ID   PQQL_ARATH              Reviewed;         956 AA.
AC   Q9FJT9;
DT   16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Zinc protease PQQL-like {ECO:0000305};
DE            EC=3.4.24.- {ECO:0000305};
GN   OrderedLocusNames=At5g56730 {ECO:0000312|Araport:AT5G56730};
GN   ORFNames=MIK19.18 {ECO:0000312|EMBL:BAB09891.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA   Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT   features of the regions of 1,367,185 bp covered by 19 physically assigned
RT   P1 and TAC clones.";
RL   DNA Res. 5:203-216(1998).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the peptidase M16 family. {ECO:0000305}.
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; AB013392; BAB09891.1; -; Genomic_DNA.
DR   EMBL; CP002688; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; Q9FJT9; -.
DR   SMR; Q9FJT9; -.
DR   STRING; 3702.AT5G56730.1; -.
DR   MEROPS; M16.A03; -.
DR   iPTMnet; Q9FJT9; -.
DR   PaxDb; Q9FJT9; -.
DR   PeptideAtlas; Q9FJT9; -.
DR   PRIDE; Q9FJT9; -.
DR   Araport; AT5G56730; -.
DR   TAIR; locus:2165081; AT5G56730.
DR   eggNOG; KOG0959; Eukaryota.
DR   HOGENOM; CLU_008156_0_0_1; -.
DR   InParanoid; Q9FJT9; -.
DR   PhylomeDB; Q9FJT9; -.
DR   PRO; PR:Q9FJT9; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FJT9; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR   GO; GO:0009536; C:plastid; HDA:TAIR.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 2.
DR   SUPFAM; SSF63411; SSF63411; 2.
DR   PROSITE; PS00143; INSULINASE; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW   Reference proteome; Zinc.
FT   CHAIN           1..956
FT                   /note="Zinc protease PQQL-like"
FT                   /id="PRO_0000435731"
FT   ACT_SITE        88
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT   ACT_SITE        165
FT                   /evidence="ECO:0000305"
FT   BINDING         85
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT   BINDING         89
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT   BINDING         172
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:22223895"
SQ   SEQUENCE   956 AA;  107981 MW;  23327FEBC11701B1 CRC64;
     MDLIAGESSK VLRKQGFRSL KLMSVDMEQE LGNELEPFGA DYGRLDNGLI YYVRRNSKPR
     MRAALALAVK VGSVLEEEDQ RGVAHIVEHL AFSATTRYTN HDIVKFLESI GAEFGPCQNA
     MTTADETIYE LFVPVDKPEL LSQAISILAE FSSEIRVSKE DLEKERGAVM EEYRGNRNAT
     GRMQDSHWQL MMEGSKYAER LPIGLEKVIR SVPAATVKQF YQKWYHLCNM AVVAVGDFPD
     TKTVVDLIKT HFEDKRSSSE PPQIPVFPVP SHEETRFSCF VESEAAGSAV MISYKMPVSD
     LKTVKDYRDM LAESMFLHAL NQRLFKISRR KDPPFFACSV AADVLVARVR LHGFSEREIS
     VVRALMMSEI ESAYLERDQV QSTSLRDEYI QHFLHKEPVI GIEYEAQLQK TLLPQISASD
     VSRYSEKLRT SCGCVIKSME PKSAATIDHM RNVVSKVNSL EEEKMIAPWD EENIPEEIVS
     EKPTPGDITH QLEYPEVGVT ELTLSNGMQV CYKSTDFLDD QVLFTGFSYG GLSELPESDY
     ISCSMGSTIA GEIGMFGYKP SVLMDMLADL ETALQLVYQL FTTNVMPQEE EVGIVMQMAE
     ESVRARERDP YTVFANRVKE LNYGNSYFFR PIRISELRKV DPLKACEYFN SCFRDPSTFT
     VVIVGNLDPT IALPLILQYL GGIPKPPQPV LNFNRDDLKG LPFTFPTKIT KEFVRSPMVE
     AQCSVQLCFP VQLTNGTMIE EIHCIGFLGK LLETKIIQFL RFEHGQIYSA EVSVFLGGNK
     PSRTADLRGD ISVNFSCDPE ISSKLVDLAL EEIVRLQKEG PSQEDISAIL EIEQRAHENG
     MQENYYWLDR IIRGYQSRVY AGDLGASCKI LEEGRLRMRE SLAPQTAQAA LQRILPHPCK
     KQYTAVILMP QRSRFGFLSS IFSSRSEGPY IRDTKILAGI AGLGVVVFGI WRYSRK