ID A0A1M5R988_9BURK Unreviewed; 785 AA.
AC A0A1M5R988;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Dipeptidyl aminopeptidase/acylaminoacyl peptidase {ECO:0000313|EMBL:SHH22914.1};
GN ORFNames=SAMN05428948_3417 {ECO:0000313|EMBL:SHH22914.1};
OS Massilia sp. CF038.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1881045 {ECO:0000313|EMBL:SHH22914.1, ECO:0000313|Proteomes:UP000184361};
RN [1] {ECO:0000313|EMBL:SHH22914.1, ECO:0000313|Proteomes:UP000184361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF038 {ECO:0000313|EMBL:SHH22914.1,
RC ECO:0000313|Proteomes:UP000184361};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FQWU01000002; SHH22914.1; -; Genomic_DNA.
DR RefSeq; WP_073218944.1; NZ_FQWU01000002.1.
DR AlphaFoldDB; A0A1M5R988; -.
DR STRING; 1881045.SAMN05428948_3417; -.
DR OrthoDB; 9812921at2; -.
DR Proteomes; UP000184361; Unassembled WGS sequence.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 2.140.10.30; Dipeptidylpeptidase IV, N-terminal domain; 1.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001375; Peptidase_S9.
DR InterPro; IPR002469; Peptidase_S9B_N.
DR PANTHER; PTHR11731:SF193; DIPEPTIDYL PEPTIDASE 9; 1.
DR PANTHER; PTHR11731; PROTEASE FAMILY S9B,C DIPEPTIDYL-PEPTIDASE IV-RELATED; 1.
DR Pfam; PF00930; DPPIV_N; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
PE 4: Predicted;
KW Aminopeptidase {ECO:0000313|EMBL:SHH22914.1};
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000313|EMBL:SHH22914.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000184361};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..785
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013177912"
FT DOMAIN 337..497
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 590..784
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
FT REGION 193..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..213
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 785 AA; 88293 MW; ECBDCB104D9A4843 CRC64;
MRLSALPLLA AIWTISGAAS AATPISLDQA MAHPDWIGTP VENAWWSWDS KQVFYKQKRT
GSQLRDTFQA LPGAARKISD TELANLDSER VVYNRERNRA ILLRNGDLFE RDLKTGALTQ
VTRGSTGLAA PQYSADGRAI QFRVGHEWLS WNRADHLVSP VAAARATKDP AAAPDEDALR
DLQLRLISTL KRQKDDRDAG RARAEEERRA DPTRAPAPIY LGDKVVIEGS ALSPDGHYLI
VVTAPKSADK GRIGKLPRYV TESGYEEFDD QRPRVGRNMP PEHTVKLVDL STRQVRDLSF
DVLPGVANDP LAAMRAERKL PALKGNRVVR VDDDGETIQW NGNGTQVAVL LRAVDNKDRW
IATVDLKDAK FKPVHRLTDP AWVNSGSNEF GWLNDNSTLW YLSEESGYSH LYTLGADGKA
RALTQGKWEA TRIDWSADGA NAYMLCNPKA PGTYEVCTVN TRDGKLREVT ALEGVEQYAL
SPDQRKLLVH YSSSYMPAQL ATVPVSGGAA VKLTDTRSAE FKARSWIEPQ IVAVPSTHGA
GPIYGKLYRP ATLEAGKQYP IVMFVHGAGY LQNVSKRYPV YFREQMFHNL LVEKGYIVLD
MDYRASKGYG RDWRTAIYRQ MGYPELEDYV DGVNWMAANH QGDLKNVGVY GGSYGGFMTF
MALMREPELF KSGAALRPVT DWTTYNHEYT ANILNTPDLD PEAYRKSSPI EYADKLKGNL
LISHGMVDDN VFYQDSVRMA QRLIELKKDH WELASYPLER HAFVQPESWY DQYRRIYQLF
ERTLK
//