ID A0A0Q4CX11_9SPHN Unreviewed; 941 AA.
AC A0A0Q4CX11;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Peptidase M16 {ECO:0000313|EMBL:KQM29098.1};
GN ORFNames=ASE58_02700 {ECO:0000313|EMBL:KQM29098.1};
OS Sphingomonas sp. Leaf9.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1735674 {ECO:0000313|EMBL:KQM29098.1, ECO:0000313|Proteomes:UP000051210};
RN [1] {ECO:0000313|EMBL:KQM29098.1, ECO:0000313|Proteomes:UP000051210}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf9 {ECO:0000313|EMBL:KQM29098.1,
RC ECO:0000313|Proteomes:UP000051210};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQM29098.1, ECO:0000313|Proteomes:UP000051210}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf9 {ECO:0000313|EMBL:KQM29098.1,
RC ECO:0000313|Proteomes:UP000051210};
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}.
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:KQM29098.1}.
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DR EMBL; LMKC01000001; KQM29098.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q4CX11; -.
DR Proteomes; UP000051210; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; 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; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR43690:SF18; INSULIN-DEGRADING ENZYME-RELATED; 1.
DR PANTHER; PTHR43690; NARDILYSIN; 1.
DR Pfam; PF00675; Peptidase_M16; 2.
DR Pfam; PF05193; Peptidase_M16_C; 2.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 51..142
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 208..380
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 520..635
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 667..842
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 941 AA; 99514 MW; 5DFC2A2D52676544 CRC64;
MLASTALAGT AAHAQAPAPA APPVKAAPLS ALVAPVDIPY EKFTLPNGLT VITHTDRKAP
IVAVSVWYDV GSKHEPEGKT GFAHLFEHLM FNGSENAPGD FFDPLRSIGA TDLNGTTSYD
RTNYFETVPK PALDRALFLE SDRMGYLLGA VTQGVLDEQR GVVQNEKRQG DNQPYGLVRY
KMTEGIFPQG HPYRHSVIGS MADLDAASLE DVKNWFRGHY GPNNAVLVLA GDIDAKEARP
LVEKYFGKIA KGPESVLPKI TVPTLAAPVR EVMKDNVAAT MIMKVWPVPG LNDPDSPALD
VAMSAFGGLA SSRLDNELVK KDKLAVQVSA GVQSLSQAGM LIVRAIVRPG VKTEVVEAKL
DQMIADYLRT GPTADEVARV ATTQVSGTIG GLESVGGFGG KAVTLASGQL YSNDPGFYKK
ELNALATMTP DRARAAAQKW MSRPAYTLIV ENGQREGYEE AKAVAAAPAA PAAEVPFKGT
RGAMPGVADS GAALQFPKVT HSRLSNGMEL VYAQRIAVPV TQVSMVFDAG TAADVAGKLG
TAGMTLALID EGTTTRNSIA MAEAKEKLGM SMSGGNSPDQ TTIGFEVPSA NLTSATGLFA
DVLRNPAFDA NELERVRGQV LAQIGQQRTN PQGLADMTLP PLLYGTDSPY AKLAAGVGDP
AAVMAMKRDD LVAWRGAWLR PDKAKVFVVS DRPLAEVQAA LNASLGNWQA TGAAGTKRFP
AQRATTAPKI VLVDRPNSPQ SLIVAGQMTP VQAKSDTLAA TTANTVLGSG FLSRINMDLR
EAKHWSYGAG GGYRLMENAV PYVISAPVQA DKTGASIASL REQINGFLGK NGVTPVEFRR
TIDGETRQLA GTYETSGAVL AAMRNNDFLG RPDDYQATLP QKYRALTTAQ LDAAARATID
PNRFVYVVVG DAKVVRPQLD GLGLPVEVVS ATPATAPTPA K
//