ID A0A0Q4GXH0_9BURK Unreviewed; 447 AA.
AC A0A0Q4GXH0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Zinc protease {ECO:0000313|EMBL:KQM80296.1};
GN ORFNames=ASE76_03920 {ECO:0000313|EMBL:KQM80296.1};
OS Xylophilus sp. Leaf220.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Xylophilus.
OX NCBI_TaxID=1735686 {ECO:0000313|EMBL:KQM80296.1, ECO:0000313|Proteomes:UP000051325};
RN [1] {ECO:0000313|EMBL:KQM80296.1, ECO:0000313|Proteomes:UP000051325}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf220 {ECO:0000313|EMBL:KQM80296.1,
RC ECO:0000313|Proteomes:UP000051325};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQM80296.1, ECO:0000313|Proteomes:UP000051325}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf220 {ECO:0000313|EMBL:KQM80296.1,
RC ECO:0000313|Proteomes:UP000051325};
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:KQM80296.1}.
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; LMKO01000001; KQM80296.1; -; Genomic_DNA.
DR RefSeq; WP_055834881.1; NZ_LMKO01000001.1.
DR AlphaFoldDB; A0A0Q4GXH0; -.
DR STRING; 1735686.ASE76_03920; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000051325; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0008233; F:peptidase 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; PTHR11851:SF149; GH01077P; 1.
DR PANTHER; PTHR11851; METALLOPROTEASE; 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:0000313|EMBL:KQM80296.1};
KW Protease {ECO:0000313|EMBL:KQM80296.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051325};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..447
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006219570"
FT DOMAIN 43..191
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 204..379
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 447 AA; 47770 MW; A0AE55FA0573886F CRC64;
MFAIKTIAIG RHIAPAVALF CLNPAFAALP IEHWTQPAGA QVYLVQSKAV PMVDVQIDFD
AGARRDPAAQ AGLAAVTASM SEKGVRAHGR EPALDENAID DAWADLGANF GAGATSDRMS
FTLRSLTDAA LLDRAAQLAA RQIGEPSFPD AIWQRERQRI TAALKEADTR PATQAGRAFQ
RAVYGSHPYG QRTTPQTLTA IGVADMRALQ ARALRSCGAK VSIVGALDRV QADRLATKLL
GRLPAGPCTP LPAVAEVQPL AAPQDIRIPF DSAQAHVYIG QPGFRRADPD YFALTVGNYI
LGGGGFVSRL TEQVREQRGL SYSVQSWFEP ALHAGAFTIN LQTRPDQAAQ AVDVARAVLD
RFVADGPTPQ ELQAAKDNLV GGFPLRIDSN AKLLSNVANI AWNGLPLDYL DTWTAQAQKV
TADDIRAAFG RKLQPDRMVT VVVGGTP
//
