ID A0A024P3V4_9BACI Unreviewed; 403 AA.
AC A0A024P3V4;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Probable succinyl-diaminopimelate desuccinylase {ECO:0000256|ARBA:ARBA00016853};
GN Name=dapE_1 {ECO:0000313|EMBL:CDQ22800.1};
GN ORFNames=BN983_01017 {ECO:0000313|EMBL:CDQ22800.1};
OS Halobacillus karajensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halobacillus.
OX NCBI_TaxID=195088 {ECO:0000313|EMBL:CDQ22800.1, ECO:0000313|Proteomes:UP000028868};
RN [1] {ECO:0000313|EMBL:CDQ22800.1, ECO:0000313|Proteomes:UP000028868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HD-03 {ECO:0000313|EMBL:CDQ22800.1,
RC ECO:0000313|Proteomes:UP000028868};
RA Urmite Genomes U.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDQ22800.1, ECO:0000313|Proteomes:UP000028868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HD-03 {ECO:0000313|EMBL:CDQ22800.1,
RC ECO:0000313|Proteomes:UP000028868};
RA Khelaifia S., Croce O., Lagier J.C., Raoult D.;
RT "Draft genome sequence of Halobacillus karajensis HK-03.";
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000256|ARBA:ARBA00001941};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
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:CDQ22800.1}.
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DR EMBL; CCDI010000001; CDQ22800.1; -; Genomic_DNA.
DR RefSeq; WP_035506257.1; NZ_CCDJ010000001.1.
DR AlphaFoldDB; A0A024P3V4; -.
DR UniPathway; UPA00034; UER00021.
DR Proteomes; UP000028868; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009014; F:succinyl-diaminopimelate desuccinylase activity; IEA:UniProtKB-EC.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway.
DR CDD; cd08659; M20_ArgE_DapE-like; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR010182; ArgE/DapE.
DR InterPro; IPR001261; ArgE/DapE_CS.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR NCBIfam; TIGR01910; DapE-ArgE; 1.
DR PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR PANTHER; PTHR43808:SF3; ACETYLORNITHINE DEACETYLASE-RELATED; 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.
DR PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE 3: Inferred from homology;
KW Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000028868};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 188..301
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 403 AA; 44628 MW; 387B61E0F6073F1F CRC64;
MHTRIETRST RDRERVIALT QSLVRIPSVY RPGEEGGNEK KCAAFVAEHL SKLGIEVYIE
EVEAGRPNVI GVIDSGKSGK TLIFEGHTDV VTEGDSHSWK YDPFGAEIVD GLMYGRGTND
TKGNLACMIT AVQSLLEDKE EWSGKIILCI PCDEEGMMIG IKHFIKQGWA DQADGAIICE
PEENQVCIAQ RGAMRLVLKT YGKMAHGAIS WSGINPNLRM AKVIVELEKL EKREQERLGK
HPTLGWPSIT PTILQAPAKG DAQINVIPEQ CMTTLDIRTV PGQDHDRLQE EIHHIFARLA
QDDPEFKADF DVIEDRPWTS TDKEEPVVEA VAEAVQSVLV KDPIYNGVPG ATDGTFLHVA
GVPIVTIGAG DREVPHQIDE YVDIEELAET TEIYRQAALN FLN
//
