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
//