutenbergia cavernae (strain ATCC BAA-8 / DSM 12333 / NBRC 16432).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Beutenbergiaceae;
OC Beutenbergia.
OX NCBI_TaxID=471853 {ECO:0000313|EMBL:ACQ82390.1, ECO:0000313|Proteomes:UP000007962};
RN [1] {ECO:0000313|EMBL:ACQ82390.1, ECO:0000313|Proteomes:UP000007962}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-8 / DSM 12333 / NBRC 16432
RC {ECO:0000313|Proteomes:UP000007962};
RX PubMed=21304633; DOI=10.4056/sigs.1162;
RA Land M., Pukall R., Abt B., Goker M., Rohde M., Glavina Del Rio T.,
RA Tice H., Copeland A., Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D.,
RA Goodwin L., Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G.,
RA Pati A., Chen A., Palaniappan K., Hauser L., Chang Y.J., Jefferies C.C.,
RA Saunders E., Brettin T., Detter J.C., Han C., Chain P., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA Lapidus A.;
RT "Complete genome sequence of Beutenbergia cavernae type strain (HKI
RT 0122).";
RL Stand. Genomic Sci. 1:21-28(2009).
CC -!- SIMILARITY: Belongs to the peptidase M20A family.
CC {ECO:0000256|PIRNR:PIRNR037226}.
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DR EMBL; CP001618; ACQ82390.1; -; Genomic_DNA.
DR RefSeq; WP_015884627.1; NC_012669.1.
DR AlphaFoldDB; C5C632; -.
DR STRING; 471853.Bcav_4151; -.
DR KEGG; bcv:Bcav_4151; -.
DR eggNOG; COG1473; Bacteria.
DR HOGENOM; CLU_031812_1_0_11; -.
DR Proteomes; UP000007962; Chromosome.
DR GO; GO:0016805; F:dipeptidase 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 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; PF07687; M20_dimer; 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:ACQ82390.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007962}.
FT DOMAIN 181..275
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 409 AA; 42123 MW; 54606D01EE14F120 CRC64;
MTTALDHDAV APPEREAHPL AARVDEVLTG LLPDLRQLAD ELHDDPETAY EEHRSAARVA
ALLERHGVAA QVGAFGLPTA LHANAGDGGP RVAILAEYDA LPDIGHACGH NLIAATAVGA
FLAVRELLEH AGGTVELIGS PAEEGGGGKQ RIIDAGGFEG VAAAVMVHPG NRDRAYGSGL
GMRHVEVTYR GVEAHASAAP ERGYNALDAV VTAYQSVAQV RQHILPTDRV HGIITDGGQA
PNIVPGRAAA HFFVRSATID GLEALSERVD AALRGAAIST GTEAEIVWDR LPAYLPVNVN
QALADRFAAN LRGRREFPPP SPAATGGGST DLGNVSHVVP AIHPNIATAP EGIGAHTAAF
AATTLQPLAT QGVLDAAFGL ATTVLDVLGD AELRAAIAAD FEASREGDA
//
