ID D7GRB1_9FIRM Unreviewed; 450 AA.
AC D7GRB1;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase and related deacylases {ECO:0000313|EMBL:CBL40336.1};
DE EC=3.4.17.4 {ECO:0000313|EMBL:CBL40336.1};
GN ORFNames=CK3_05260 {ECO:0000313|EMBL:CBL40336.1};
OS butyrate-producing bacterium SS3/4.
OC Bacteria; Bacillota; Clostridia; Eubacteriales.
OX NCBI_TaxID=245014 {ECO:0000313|EMBL:CBL40336.1, ECO:0000313|Proteomes:UP000008961};
RN [1] {ECO:0000313|EMBL:CBL40336.1, ECO:0000313|Proteomes:UP000008961}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SS3/4 {ECO:0000313|EMBL:CBL40336.1,
RC ECO:0000313|Proteomes:UP000008961};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT "The genome sequence of Clostridiales sp. SS3/4.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBL40336.1, ECO:0000313|Proteomes:UP000008961}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SS3/4 {ECO:0000313|EMBL:CBL40336.1,
RC ECO:0000313|Proteomes:UP000008961};
RA Pajon A.;
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M20A family.
CC {ECO:0000256|ARBA:ARBA00006247}.
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DR EMBL; FP929062; CBL40336.1; -; Genomic_DNA.
DR AlphaFoldDB; D7GRB1; -.
DR KEGG; bprs:CK3_05260; -.
DR PATRIC; fig|245014.3.peg.2257; -.
DR HOGENOM; CLU_021802_11_1_9; -.
DR BioCyc; BBAC245014:G1314-434-MONOMER; -.
DR Proteomes; UP000008961; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:UniProtKB-EC.
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 SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:CBL40336.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CBL40336.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 201..346
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 450 AA; 49547 MW; 1BDB5F970E0F7445 CRC64;
MGKHTIDPQI SAEHLAGAVR FATVSNADNS LTDYTKFDAF HEYLKETYPL VHKHLTLEHT
GQAGLLYHWK GTGKSGAAPL LLMAHQDVVP EGDLEKWIYP PYSGTIADGK IWGRGSSDCK
SNLIGQLEAV EALLEKGYEP DYDLYLSYGY MEEVAGGKIP AETLRGTGIR FGAVLDEGGG
VRPGSDYGID DKGLCTIGLC EKGYVDFELS YTAKGGHSSR PGENFAMTMI AKALIAIQEN
PMPYRVTDTI RRRFEVLAPY MAKENPELAK LLEKPDENLE KLVPYFKKDP ALDAMFHTTV
VPTMLSGSAQ ANILPAKVTA VVNSRILTGD TVESVKKHLE DIVPDEVEVR VLKGSNASPT
SLYDGAIKDL LVEISGKIYG DVIPCPEMML GGTDARFVYD LSDRVYRFST IYAREDHHVH
AANEFTGVEE LADSIDFYME LLTRYGETAK
//
