ID A0A2S2E1T0_9ALTE Unreviewed; 831 AA.
AC A0A2S2E1T0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Dipeptidyl-peptidase IV {ECO:0000313|EMBL:AWL11605.1};
DE EC=3.4.14.5 {ECO:0000313|EMBL:AWL11605.1};
GN Name=dpp4 {ECO:0000313|EMBL:AWL11605.1};
GN ORFNames=HMF8227_01124 {ECO:0000313|EMBL:AWL11605.1};
OS Saliniradius amylolyticus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Saliniradius.
OX NCBI_TaxID=2183582 {ECO:0000313|EMBL:AWL11605.1, ECO:0000313|Proteomes:UP000245728};
RN [1] {ECO:0000313|EMBL:AWL11605.1, ECO:0000313|Proteomes:UP000245728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMF8227 {ECO:0000313|EMBL:AWL11605.1,
RC ECO:0000313|Proteomes:UP000245728};
RA Kang H., Kang J., Cha I., Kim H., Joh K.;
RT "Salinimonas sp. HMF8227 Genome sequencing and assembly.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP029347; AWL11605.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S2E1T0; -.
DR KEGG; salh:HMF8227_01124; -.
DR Proteomes; UP000245728; Chromosome.
DR GO; GO:0008239; F:dipeptidyl-peptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
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:SF203; PEPTIDASE S9 FAMILY; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AWL11605.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000245728};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..831
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015633633"
FT DOMAIN 382..543
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 635..830
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
FT REGION 26..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 831 AA; 95082 MW; 5852109C51816B88 CRC64;
MMQNKSKILT ALVLSGALAA CSTTSQTPEM DASTNAATTA APAVQAESMS PATDGTITLE
QVMAHPDWLG RQPQKPFWSL DSEQVRYWRK RDGQPIEDLW QSDAANAGNG DKLSLSEYHL
ADNADRVFNS ERSQVLWVFE NNLFIKNLDS GEVRQLTRTD KPIQSPQFLL DGRIAYQSGN
GFYAIHPQSG FTELLVSWQF SEPPKANKEL NDYLAREQVK LIDYVAKERA DRHAKFEHKQ
ALQQQNPATG PQPFYLKEGF KTVDASLSPD GKRVILAIQE DKPSRSDGDI MPNYINEDGR
IYAESARRMV ADAESVNQEL LLLELEAHQQ HALSYQTLPG YNEDVLAEVK KENAEAKGET
YEPNRLPRDI GLMTDWYWHQ SAIEWHNSGE QVAVMLQAWD NKDRWIATVD LKDRVLVSQH
RLHDDAWINY KFNSFGWLNN SQRLYFLSEQ SGYAHLYLQT PGTKEQALTY GDYVVDDLTL
THDDQYIYFR ANKKHPGIYE IYRVNLENGA IEPITDMGGM NEYVLSPDEQ RLIITHSKIT
MPPELYVQRA DVAQRPMKLT STVSEAFQSL PWTAPKIMPV PSSHTDKPIY SKVYLPEDYQ
AGEKRKAVIF NHGAGYLQNS HMGWSGYFRE FMFHSMLVQQ GYVVMDMDYR ASQGYGRDWR
TAIYRQMGTP ETQDLSDGVN WLVNNANVGR DNVCTYGGSY GGFMTFMALF TEPDLFQCGA
ALRPVTDWAY YNTPYTSNIL NTPQVDPIAY KRSSPIYHAE GLEKPLLINA PMIDDNVFFV
DVVRLVQRLI ELEKQDFETA IYPVEPHGFR QPSSWLDEYR RIYKLFEENL E
//