ID A0A0Q6BNF7_9PROT Unreviewed; 436 AA.
AC A0A0Q6BNF7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Zinc protease {ECO:0000313|EMBL:KQT43751.1};
GN ORFNames=ASG34_02945 {ECO:0000313|EMBL:KQT43751.1};
OS Methylophilus sp. Leaf416.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Methylophilaceae; Methylophilus.
OX NCBI_TaxID=1736373 {ECO:0000313|EMBL:KQT43751.1, ECO:0000313|Proteomes:UP000050891};
RN [1] {ECO:0000313|EMBL:KQT43751.1, ECO:0000313|Proteomes:UP000050891}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf416 {ECO:0000313|EMBL:KQT43751.1,
RC ECO:0000313|Proteomes:UP000050891};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQT43751.1, ECO:0000313|Proteomes:UP000050891}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf416 {ECO:0000313|EMBL:KQT43751.1,
RC ECO:0000313|Proteomes:UP000050891};
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 M16 family.
CC {ECO:0000256|ARBA:ARBA00007261}.
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:KQT43751.1}.
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DR EMBL; LMQS01000001; KQT43751.1; -; Genomic_DNA.
DR RefSeq; WP_055826267.1; NZ_LMQS01000001.1.
DR AlphaFoldDB; A0A0Q6BNF7; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000050891; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR11851:SF149; GH01077P; 1.
DR PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:KQT43751.1};
KW Protease {ECO:0000313|EMBL:KQT43751.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..436
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006273108"
FT DOMAIN 50..179
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 192..369
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 436 AA; 47549 MW; D216122822F1D6A6 CRC64;
MKAFKYLKIT LLALLLQSHA INVLAGLNIQ HWTTAQGSEV YFVENHALPM MDISVNFPAG
SAHDSPETSG AAGVTQHLMA LVAGGLDEET LTNRFADIGA VLGGNFDADR AGFKLRTLTS
EQAVALEAFS FVLHKPDFPE AVLKREQARI VAGLQEAETE PDSIAQKAFM RSLYGTHPYS
LDQSGEIDTV QSLTVTHLRQ FYETHYTAKS AVISLIGDLT AAQAKQIAER LSAGLPQGPA
VAAVPPVPAL KTASVKKLPH PALQAHILLG QPGNKRGDAD FFPLYVGNYI LGGGGFVSRL
TEEVREKRGL AYSVYSYFLP MAELGPFQIG LQTKKEQAEE GLQLVKQTVQ QFIDKGVTEK
ELQAAKDNLI GGFPLRIDSN GKILEYLNII GFYKLPLDYL DSFNDRVAQV TVQQVNDAFK
RRLHPENFAT VIVGSE
//
