ID A0A0Q9RQJ6_9BACL Unreviewed; 357 AA.
AC A0A0Q9RQJ6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Xaa-Pro dipeptidase {ECO:0000313|EMBL:KRF12069.1};
GN ORFNames=ASG93_14730 {ECO:0000313|EMBL:KRF12069.1};
OS Paenibacillus sp. Soil787.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1736411 {ECO:0000313|EMBL:KRF12069.1, ECO:0000313|Proteomes:UP000051948};
RN [1] {ECO:0000313|EMBL:KRF12069.1, ECO:0000313|Proteomes:UP000051948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil787 {ECO:0000313|EMBL:KRF12069.1,
RC ECO:0000313|Proteomes:UP000051948};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRF12069.1, ECO:0000313|Proteomes:UP000051948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil787 {ECO:0000313|EMBL:KRF12069.1,
RC ECO:0000313|Proteomes:UP000051948};
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 -!- 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:KRF12069.1}.
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DR EMBL; LMSP01000045; KRF12069.1; -; Genomic_DNA.
DR RefSeq; WP_056837851.1; NZ_LMSP01000045.1.
DR AlphaFoldDB; A0A0Q9RQJ6; -.
DR STRING; 1736411.ASG93_14730; -.
DR OrthoDB; 9806388at2; -.
DR Proteomes; UP000051948; Unassembled WGS sequence.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProt.
DR GO; GO:0008235; F:metalloexopeptidase activity; IEA:UniProt.
DR GO; GO:0046914; F:transition metal ion binding; IEA:UniProt.
DR CDD; cd01092; APP-like; 1.
DR Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 1.
DR Gene3D; 3.40.350.10; Creatinase/prolidase N-terminal domain; 1.
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; IPR001714; Pept_M24_MAP.
DR InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS.
DR PANTHER; PTHR46112; AMINOPEPTIDASE; 1.
DR PANTHER; PTHR46112:SF3; AMINOPEPTIDASE YPDF; 1.
DR Pfam; PF01321; Creatinase_N; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR PRINTS; PR00599; MAPEPTIDASE.
DR SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
DR SUPFAM; SSF53092; Creatinase/prolidase N-terminal domain; 1.
DR PROSITE; PS00491; PROLINE_PEPTIDASE; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 5..130
FT /note="Creatinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01321"
FT DOMAIN 138..340
FT /note="Peptidase M24"
FT /evidence="ECO:0000259|Pfam:PF00557"
SQ SEQUENCE 357 AA; 39726 MW; 962EA732B8598EF1 CRC64;
MQEKRLERLR KVMQQQDLPA ILITNAYNRT YVSGFTGSSG YVLITLDRAL LLTDFRYMTQ
APQQAKLFEV VEHKAKAIET VKELLQQQGI TKLGFEQVDV SYGDFLSYQE GLAGIELVPT
SRVVELIRMV KDEAELQIMQ EAADLADQTF SHILSFIKPG VKEKDIALEI EIFIRKNGGT
STSFETIVAS GERSALPHGK ASDRVLQLNE FVKLDFGAYY KGYCSDITRT VMLGKPTDKH
KEIYDIVLEA QLNCLANLKP GISGREGDAY ARDVIVKHGY GDYFGHGTGH GLGMEVHENP
RLSKTEDMIL TPGMVVTVEP GIYLPGFGGV RIEDDAVITD TGIKILTHST KDFLIID
//
