ID G5EQM2_9MICC Unreviewed; 392 AA.
AC G5EQM2;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Succinyl-diaminopimelate desuccinylase {ECO:0000313|EMBL:EHB88270.1};
GN ORFNames=HMPREF0737_00582 {ECO:0000313|EMBL:EHB88270.1};
OS Rothia mucilaginosa M508.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Rothia.
OX NCBI_TaxID=563033 {ECO:0000313|EMBL:EHB88270.1, ECO:0000313|Proteomes:UP000004897};
RN [1] {ECO:0000313|EMBL:EHB88270.1, ECO:0000313|Proteomes:UP000004897}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M508 {ECO:0000313|EMBL:EHB88270.1,
RC ECO:0000313|Proteomes:UP000004897};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Ward D., Feldgarden M., Gevers D., Sibley C.D., Field T.R.,
RA Grinwis M., Eshaghurshan C.S., Surette M.G., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Rothia mucilaginosa M508.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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:EHB88270.1}.
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DR EMBL; ACSB01000006; EHB88270.1; -; Genomic_DNA.
DR RefSeq; WP_005505237.1; NZ_JH370351.1.
DR AlphaFoldDB; G5EQM2; -.
DR PATRIC; fig|563033.4.peg.575; -.
DR HOGENOM; CLU_021802_1_0_11; -.
DR Proteomes; UP000004897; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009014; F:succinyl-diaminopimelate desuccinylase activity; IEA:InterPro.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:InterPro.
DR CDD; cd05647; M20_DapE_actinobac; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR InterPro; IPR010174; Succinyl-DAP_deSuclase_DapE.
DR NCBIfam; TIGR01900; dapE-gram_pos; 1.
DR PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR PANTHER; PTHR43808:SF8; M20_DIMER DOMAIN-CONTAINING PROTEIN; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 201..298
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 392 AA; 42145 MW; 7DCBE4EE2DF84AF7 CRC64;
MSVSPKNSEL HPVPQPPLNL DVSMPELTRA LLDYESVSGN EQPIADAVHM ALSFCPHLHL
TRDGDAIIAR TEFPPLPGAE GERTRIILAG HLDTVPLPTV EGSLGTVPST VREEEEGYVL
YGRGATDMKG GVAVQLKLAA ELTAQDTDYN LTYIFYDNEE VASELSGLAR LIRNHGELIT
DADFGVLLEP TNGTIEGGCN GTMRFFVRTR GLAAHSGRAW RGENAIHALA PALAALASYE
PKTIAVEGLD YREGLNAVQI SGGVAGNVIP DAAAMHVNYR FAPDKTLDEA IAHVREVFAG
YELDFVDLSP AARPGLDTPL AASLIEAVGE EPQPKYGWTD VARLSEIGIP AVNFGPGDAL
LAHTDNEHVS FSQLTRCHAD LRAWLLSDRD ED
//
