ID A0A0Q5UDI5_9SPHI Unreviewed; 437 AA.
AC A0A0Q5UDI5;
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=Peptidase M16 {ECO:0000313|EMBL:KQS41494.1};
GN ORFNames=ASG14_03240 {ECO:0000313|EMBL:KQS41494.1};
OS Pedobacter sp. Leaf194.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=1736297 {ECO:0000313|EMBL:KQS41494.1, ECO:0000313|Proteomes:UP000051708};
RN [1] {ECO:0000313|EMBL:KQS41494.1, ECO:0000313|Proteomes:UP000051708}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf194 {ECO:0000313|EMBL:KQS41494.1,
RC ECO:0000313|Proteomes:UP000051708};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQS41494.1, ECO:0000313|Proteomes:UP000051708}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf194 {ECO:0000313|EMBL:KQS41494.1,
RC ECO:0000313|Proteomes:UP000051708};
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:KQS41494.1}.
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DR EMBL; LMPU01000001; KQS41494.1; -; Genomic_DNA.
DR RefSeq; WP_056869605.1; NZ_LMPU01000001.1.
DR AlphaFoldDB; A0A0Q5UDI5; -.
DR STRING; 1736297.ASG14_03240; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000051708; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase 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; PTHR43690; NARDILYSIN; 1.
DR PANTHER; PTHR43690:SF17; PROTEIN YHJJ; 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:0000256|ARBA:ARBA00022801};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670}; Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..437
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006264345"
FT DOMAIN 36..149
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 192..367
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 437 AA; 49579 MW; A68247893C7E6EDF CRC64;
MKKRIIFALA ISGLCLSVSA QKVQFTEFDL DNGLHVILHQ DKTAPVVAVS VMYHVGSKDE
DTTRTGFAHF FEHLLFEGSK NIKKGEFMKL VSSNGGQNNA NTSQDRTFYY EVFPSNQLEL
GLWLESERML HPVINEQGVK TQNEVVKEEK RLRIDNSPYG KFTEKIFSHL FDGHPYRWQP
IGSLAHLDAA RLDEFIAFNK KYYVPNNAVL TIAGDIDVEK TRGLVKAYFA EVAKGKDVVR
KDYKLPEITK EIIDTAYDAN IQIPAIFAAY RVPGMKSRES KVLGMISSIL SAGGSSRLST
KMVDEKKTAL QVAAFNYSLE DYGAYITLAL PNKNTPLNDL LKDIDEEVLR LQTELISESD
YKKLQNQFEN SYVSANSRML GVAENLANGY TFHNKDTNDI NEELNVIKSI TREEIRDVAK
KYLNKNQRVV LYYLPKK
//
