ID A0A0Q6L1U2_9SPHN Unreviewed; 943 AA.
AC A0A0Q6L1U2;
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:KQU61891.1};
GN ORFNames=ASG67_01610 {ECO:0000313|EMBL:KQU61891.1};
OS Sphingomonas sp. Leaf339.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736343 {ECO:0000313|EMBL:KQU61891.1, ECO:0000313|Proteomes:UP000051371};
RN [1] {ECO:0000313|EMBL:KQU61891.1, ECO:0000313|Proteomes:UP000051371}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf339 {ECO:0000313|EMBL:KQU61891.1,
RC ECO:0000313|Proteomes:UP000051371};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQU61891.1, ECO:0000313|Proteomes:UP000051371}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf339 {ECO:0000313|EMBL:KQU61891.1,
RC ECO:0000313|Proteomes:UP000051371};
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:KQU61891.1}.
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DR EMBL; LMRS01000001; KQU61891.1; -; Genomic_DNA.
DR RefSeq; WP_056524340.1; NZ_LMRS01000001.1.
DR AlphaFoldDB; A0A0Q6L1U2; -.
DR STRING; 1736343.ASG67_01610; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000051371; 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; PTHR11851; METALLOPROTEASE; 1.
DR PANTHER; PTHR11851:SF229; PEPTIDASE M16 DOMAIN PROTEIN; 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 Reference proteome {ECO:0000313|Proteomes:UP000051371};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..943
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006282513"
FT DOMAIN 49..195
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 204..381
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 519..643
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 669..843
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 943 AA; 99496 MW; 4B3ADBEA04F1A62F CRC64;
MKLRLALLLA AALPTGVVAQ TVAPVPPAPS AVKPIAFTER TLSNGLRVYA LRDTGTPNVS
VQVWYDVGSK DDPAGRSGFA HMFEHLMFKA TRNLVPEQMD RLTEDVGGYN NASTNDDYTN
YYELVPANHL QRLLFAEADR MASLIVEPVT FASERDVVKE ELRQSTMARP YGKLFSTYLS
AASYTTHPYA RSTIGSIDEL QAASIDDVRA FHATYYRPDN AILVVSGNFD PAQLNAWIDR
YFAPIKRPAG PIPRVTVTEP ARTKAVTYTT YEPNTPLPAV VMTWHVPPDN AADIPALTVL
QTVLATGESS RLYENVVYRD QLAQSAEAFL DTKKGTGNLI AYAIMAGGKT VDQGEAALKR
EIARFRDAPV SAAELTEAKN QILTGAIKGR ETAEGKARVI ASSVIIDGDP RDADRQLAAI
ATVTAADVQR VARQYLGDNQ AAIIRYLPGQ PPANVRLMPI TVAPTVKVAA LTPPANIQVV
TAATGPARIM PPAPTAPIAA VLPQPVETKL ANGMRLITVE RHGLPIVTAA LVAIGGGATD
PAMQSGVANL TAGLMTKGTA TRSATEIARA VEALGGSIGS SADRDGSSVS LTVKSDQLAK
AMPILADVAI RPAFAPEEIE RARAQTIDGI EVTLKDPAQL AALVATRAVF GKGPYAPPLD
GTPTSLKAIT RDDITRSYAG TWSPDRAALV MVGDVTPAAA RALAESQFGT WKATPLPPAV
MLAAPPAPRV IVVDMPDAGQ AGVVVARPGI MRGDDRYYPL NVGNTVLGGG FSSRLNQEIR
IKRGLAYGAG SSVTARRLGG SVSARTQTKN PTAAEAVQLI AAEMARMGAT PVPADELDTR
KAVLVGGFGR AIETTDGVAD IIGDYVVQDV PLTEIGRYTA KVQGVDPAAV QKAAQALLDP
KAASVVVVGD AKQFIAPLKA LYPNVEVIPA AALDLNTASL RRP
//