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Database: UniProt
Entry: A0A0Q9U8I3_9BACL
LinkDB: A0A0Q9U8I3_9BACL
Original site: A0A0Q9U8I3_9BACL 
ID   A0A0Q9U8I3_9BACL        Unreviewed;       602 AA.
AC   A0A0Q9U8I3;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Oligoendopeptidase {ECO:0000313|EMBL:KRF43013.1};
GN   ORFNames=ASG93_19675 {ECO:0000313|EMBL:KRF43013.1};
OS   Paenibacillus sp. Soil787.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1736411 {ECO:0000313|EMBL:KRF43013.1, ECO:0000313|Proteomes:UP000051948};
RN   [1] {ECO:0000313|EMBL:KRF43013.1, ECO:0000313|Proteomes:UP000051948}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil787 {ECO:0000313|EMBL:KRF43013.1,
RC   ECO:0000313|Proteomes:UP000051948};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRF43013.1, ECO:0000313|Proteomes:UP000051948}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil787 {ECO:0000313|EMBL:KRF43013.1,
RC   ECO:0000313|Proteomes:UP000051948};
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|RuleBase:RU003435};
CC       Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC   -!- SIMILARITY: Belongs to the peptidase M3 family.
CC       {ECO:0000256|RuleBase:RU003435}.
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:KRF43013.1}.
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DR   EMBL; LMSP01000002; KRF43013.1; -; Genomic_DNA.
DR   RefSeq; WP_056829946.1; NZ_LMSP01000002.1.
DR   AlphaFoldDB; A0A0Q9U8I3; -.
DR   STRING; 1736411.ASG93_19675; -.
DR   OrthoDB; 9769691at2; -.
DR   Proteomes; UP000051948; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd09607; M3B_PepF; 1.
DR   Gene3D; 1.10.1370.20; Oligoendopeptidase f, C-terminal domain; 1.
DR   Gene3D; 1.20.140.70; Oligopeptidase f, N-terminal domain; 1.
DR   InterPro; IPR034006; M3B_PepF_2.
DR   InterPro; IPR013647; OligopepF_N_dom.
DR   InterPro; IPR042088; OligoPept_F_C.
DR   InterPro; IPR001567; Pept_M3A_M3B_dom.
DR   InterPro; IPR011977; Pept_M3B_clade3.
DR   InterPro; IPR001333; Peptidase_M32_Taq.
DR   NCBIfam; TIGR02290; M3_fam_3; 1.
DR   PANTHER; PTHR34217:SF1; CARBOXYPEPTIDASE 1; 1.
DR   PANTHER; PTHR34217; METAL-DEPENDENT CARBOXYPEPTIDASE; 1.
DR   Pfam; PF01432; Peptidase_M3; 1.
DR   Pfam; PF08439; Peptidase_M3_N; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU003435};
KW   Metal-binding {ECO:0000256|RuleBase:RU003435};
KW   Metalloprotease {ECO:0000256|RuleBase:RU003435};
KW   Protease {ECO:0000256|RuleBase:RU003435};
KW   Zinc {ECO:0000256|RuleBase:RU003435}.
FT   DOMAIN          119..183
FT                   /note="Oligopeptidase F N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08439"
FT   DOMAIN          205..582
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   602 AA;  68418 MW;  D24DD0A9A01C38BA CRC64;
     MLNLPLNQTW NLETFFPGGS ESPSFAAHLK ELQASIAAFQ EQVRNTPSPG QVEDTDSLVR
     LIELFQHNLK HIHEADSFVG CLLADNQKDK KAPVLSGQVK SLFAEHLSSL THFDQVLTGI
     PDDVWSALLQ KEPFKDIAFP LDERRALAQE KLPPEQEALI NDLAVDGYHG WGDLYNTTVG
     QFRMPIEVDG EMVELSAGQA FNKLHTENRE ERLELFDKWE QAWTDKEEYC AEALNHLAGF
     RLQVYKYRGW KNIHKEPLAI NRMEEKTLNV MWEVIDRNKD IFVDYLNRKA KLLGVDKLAW
     VDVDAPLGDS SKKISYDEGA TLIVDQFKRF SPKLAAFSQE AFEKRWIEAE DRAGKRPGGF
     CTSFPIAGET RIFMTYGGTL NNVSTLAHEL GHGYHQHVMT DMPALAQEYA MNVAETASTF
     AEMIVADAVV KSASTDEERI ILLEDKIQRA IAFFMNIHAR FIFETNFYEA RSQGLVSVER
     LNELMADAQK LAYKDALSSY HPHFWAAKLH FYATDVPFYN FPYTFGYLFS AGIYARAVQE
     GAAFEDKYIS LLRDTGSMNV EELAQKHLGV DLTEPDFWQS AVDMAAQDVK QFMELTEAKV
     QM
//
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