ID A0A1V1UZA6_9CAUL Unreviewed; 697 AA.
AC A0A1V1UZA6;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Dipeptidyl-peptidase {ECO:0000256|RuleBase:RU366067};
DE EC=3.4.14.- {ECO:0000256|RuleBase:RU366067};
GN ORFNames=SH203_01611 {ECO:0000313|EMBL:GAW41207.1};
OS Brevundimonas sp. SH203.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Brevundimonas.
OX NCBI_TaxID=345167 {ECO:0000313|EMBL:GAW41207.1, ECO:0000313|Proteomes:UP000195546};
RN [1] {ECO:0000313|EMBL:GAW41207.1, ECO:0000313|Proteomes:UP000195546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH203 {ECO:0000313|EMBL:GAW41207.1,
RC ECO:0000313|Proteomes:UP000195546};
RA Suzuki T., Kikuchi M., Habu N., Konno N.;
RT "Draft Genome Sequence of Brevundimonas sp. SH203, producing Cellouronate
RT (beta-1,4-linked polyglucuronate) lyase.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the removal of dipeptides from the N-terminus of
CC oligopeptides. {ECO:0000256|RuleBase:RU366067}.
CC -!- SIMILARITY: Belongs to the peptidase S46 family.
CC {ECO:0000256|ARBA:ARBA00010491, ECO:0000256|RuleBase:RU366067}.
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:GAW41207.1}.
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DR EMBL; BDMM01000003; GAW41207.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V1UZA6; -.
DR OrthoDB; 9805367at2; -.
DR Proteomes; UP000195546; Unassembled WGS sequence.
DR GO; GO:0008239; F:dipeptidyl-peptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0070009; F:serine-type aminopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043171; P:peptide catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR019500; Pep_S46.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR PANTHER; PTHR38469; -; 1.
DR PANTHER; PTHR38469:SF1; PERIPLASMIC PEPTIDASE SUBFAMILY S1B; 1.
DR Pfam; PF10459; Peptidase_S46; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000256|RuleBase:RU366067}; Hydrolase {ECO:0000256|RuleBase:RU366067};
KW Protease {ECO:0000256|RuleBase:RU366067};
KW Reference proteome {ECO:0000313|Proteomes:UP000195546};
KW Serine protease {ECO:0000256|RuleBase:RU366067};
KW Signal {ECO:0000256|RuleBase:RU366067}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|RuleBase:RU366067"
FT CHAIN 32..697
FT /note="Dipeptidyl-peptidase"
FT /evidence="ECO:0000256|RuleBase:RU366067"
FT /id="PRO_5023084637"
SQ SEQUENCE 697 AA; 76148 MW; B85EDDAA6F4E94DA CRC64;
MSLPSLRLTA SLAALGAATA VLSAPASPAR ADEGMWTFDN FPIATVNQKY GTNIDQAWLD
RVRNAAVRLQ GCSASLVSAE GLVLTNHHCV VSCVQDLSTA QNDYVKNGWM PGSREEEKKC
PGQTAEILTD IVDVTDRVTG AGAGLEGAAF VQARAAEIDK IQKETCGDDQ KLTCQVISFY
RGGQYKLYKF RKYDDVRLVF APEFQAAFFG GDPDNFNFPR YALDAGFLRL YEDGKPVATP
NHLTWNPNAP KEGDVTFVAG NPGSTQRLLT VAQLEVLRDQ QMPLTLIQSS ELRGRLIEYS
TTGEEAKRVT VDPLFGLENS FKVFYGQEGA LTDPSFMATK RREEQELRQR VAAAPALAQR
IGDPWADLER VSTAQRDLYL PYRQLESAAG QRSQLYSYAK AIVRAAKERA KPVAERRAGY
SDADIASLGR RLATETPIST DLEKIFLDFW LSKTREYLTV DNANVKALLG KESPEQVAAR
LIDGTRLADP AFRAQALAMT PEQLAASGDP LIQFVLANDD AAQAIRTQWE SAVSGPTSRA
GEKIAQARFA VYGANLYPDA TFSLRLSYGQ VKGWTYRGVT VEPFTHIGGL YERNTGAEPF
NAATDWLAAE NKVDKATVYD FVSTNDIIGG NSGSPVINAK GEVIGAAFDG NIHSLGGSFG
YDPELNRTVT VSTAAITEAL RNVYNQPRLL RELGVRR
//
