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Database: UniProt
Entry: F2RDI0_STRVP
LinkDB: F2RDI0_STRVP
Original site: F2RDI0_STRVP 
ID   F2RDI0_STRVP            Unreviewed;       435 AA.
AC   F2RDI0;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   SubName: Full=N-acetyl-L,L-diaminopimelate deacetylase {ECO:0000313|EMBL:CCA59472.1};
DE            EC=3.5.1.47 {ECO:0000313|EMBL:CCA59472.1};
GN   OrderedLocusNames=SVEN_6186 {ECO:0000313|EMBL:CCA59472.1};
OS   Streptomyces venezuelae (strain ATCC 10712 / CBS 650.69 / DSM 40230 / JCM
OS   4526 / NBRC 13096 / PD 04745).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=953739 {ECO:0000313|EMBL:CCA59472.1, ECO:0000313|Proteomes:UP000006854};
RN   [1] {ECO:0000313|EMBL:CCA59472.1, ECO:0000313|Proteomes:UP000006854}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10712 {ECO:0000313|EMBL:CCA59472.1};
RX   PubMed=21463507; DOI=10.1186/1471-2164-12-175;
RA   Pullan S.T., Bibb M.J., Merrick M.;
RT   "Genome-wide analysis of the role of GlnR in Streptomyces venezuelae
RT   provides new insights into global nitrogen regulation in actinomycetes.";
RL   BMC Genomics 12:175-175(2011).
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DR   EMBL; FR845719; CCA59472.1; -; Genomic_DNA.
DR   AlphaFoldDB; F2RDI0; -.
DR   STRING; 953739.SVEN_6186; -.
DR   KEGG; sve:SVEN_6186; -.
DR   PATRIC; fig|953739.5.peg.1392; -.
DR   eggNOG; COG1473; Bacteria.
DR   HOGENOM; CLU_023257_6_0_11; -.
DR   OMA; HMTWGLA; -.
DR   Proteomes; UP000006854; Chromosome.
DR   GO; GO:0050118; F:N-acetyldiaminopimelate deacetylase activity; IEA:UniProtKB-EC.
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   Hydrolase {ECO:0000313|EMBL:CCA59472.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006854}.
FT   DOMAIN          199..295
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   435 AA;  45294 MW;  38934B986AE45615 CRC64;
     MTAASVTRLL AALPDRLPGL RALYEDLHAH PELSFQEFRT AGIVADRLRR QGWEVSEGVG
     GTGVVGVLAN GEGPVVLLRA DMDGLPVQER TGLAYASRAT AVDGEGNEVP VMHACGHDMH
     VTCLLGATAQ LAAARGEWRG TVVAVFQPAE EVGGAPAMIE DGFLDRFPRA DVCLGQHVAP
     APAGFVGTRP GPVMAASDSL RVRLHGRGGH GSTPESTVDP VVMAAAVVMR LQTIVSRETG
     AAQTAVVTVG SLHAGTKENI IPDTADLRIN VRSTATVVRD RTLAAVERIV RAEAAASDAP
     KDPEITRLNS FPLTVNDGPA TSTVMTAIAG VFGEERVFTL PQTLTGSEDF GVFGTALGVP
     SVFWHFGGAD PELFRDIDPE TLLTDGLPET VPANHSPYFA PVPDPTIGIG VTALLAAAAA
     WLCPEDAPAP GGQED
//
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