ID A0A0Q7D7I0_9CAUL Unreviewed; 491 AA.
AC A0A0Q7D7I0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Peptidase M20 {ECO:0000313|EMBL:KQW73388.1};
GN ORFNames=ASC73_03315 {ECO:0000313|EMBL:KQW73388.1};
OS Phenylobacterium sp. Root1277.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Phenylobacterium.
OX NCBI_TaxID=1736442 {ECO:0000313|EMBL:KQW73388.1, ECO:0000313|Proteomes:UP000051150};
RN [1] {ECO:0000313|EMBL:KQW73388.1, ECO:0000313|Proteomes:UP000051150}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1277 {ECO:0000313|EMBL:KQW73388.1,
RC ECO:0000313|Proteomes:UP000051150};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQW73388.1, ECO:0000313|Proteomes:UP000051150}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1277 {ECO:0000313|EMBL:KQW73388.1,
RC ECO:0000313|Proteomes:UP000051150};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQW73388.1}.
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DR EMBL; LMDZ01000001; KQW73388.1; -; Genomic_DNA.
DR RefSeq; WP_056017451.1; NZ_LMDZ01000001.1.
DR AlphaFoldDB; A0A0Q7D7I0; -.
DR Proteomes; UP000051150; 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:UP000051150};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 242..386
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 491 AA; 51580 MW; EE2D9A990B8B1F27 CRC64;
MKLIGKVALA LVGLILLLAA IVVVRTLTYK PAAGADLSQV KLAPAVAIDS AKAAEHLSQS
IRFQTISHQD KADNQLAEWE KLHAWLQTTY PAAHAAMTRE VVAGHTLVYT WAGSDPSLAP
VVLMAHQDVV PVTPGTEDDW KYAPFEGTIA EGAVWGRGAI DDKGSLITLF EGVEALATQG
FKPKRTVILV SGHDEEAGGT GAQAAAELFK SRGIKAQFVL DEGMAIISDN PLTGGPVALI
GIAEKGYATL MVTAEAVGGH SSAPPADSGG VLTLARAVTK IAEDQAPMKL DGPGGQMMET
LAPQGSFMIR MAMANRWLFE PLIIKQAAAS PAGAALLHTT IAPTMLKGSP KENVLPQDAT
AWINYRIAPG DSSAAVMDRA KAAVGDLPVA FAWSRAPNEP SPVSSTTSEA WKMVAALAGD
TAKAPVAPSL VTAGTDSRYM TGVAVDVYRF QPMVFSMETI KMIHGTNEHM SLQNLERAVQ
FYARLIATSA G
//
