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Database: UniProt
Entry: A0A0Q5CVU0_9BURK
LinkDB: A0A0Q5CVU0_9BURK
Original site: A0A0Q5CVU0_9BURK 
ID   A0A0Q5CVU0_9BURK        Unreviewed;       607 AA.
AC   A0A0Q5CVU0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=Peptidase M24 {ECO:0000313|EMBL:KQQ32822.1};
GN   ORFNames=ASF61_14545 {ECO:0000313|EMBL:KQQ32822.1};
OS   Duganella sp. Leaf126.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Duganella.
OX   NCBI_TaxID=1736266 {ECO:0000313|EMBL:KQQ32822.1, ECO:0000313|Proteomes:UP000051032};
RN   [1] {ECO:0000313|EMBL:KQQ32822.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf126 {ECO:0000313|EMBL:KQQ32822.1};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQQ32822.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf126 {ECO:0000313|EMBL:KQQ32822.1};
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 M24B family.
CC       {ECO:0000256|ARBA:ARBA00008766}.
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:KQQ32822.1}.
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DR   EMBL; LMNW01000033; KQQ32822.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q5CVU0; -.
DR   STRING; 1736266.ASF61_14545; -.
DR   Proteomes; UP000051032; Unassembled WGS sequence.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR   CDD; cd01085; APP; 1.
DR   Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 1.
DR   Gene3D; 3.40.350.10; Creatinase/prolidase N-terminal domain; 2.
DR   InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR   InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR   InterPro; IPR000587; Creatinase_N.
DR   InterPro; IPR000994; Pept_M24.
DR   InterPro; IPR033740; Pept_M24B.
DR   InterPro; IPR032416; Peptidase_M24_C.
DR   PANTHER; PTHR43763; XAA-PRO AMINOPEPTIDASE 1; 1.
DR   PANTHER; PTHR43763:SF6; XAA-PRO AMINOPEPTIDASE 1; 1.
DR   Pfam; PF01321; Creatinase_N; 1.
DR   Pfam; PF16189; Creatinase_N_2; 1.
DR   Pfam; PF00557; Peptidase_M24; 1.
DR   Pfam; PF16188; Peptidase_M24_C; 1.
DR   SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
DR   SUPFAM; SSF53092; Creatinase/prolidase N-terminal domain; 1.
PE   3: Inferred from homology;
FT   DOMAIN          12..138
FT                   /note="Creatinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01321"
FT   DOMAIN          317..536
FT                   /note="Peptidase M24"
FT                   /evidence="ECO:0000259|Pfam:PF00557"
FT   DOMAIN          548..606
FT                   /note="Peptidase M24 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16188"
SQ   SEQUENCE   607 AA;  66014 MW;  979910F4E722B5E6 CRC64;
     MPMTTSPPPA KRLQRLRDAM RQHGVDAVLV PSADPHLSEY LPPRWQGRAW LSQFTGSVGT
     FIITHQFCGI WTDARYWTQA EQQLAGSGIE LMKITSGASV QYIDWLAAHV KPGQTVAVDG
     AVLGLSIARL LQQALAAREA TLRFDLDLLD AVWRDRPGLP TAPVFEHLPP YASKSRSGKL
     ADVRAAMQQQ GANRHVISTL DDIAYLFNLR GADVPFNPVF LAHALVTPTR ATLFVADGKM
     SPELREQLAQ EAIDVARYDS LAAALAALGP DTTVLIDPRR VTHGTRQALP AKVKVVEATN
     PTTLAKARKS EADAIHVRAV MEQDGAALCE FFSWLDATLA DRERPGAAEL TELTIDAQIT
     AARARRPGFV SPSFATIAGF RANGAIMHYR ATEAQHAVIE GDGLLLIDSG GQYLGGTTDI
     TRMVAVGAIS AEHKRDVTLV LKGLIALSSA HFPRGTRAPM LDAIARAPLW AAGIDYGHGT
     GHGVGYFLNV HEGPQSISPS AMPEPQTAME PGMITSIEPG LYRPGKWGIR LENLVLNRSA
     GQTDFGDFLQ FETLTLCPID TRCLAVALLR DDERRWLNDY HAMVRERLSP LVTGAALTWL
     HQRTETL
//
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