ID   A0A0Q6L1Z1_9SPHN        Unreviewed;       724 AA.
AC   A0A0Q6L1Z1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=Dipeptidyl carboxypeptidase {ECO:0000313|EMBL:KQU59190.1};
GN   ORFNames=ASG67_16835 {ECO:0000313|EMBL:KQU59190.1};
OS   Sphingomonas sp. Leaf339.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1736343 {ECO:0000313|EMBL:KQU59190.1, ECO:0000313|Proteomes:UP000051371};
RN   [1] {ECO:0000313|EMBL:KQU59190.1, ECO:0000313|Proteomes:UP000051371}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf339 {ECO:0000313|EMBL:KQU59190.1,
RC   ECO:0000313|Proteomes:UP000051371};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQU59190.1, ECO:0000313|Proteomes:UP000051371}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf339 {ECO:0000313|EMBL:KQU59190.1,
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|RuleBase:RU003435};
CC       Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC   -!- SIMILARITY: Belongs to the peptidase M3 family.
CC       {ECO:0000256|RuleBase:RU003435}.
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:KQU59190.1}.
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; LMRS01000003; KQU59190.1; -; Genomic_DNA.
DR   RefSeq; WP_056526984.1; NZ_LMRS01000003.1.
DR   AlphaFoldDB; A0A0Q6L1Z1; -.
DR   OrthoDB; 9773538at2; -.
DR   Proteomes; UP000051371; Unassembled WGS sequence.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd06456; M3A_DCP; 1.
DR   Gene3D; 1.10.1370.40; -; 3.
DR   InterPro; IPR034005; M3A_DCP.
DR   InterPro; IPR045090; Pept_M3A_M3B.
DR   InterPro; IPR001567; Pept_M3A_M3B_dom.
DR   PANTHER; PTHR43660; DIPEPTIDYL CARBOXYPEPTIDASE; 1.
DR   PANTHER; PTHR43660:SF1; DIPEPTIDYL CARBOXYPEPTIDASE; 1.
DR   Pfam; PF01432; Peptidase_M3; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000313|EMBL:KQU59190.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003435};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU003435};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU003435};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003435};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051371};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..724
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006282518"
FT   DOMAIN          269..715
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   724 AA;  80131 MW;  0B459891D8C565BF CRC64;
     MIRSPWLQSV ALLGLLASGA NAQTASPRAG SGKANSISER ANPLVVPSTL PFQAPRFDQI
     ADADYQPALE QGMAEQITEM RAIRVQRSAP TFQNTIEAME RSGRTLDRAS QAFFGVAQAN
     TNDTLDKTRS VMAPKMAQNN DAIYLDPQLF ARVDTLYKQR DKLSLTPEQR QVLELYHSDF
     LHAGAQLNDA DKTKLRALNT EISSATTAFQ QQLLAATKAG ALVVDDKAQL AGLSDAEIAA
     AAEGAKDRGM PGKYVLSLQN TTQQPALGSL TDRQTRAALF AKAWTRAEQG DANDTRTLII
     KIARLRAEKA KLLGYPNYAA YSLYDQMAKT PEAAKRFMAQ LVPATAAEQR REAAELQRTI
     NASGASYPLT PADWDYNSEK VRKAKYDLDQ NELKPYFEIS RVLTDGVFFA AGQLYGVTFK
     ERRDIPVYQT DVRVFTVYDK DGSELGLMYF DYWKRDNKAG GAWMSNFVGQ SKLLGTKPIV
     YNVANFTKPA PGQPALITFD DVTTMFHEFG HALHGLFANQ TYPLVSGTNT ARDWVEFPSQ
     FNEHWALDPK ILANYAKDYR TGAPMPTTLV TKIKNAAKFN QGYELGELVA AATLDQDWHA
     LPAGSTPTDV DAFEAAKLAD MGLDTKDVPP RYRTSYFAHI WAGGYAAGYY AYLWTQMLDN
     DAYAWFMAHG GLTRANGQRF RDMILSKGHT EDYGPMFRTF YGKDPDIEPM LEDRGLTATA
     TASK
//