ID   A0A222X662_9CELL        Unreviewed;       669 AA.
AC   A0A222X662;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Dipeptidyl aminopeptidase {ECO:0000313|EMBL:ASR54317.1};
GN   ORFNames=CBP52_03225 {ECO:0000313|EMBL:ASR54317.1};
OS   Cellulomonas sp. PSBB021.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Cellulomonas.
OX   NCBI_TaxID=2003551 {ECO:0000313|EMBL:ASR54317.1, ECO:0000313|Proteomes:UP000214627};
RN   [1] {ECO:0000313|EMBL:ASR54317.1, ECO:0000313|Proteomes:UP000214627}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PSBB021 {ECO:0000313|EMBL:ASR54317.1,
RC   ECO:0000313|Proteomes:UP000214627};
RA   Song R., Chenine A.L., Ruprecht R.M.;
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP021430; ASR54317.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A222X662; -.
DR   KEGG; cez:CBP52_03225; -.
DR   OrthoDB; 262125at2; -.
DR   Proteomes; UP000214627; Chromosome.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
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; 2.120.10.30; TolB, C-terminal domain; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR011659; PD40.
DR   InterPro; IPR001375; Peptidase_S9.
DR   PANTHER; PTHR42776:SF28; DIPEPTIDYL-PEPTIDASE 5; 1.
DR   PANTHER; PTHR42776; SERINE PEPTIDASE S9 FAMILY MEMBER; 1.
DR   Pfam; PF07676; PD40; 2.
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:ASR54317.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000313|EMBL:ASR54317.1}.
FT   DOMAIN          455..659
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
SQ   SEQUENCE   669 AA;  71384 MW;  0CB6E83E2DF389F8 CRC64;
     MLPHDLFHLR TPGSVALVPD GSAAVVALSQ PDEEADEYRG GLWLVPLDGS APRVLTRGHA
     DSAPDVSPDG RWVVFVRSTT GDKPQLYVVE TSGGEPFRVT DQPLGAGQPR FSPDGRRIAY
     VARVPDEGRY AADGDAGAER PRLITQLRNR ADGLGHLRDR VRQVFVLEVP DASGSTVHVP
     ASYALTCADD DVDLPHWFPD GRAVAALLRR HGTREQDLRR DAVALLVPED LTGVSGDAQV
     VPLTDADAGA SLSLSRAVPA PDGARVWLLA EDVGESGRDF VAALTGLFEL PLTAEARPAG
     PPRRVTDPDE VDLDPGVLVP VGDGVLVAPL RSGAVHLTLV GSDGGSRDLL DGAVVVGAAA
     AAGGAVVAVR ATPDSAGDVV LVDTGRALTD WSAPLRATGR VRVSEPLVAH APDGYRVEGW
     LTTPDPDRYG AGPHPTILLI HGGPFAQYTH ALFDEVQTLA EAGYAVVHGN PRGSSGRGRA
     HGRAIRRAFG TVDADDVLAL LDEALTDPRL DPQRTGVMGG SYGGYLTAWL TTRTQRFAAA
     IVERGFLDPV SFTGSSDIGW FFGLEYLGDP ATEAELVAAQ SPMARVAEVG TPTLVVHSEQ
     DWRCPVEQGQ RWFVELRRRG VPSELLLFPG EGHELTRSGR PSHRVARFEH VLRWWDRWLP
     VGSRSRDVA
//