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Database: UniProt
Entry: A0A2N0HJT6_9SPHN
LinkDB: A0A2N0HJT6_9SPHN
Original site: A0A2N0HJT6_9SPHN 
ID   A0A2N0HJT6_9SPHN        Unreviewed;       473 AA.
AC   A0A2N0HJT6;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase-like protein {ECO:0000313|EMBL:PKB19214.1};
GN   ORFNames=B0I00_1444 {ECO:0000313|EMBL:PKB19214.1};
OS   Novosphingobium kunmingense.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=1211806 {ECO:0000313|EMBL:PKB19214.1, ECO:0000313|Proteomes:UP000232587};
RN   [1] {ECO:0000313|EMBL:PKB19214.1, ECO:0000313|Proteomes:UP000232587}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.12274 {ECO:0000313|EMBL:PKB19214.1,
RC   ECO:0000313|Proteomes:UP000232587};
RA   Whitman W.;
RT   "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT   soil and plant-associated and newly described type strains.";
RL   Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
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:PKB19214.1}.
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DR   EMBL; PHUF01000003; PKB19214.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N0HJT6; -.
DR   Proteomes; UP000232587; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
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; 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.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000232587};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..473
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014696447"
FT   DOMAIN          223..368
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   473 AA;  50354 MW;  215CDD90C2DF28A9 CRC64;
     MIRIAVLAAM LASAALSAPA AAQPLRPDQA AFREIFKELV ETNTTLSSGS CTLAAERTAA
     RLRAGGLPES QITLFATADK PREGGLVAVY PGTSKTLKPI LAIAHIDVVE ARRADWERDP
     FTLIEEGGYF YGRGTLDTKG LAAVYVDTLI RFQQAGYKPK RTVKIALTCG EETNGAFNGV
     EWLAANQRDL IDAEFAINEG GGGGTDGKGV VDGGKVVEQA MQVGEKTFAN YQLETRNPGG
     HSSVPRPDNA IYQLARALAR VEAYEFPLEF SETTRTYFRA AGAARGDAVG KAMVALAANP
     ADRDAEKTVN AEAFLHSNLR TTCVATMLEA GHARNALAQR AQANVNCRIF PGHSIEAIAA
     ELGRVIADPG VAITVLPPKR PSPPPPALDP KVMEPARKLV AKYWPGVPLV PQMANGYTDA
     TFLGAVGIPT YGVPGMWGDP DGNGVHGLNE RIEVRSLLTG RDFLYDLIKA YAG
//
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