ID A0A161SJW1_9MICO Unreviewed; 448 AA.
AC A0A161SJW1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Succinyl-diaminopimelate desuccinylase {ECO:0000313|EMBL:KZE91450.1};
GN Name=dapE_5 {ECO:0000313|EMBL:KZE91450.1};
GN ORFNames=AVP41_00992 {ECO:0000313|EMBL:KZE91450.1};
OS Microbacterium sp. TNHR37B.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1775956 {ECO:0000313|EMBL:KZE91450.1, ECO:0000313|Proteomes:UP000076535};
RN [1] {ECO:0000313|EMBL:KZE91450.1, ECO:0000313|Proteomes:UP000076535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TNHR37B {ECO:0000313|EMBL:KZE91450.1,
RC ECO:0000313|Proteomes:UP000076535};
RA Adelskov J., Patel B.K.;
RT "Draft Genome Sequence of Microbacterium sp. TNHR37B isolated from the
RT Great Artesian Basin of Australia.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M20A family.
CC {ECO:0000256|ARBA:ARBA00006247}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KZE91450.1}.
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DR EMBL; LQGV01000001; KZE91450.1; -; Genomic_DNA.
DR RefSeq; WP_067161537.1; NZ_LQGV01000001.1.
DR AlphaFoldDB; A0A161SJW1; -.
DR STRING; 1775956.AVP41_00992; -.
DR PATRIC; fig|1775956.3.peg.977; -.
DR OrthoDB; 3665926at2; -.
DR Proteomes; UP000076535; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.150.900; -; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR001261; ArgE/DapE_CS.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR047177; Pept_M20A.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR PANTHER; PTHR45962; N-FATTY-ACYL-AMINO ACID SYNTHASE/HYDROLASE PM20D1; 1.
DR PANTHER; PTHR45962:SF1; N-FATTY-ACYL-AMINO ACID SYNTHASE_HYDROLASE PM20D1; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF036696; ACY-1; 2.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000076535};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 200..347
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 448 AA; 48332 MW; 7D962DE673EAD1A8 CRC64;
MRAPRPDAAA VDRFRELLRI PTISHADESA TDGAAFDEFS AAVERLYPLL HAQLEREVVA
GHSLLYRWRG RSEAGCLVLM AHIDVVPVVE TDWQHPPFDA DIVGEGEAAE IHARGAIDDK
GSLVAILEAV EGLVASGFTP ARDVYLAFGH NEETAGDGAQ AIVALLRSRD VRPGLVLDEG
GAVVEGAVPG VTVPTAMVGV AERGVMTLIL TVREDGGHAS TPPALPATAR LARAIHRLHR
RPFPPRITAP IRAMFATLAP HARRPLRLVF ARMGAWGPVM ARIFPRLGPE LNAMVRTTAV
VTELSGAPGE NVLAATARAA VNVRLLTGDT VAGVTQRVRR AIGDDAVDIE VRHGSDPSPV
SPWQGEPWRR IATAVSVAVG AEVVTTPYLQ LGASDSRWFT ALSAHVYRFT PFHLTRAERD
ALHSHDERIR ISSWLRGIDF YRELLAAS
//
