ID A0A0Q9PLH1_9GAMM Unreviewed; 644 AA.
AC A0A0Q9PLH1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Peptidase {ECO:0000313|EMBL:KRE88824.1};
GN ORFNames=ASG87_09675 {ECO:0000313|EMBL:KRE88824.1};
OS Frateuria sp. Soil773.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Frateuria.
OX NCBI_TaxID=1736407 {ECO:0000313|EMBL:KRE88824.1, ECO:0000313|Proteomes:UP000051919};
RN [1] {ECO:0000313|Proteomes:UP000051919}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil773 {ECO:0000313|Proteomes:UP000051919};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRE88824.1, ECO:0000313|Proteomes:UP000051919}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil773 {ECO:0000313|EMBL:KRE88824.1,
RC ECO:0000313|Proteomes:UP000051919};
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR036685-1};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|PIRSR:PIRSR036685-
CC 1};
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:KRE88824.1}.
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DR EMBL; LMSL01000041; KRE88824.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q9PLH1; -.
DR STRING; 1736407.ASG87_09675; -.
DR Proteomes; UP000051919; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.380; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR045175; M28_fam.
DR InterPro; IPR002884; P_dom.
DR InterPro; IPR012189; Pept_M28E_Ap1.
DR InterPro; IPR007280; Peptidase_C_arc/bac.
DR InterPro; IPR007484; Peptidase_M28.
DR PANTHER; PTHR12147:SF26; ENDOPLASMIC RETICULUM METALLOPEPTIDASE 1; 1.
DR PANTHER; PTHR12147; METALLOPEPTIDASE M28 FAMILY MEMBER; 1.
DR Pfam; PF01483; P_proprotein; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR Pfam; PF04151; PPC; 1.
DR PIRSF; PIRSF036685; BacLeuNPeptidase; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS51829; P_HOMO_B; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR036685-2};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR036685-1};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Zinc {ECO:0000256|PIRSR:PIRSR036685-1}.
FT DOMAIN 523..644
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT REGION 408..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 209
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR036685-1"
FT BINDING 236
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR036685-1"
FT BINDING 271
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR036685-1"
FT BINDING 298
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR036685-1"
FT BINDING 375
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR036685-1"
FT DISULFID 342..346
FT /evidence="ECO:0000256|PIRSR:PIRSR036685-2"
SQ SEQUENCE 644 AA; 68011 MW; F40D1F78E9568A6E CRC64;
MLLAVGAQAS TPTASGKVWI TLDQRTYALL GQIDPSAHSL ESRYVPNGIG AGGQSTMDKV
HIVQVDRSVL GALGKRVHQV QHHCAGYVTY DSLQAAQAAL QPQGAMAAFT RPDYRITHNA
LLQPMLGQAT AVGIAQTIQD LSAFQNRYYN GDYGAQAADW LRDKWQGMAG SRADIGVEQV
RRGTDKQPSV VLTIKGNEHP DQVLVLGAHL DTVDWQDATG TNDPRHASLR APGADDDASG
VASLTEALRV MLASGYKPQR TIQLMAYSGE EFGLYGSNYI ATDYASRNVD VVGMLQLDMT
NYKGSAGDIY LMDDYTDAQQ NQFVENLANT YQPALKVLHD RCGYGCSDHA SWNSQGYPTS
MPFESAMHEY SPYIHSSNDT YANSGNQADH ALKFARLALS FAVELGDVSG DGDTDPPGGD
NGNALQNGVP LTGLGAAAKS QAAYTVTIPA GASNLVISTS GGTGDVDLYT RFGSAPTRSS
YDCRPYRNGN SESCTVAVPR AGVYHVMLDA YAAYAGVSLK ASWNTGTPST GGVFGNTDDL
AIPDGGSATS TVSVSGRSGN APAALKVAVK VVHSYAGDLR LTLAGPDGAT RVLKNPDGRD
GSAGLDTSYT VDASAMPANG DWTLKVDDVY SGDTGYLDQW SLAF
//
