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Database: UniProt
Entry: A0A0J1BMW8_9SPHI
LinkDB: A0A0J1BMW8_9SPHI
Original site: A0A0J1BMW8_9SPHI 
ID   A0A0J1BMW8_9SPHI        Unreviewed;       694 AA.
AC   A0A0J1BMW8;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Acyl-peptide hydrolase {ECO:0000256|ARBA:ARBA00032596};
DE   AltName: Full=Acylaminoacyl-peptidase {ECO:0000256|ARBA:ARBA00032284};
GN   ORFNames=AB669_05900 {ECO:0000313|EMBL:KLT66698.1};
OS   Pedobacter sp. BMA.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=1663685 {ECO:0000313|EMBL:KLT66698.1, ECO:0000313|Proteomes:UP000036014};
RN   [1] {ECO:0000313|EMBL:KLT66698.1, ECO:0000313|Proteomes:UP000036014}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BMA {ECO:0000313|EMBL:KLT66698.1,
RC   ECO:0000313|Proteomes:UP000036014};
RA   Anderson B.M., Pipes S.E., Miller J.R., Newman J.D.;
RT   "Pedobacter sp. BMA.";
RL   Submitted (JUN-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:KLT66698.1}.
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DR   EMBL; LECU01000003; KLT66698.1; -; Genomic_DNA.
DR   RefSeq; WP_047798359.1; NZ_LECU01000003.1.
DR   AlphaFoldDB; A0A0J1BMW8; -.
DR   STRING; 1663685.AB669_05900; -.
DR   PATRIC; fig|1663685.3.peg.1234; -.
DR   OrthoDB; 9777457at2; -.
DR   Proteomes; UP000036014; Unassembled WGS sequence.
DR   GO; GO:0008242; F:omega peptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004252; F:serine-type endopeptidase 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; 2.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR011659; PD40.
DR   InterPro; IPR002471; Pept_S9_AS.
DR   InterPro; IPR001375; Peptidase_S9.
DR   InterPro; IPR002469; Peptidase_S9B_N.
DR   PANTHER; PTHR42776:SF27; DIPEPTIDYL PEPTIDASE FAMILY MEMBER 6; 1.
DR   PANTHER; PTHR42776; SERINE PEPTIDASE S9 FAMILY MEMBER; 1.
DR   Pfam; PF00930; DPPIV_N; 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.
DR   PROSITE; PS00708; PRO_ENDOPEP_SER; 1.
PE   4: Predicted;
KW   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036014}.
FT   DOMAIN          229..396
FT                   /note="Dipeptidylpeptidase IV N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00930"
FT   DOMAIN          495..691
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
SQ   SEQUENCE   694 AA;  75503 MW;  98354598BD5B7C30 CRC64;
     MNKAAIILLS LILFSVCGFC QPFPIKSVLS YPFPSQLVSS PSGSKIAWAV NEQGKRNIYT
     ATAPDYQVMK LTSYNEDDGQ ELTSLSVSDD GKWIVFVRGG DHGGRDGGPV NAGSSPVAPK
     MQVLSIPFAG GKTITIGEGD YPVIAPNSKD LIFSSGGQIK IAAIDGSSPA KNLFYAKGNN
     SGYKWSPDGT KIVFVSNRTD HSFIGIYKDQ STPVQWLLPS FARDHSPAWS PDGSEITFIR
     TQGLGRETDS ILAKKHQPWA IWTANVITGE GKQIWKAPTT IKGSYPSIEG GANLAWAAGR
     IIFSSYEDGW PHLYSMDSKG RNRLLLTPGN FVVDNVKLTQ DKKTIIFAAN TGKDKDDLDR
     RHICKVSVDK GDMKPLSGGL GIEAYPVIAG DGEQVYCLSA TAQRPLLPAV LQDGGKIRLI
     GEELIPADFP LKHMVIPKHI SFRAADGQLV YGQLFSPKNP LKSHPAILYV HGGPQRQMYL
     GWSPMDYYSI DYGLNQYLVS LGFTVLSVNY RLGLGYGYDF HKPLNAGAQG ASEYQDIKAA
     GEWLSAQAHV DPKRVGIYGG SYGGYLTALA LGRDSKLFAA GVDIHGVNNR FSANTAEAKA
     PAPDATLAAK IAQESSPVSY LKTWTSPTLI IHADDDRNVS FSQSVDLAKR FEDKNFEFES
     LVIPDDTHHW MKFSNGVKVS EATAEFLKRK LFGN
//
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