ID A0A0Q4KVM9_9SPHN Unreviewed; 944 AA.
AC A0A0Q4KVM9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Peptidase M16 {ECO:0000313|EMBL:KQN26755.1};
GN ORFNames=ASE86_00950 {ECO:0000313|EMBL:KQN26755.1};
OS Sphingomonas sp. Leaf33.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736215 {ECO:0000313|EMBL:KQN26755.1, ECO:0000313|Proteomes:UP000051455};
RN [1] {ECO:0000313|EMBL:KQN26755.1, ECO:0000313|Proteomes:UP000051455}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf33 {ECO:0000313|EMBL:KQN26755.1,
RC ECO:0000313|Proteomes:UP000051455};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQN26755.1, ECO:0000313|Proteomes:UP000051455}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf33 {ECO:0000313|EMBL:KQN26755.1,
RC ECO:0000313|Proteomes:UP000051455};
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|ARBA:ARBA00001947};
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:KQN26755.1}.
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DR EMBL; LMLB01000001; KQN26755.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q4KVM9; -.
DR STRING; 1736215.ASE86_00950; -.
DR Proteomes; UP000051455; 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:UniProtKB-KW.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 3.
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 PANTHER; PTHR43690:SF18; INSULIN-DEGRADING ENZYME-RELATED; 1.
DR PANTHER; PTHR43690; NARDILYSIN; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 2.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 3.
DR PROSITE; PS00143; INSULINASE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000051455};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 61..174
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 211..296
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 689..865
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 944 AA; 99973 MW; F66CF3E568501ACA CRC64;
MPAQQAPQPA AATVQAPAVA VDRSAWLYKG SDITPDPDWR FGTLPNGLRY AVRKNGVPPG
QVSIRVRMDV GSLHERDSER GFAHLIEHLS FRGSEHVPDG EAKRIWQRMG VTFGADTNAS
TSFTQTVYKL DLPMANQTGL DESLKILSGM MAGPSLTQTA LDAERPVVLS EAREQPGPQV
RLGDATREVF FAGQPLADRS PIGTTETLSS ATAAAVTAFH DRWYRPERAI VVVSGDMDPA
LFEAAIVKHF ADWRGNGAAV PAPDFGTPKP AKTDTAALVE PQLPTLVSLA WLRPWTVGDD
TVIFNQKRMI DMVAVRIVNR RLESRARGGG SFISAGANLE DISRSANATL MNILPLGNDW
QTALKDVRTG IADAIATPPT QGEIDRELTD IQTSMKASVA QASVEAGAKK ADDLVDAVDI
KETTTTAQTS LGILQDAIAK KMFTPAAVQA SAKAVFSGVA LRGVVNTPQP SENAAAALQA
ALTAEMKPGV AANSKLAAIG FDALPKLGAP GKVVARSIAV TDPKMEKVTF ANGVNLLLFE
NPSEASRVYV RVRFGRGLAG LPADRQTPVY AGDLALVASG IGKLGQEEID RITTGRRIAL
DFAVDEDAFL FGATTSAEDL ADQLKLIAAK LSTPGWDPNP VARAKAVMLA GYASQAASPD
GVLARDLDRL LHDGDPRWGT PSRADLEKLD ARSFRAFWEP ILASGPIEVQ IYGDMKSDAA
IAAVASSLGA LKPRKDAPVA TAPIRFPAPT TTPVTRTHDG RDTQAAAVIA WPTGGGSDGI
ATGRKLEVLA AVFRDRLLDK LRSSAGISYT PNVASNWPVG LSGGGRIMAI GSVPPDKTGY
FFDLSREIAA DLVARPVDAD ELRRALVPVV QFVARLSTGN QFWLMQTEGG STDPKRLAAL
NTIATDLTTI TPSELQALAA QYLVPAKAWT MTVLPKDGAA GAAK
//