ID A0A0Q6VQQ6_9BURK Unreviewed; 964 AA.
AC A0A0Q6VQQ6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Peptidase {ECO:0000313|EMBL:KQV80885.1};
GN ORFNames=ASD15_13395 {ECO:0000313|EMBL:KQV80885.1};
OS Massilia sp. Root351.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1736522 {ECO:0000313|EMBL:KQV80885.1, ECO:0000313|Proteomes:UP000051876};
RN [1] {ECO:0000313|EMBL:KQV80885.1, ECO:0000313|Proteomes:UP000051876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root351 {ECO:0000313|EMBL:KQV80885.1,
RC ECO:0000313|Proteomes:UP000051876};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQV80885.1, ECO:0000313|Proteomes:UP000051876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root351 {ECO:0000313|EMBL:KQV80885.1,
RC ECO:0000313|Proteomes:UP000051876};
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, ECO:0000256|RuleBase:RU004447}.
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:KQV80885.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LMDJ01000031; KQV80885.1; -; Genomic_DNA.
DR RefSeq; WP_057157121.1; NZ_LMDJ01000031.1.
DR AlphaFoldDB; A0A0Q6VQQ6; -.
DR OrthoDB; 9762027at2; -.
DR Proteomes; UP000051876; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR001431; Pept_M16_Zn_BS.
DR InterPro; IPR007863; Peptidase_M16_C.
DR InterPro; IPR013578; Peptidase_M16C_assoc.
DR PANTHER; PTHR43016; PRESEQUENCE PROTEASE; 1.
DR PANTHER; PTHR43016:SF13; PRESEQUENCE PROTEASE, MITOCHONDRIAL; 1.
DR Pfam; PF08367; M16C_assoc; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 2.
DR SMART; SM01264; M16C_associated; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
DR PROSITE; PS00143; INSULINASE; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000051876}.
FT DOMAIN 450..693
FT /note="Peptidase M16C associated"
FT /evidence="ECO:0000259|SMART:SM01264"
SQ SEQUENCE 964 AA; 103486 MW; A5E503D872ECDB33 CRC64;
MNTFELVRSH RIAALQATVE EYVAPSSGAR HIHLATAGAD LAFLVGFPTV PDTSDGRAHI
LEHLALCGSQ RYPVRAPFFS MLRRSTATFM NAMTYADRTV YPFASTDRND FFNLLDVYLD
ATFFPRLDYL NFLQEGWRHT LEDGKLRYQG VVFNEMKGAF ADPTRALYNG ISAALLKDTT
YEVVSGGDPL AIPELSHQML KDFHASHYHP SQAVFMTAGD IPAAEIQRHV AERVLSRLPG
AMPRRMPQLA AAAAPREATI RVPSQSARGD EFGFQLTWLM GESSDATVQH HANLLQAGLL
GDASAPLKKA MESAGYGRPS RLNGMDTGPR QLLFHLGMDG LAQHQLADAR ARVWAALEDA
ANAGVPQSAL QAALRDIKYS QRDTSSGRMP NVMNRMLQAL PVAMRGGDVV GAFDSEAVLR
SLEQHIADPA FFKGLVRALL DSPARLDAAI VPDADFFTAR AAAEEEGLAA RLAALSGEER
ARIEADSVAL DAHQRLPSDT TLLPRIKPGD VSPHPRPLPA IPAAQDGKYL FPIASNGISY
AVVQYDVGAL PESAWPWLQL YADLRRDLGV AGHSYEQAGA WRKRMVPAFK LGLEALVKAD
DTLDLALQFS VTGLREEHAN MAAVLEAYIG SPRFDEHERI AFLVARMVKN RINGLASSGN
VYASLAATAP LSPLRRFENA CGGVAMLPFL GELGRLAATP EGVAHIAARL AEIHLQVVSC
PSKVLCAGTG DDAQALAGML AAPAAKSAAA AARGSAAAAA SAARANLALY AAGQVNHCYI
AWPAPPQTHP QAPALAVAAE LLTHQLLHQA LREKGGAYGG SASYAGGLRL FSMSSYRDPR
LAGTYADFAA AIGHLLETDF SPEQIEEAII CVIKSLDRPA SPFDAVLNAW SLQARGIGPE
QRQRFRSGVL ACTQDEIRLA VRQWLKQATP SRAAFVGNTA QDLDGLEVTD LHALSGENPV
QATG
//