ID A0A2N5MKT5_9BACI Unreviewed; 429 AA.
AC A0A2N5MKT5;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Acetylornithine deacetylase {ECO:0000313|EMBL:PLT34967.1};
DE EC=3.5.1.16 {ECO:0000313|EMBL:PLT34967.1};
GN ORFNames=CUU64_06135 {ECO:0000313|EMBL:PLT34967.1};
OS Bacillus sp. V5-8f.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=2053044 {ECO:0000313|EMBL:PLT34967.1, ECO:0000313|Proteomes:UP000235260};
RN [1] {ECO:0000313|EMBL:PLT34967.1, ECO:0000313|Proteomes:UP000235260}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=V5-8f {ECO:0000313|EMBL:PLT34967.1,
RC ECO:0000313|Proteomes:UP000235260};
RA Seuylemezian A., Cooper K., Vaishampayan P.;
RT "Comparitive Functional Genomics of Dry Heat Resistant Strains Isolated
RT from the Viking Spacecraft.";
RL Submitted (NOV-2017) 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 -!- 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:PLT34967.1}.
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DR EMBL; PGUW01000004; PLT34967.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N5MKT5; -.
DR OrthoDB; 9792335at2; -.
DR Proteomes; UP000235260; Unassembled WGS sequence.
DR GO; GO:0008777; F:acetylornithine deacetylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR010182; ArgE/DapE.
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.
PE 3: Inferred from homology;
KW Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW Hydrolase {ECO:0000313|EMBL:PLT34967.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000235260}.
FT DOMAIN 201..313
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 429 AA; 47037 MW; 478A327AA3AD2094 CRC64;
MIHNQTIHEW LKQNGMRGIR LLQRLVQEPS KRGQEGRAQA IILEKCRELG LSIDLWELGD
DSLRNHSNFY CDRTDFKGNP NLVAVLKGSG GGKSLILNGH IDVVPEGNPK DWDDDPFSGI
LRDGKVYGRG TTDMKGGTVS LLLALDAILS LGITLKGDVI FQSVIEEESG GAGTLAAVLR
GYQADGAIIP EPTNMKFFPL QQGSMWFRLT VKGKSAHGGT RYEGVSAIDL ALEVVNEIKA
LEKYRNDSLD HPLYKDIKIP IPINIGKIES GSWPSSVPDK AIIEGRFGIA PTETMESAQR
AMEDCIASLN AEHEWFHQKP IEIEWFGARW LPGNLDLHHP LMETLSNNFS KVMQKPPVIE
ASPWGTDGGY LSNVGGIPVI VFGPGKTEVA HDANEYIEID KVIEAAEIIA LAIIEWCGVD
QAGTSLLEN
//
