ID Q5HKT9_STAEQ Unreviewed; 414 AA.
AC Q5HKT9;
DT 15-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2005, sequence version 1.
DT 27-MAR-2024, entry version 107.
DE RecName: Full=Probable succinyl-diaminopimelate desuccinylase {ECO:0000256|ARBA:ARBA00016853};
DE EC=3.5.1.18 {ECO:0000256|ARBA:ARBA00011921};
GN OrderedLocusNames=SERP2253 {ECO:0000313|EMBL:AAW53097.1};
OS Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176279 {ECO:0000313|EMBL:AAW53097.1, ECO:0000313|Proteomes:UP000000531};
RN [1] {ECO:0000313|EMBL:AAW53097.1, ECO:0000313|Proteomes:UP000000531}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35984 / RP62A {ECO:0000313|Proteomes:UP000000531};
RX PubMed=15774886; DOI=10.1128/JB.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., Deboy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L., Beanan M., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J., Khouri H., Utterback T., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K., Hance I.R., Nelson K.E., Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-succinyl-(2S,6S)-2,6-diaminoheptanedioate =
CC (2S,6S)-2,6-diaminoheptanedioate + succinate; Xref=Rhea:RHEA:22608,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:30031, ChEBI:CHEBI:57609,
CC ChEBI:CHEBI:58087; EC=3.5.1.18;
CC Evidence={ECO:0000256|ARBA:ARBA00001246};
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; L-lysine biosynthesis via DAP
CC pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate
CC (succinylase route): step 3/3. {ECO:0000256|ARBA:ARBA00005130}.
CC -!- SIMILARITY: Belongs to the peptidase M20A family.
CC {ECO:0000256|ARBA:ARBA00006247}.
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DR EMBL; CP000029; AAW53097.1; -; Genomic_DNA.
DR RefSeq; WP_002437925.1; NC_002976.3.
DR AlphaFoldDB; Q5HKT9; -.
DR STRING; 176279.SERP2253; -.
DR KEGG; ser:SERP2253; -.
DR eggNOG; COG0624; Bacteria.
DR HOGENOM; CLU_021802_2_2_9; -.
DR UniPathway; UPA00034; UER00021.
DR Proteomes; UP000000531; Chromosome.
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: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.
DR PROSITE; PS00758; ARGE_DAPE_CPG2_1; 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 Reference proteome {ECO:0000313|Proteomes:UP000000531};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 173..308
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 414 AA; 46088 MW; 4A293E9B3A9BE7F9 CRC64;
MSVLSNEERV KILSDIVSIK TVNSNELEVA HYFKRLFSQY GIRSHIDTVT DGRANLIATV
GSSQPVIGIS GHMDVVSEGN HDDWTYDPFT LTENQGYLYG RGAADMKSGL AALAIALIEI
KESGKLTQGT IKFMATVGEE MEQSGSQQLF EKGYADDLDA LLIAEPSFPS LVYAHKGSMD
FRIKSKGRAS HSSIPFLGQN AIKPLLEFIQ NINQEYEKIM QTVKGESLDF SNMINKLENQ
LPSHITKEKA QELIQGLVMT NSIVQGGTQV NSVPDFATAE FNVRTIPEYN NNKVKALFNE
YIEQANHNGA SLTQELYLDL EPVVTTGQNR LVELGFDIAK SHFSNERDLI ITPTVAVTDA
SNLLKGKDEN FPFLMFGPGN GPHQINECVE KANYLEFVEY YIEFITSYLN EENE
//
