ID A0A127MCF8_9SPHN Unreviewed; 683 AA.
AC A0A127MCF8;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Dipeptidyl-peptidase {ECO:0000256|RuleBase:RU366067};
DE EC=3.4.14.- {ECO:0000256|RuleBase:RU366067};
GN ORFNames=AZE99_02835 {ECO:0000313|EMBL:AMO70929.1};
OS Sphingorhabdus sp. M41.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingorhabdus.
OX NCBI_TaxID=1806885 {ECO:0000313|EMBL:AMO70929.1, ECO:0000313|Proteomes:UP000073959};
RN [1] {ECO:0000313|EMBL:AMO70929.1, ECO:0000313|Proteomes:UP000073959}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M41 {ECO:0000313|EMBL:AMO70929.1,
RC ECO:0000313|Proteomes:UP000073959};
RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL Submitted (DEC-2015) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP014545; AMO70929.1; -; Genomic_DNA.
DR RefSeq; WP_067197921.1; NZ_CP014545.1.
DR AlphaFoldDB; A0A127MCF8; -.
DR STRING; 1806885.AZE99_02835; -.
DR KEGG; sphg:AZE99_02835; -.
DR OrthoDB; 9805367at2; -.
DR Proteomes; UP000073959; Chromosome.
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; DIPEPTIDYL-PEPTIDASE; 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 Serine protease {ECO:0000256|RuleBase:RU366067};
KW Signal {ECO:0000256|RuleBase:RU366067}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|RuleBase:RU366067"
FT CHAIN 26..683
FT /note="Dipeptidyl-peptidase"
FT /evidence="ECO:0000256|RuleBase:RU366067"
FT /id="PRO_5023106284"
SQ SEQUENCE 683 AA; 74075 MW; 4AE20DFB64A1B9D4 CRC64;
MTQRSVYLAT GMICLFGAAA SPAYAEEGMW TFGAFPTEQM REAYGWAPDK AWLDRVQAAS
VRLTGGCSAS FVSSQGLILT NHHCVASCLY QNSDDDNDFL KNGFTAGNRA EEKKCAGQQA
EVVTMISDVT ADITAAIGNL SGEALTKARD AKIAAIESAG CPDTDTTRCQ VVTLFGGGQY
KLYSYRKYSD VRLAWSPEDR AATFGGDPDN FNFPRYSLDA SFLRAYENGK PVATPAHLKW
NPRAPKEGEL TFVVGNPGST SRLYTQSQLA FEREVRLPVT VATMSELRGR LIRAMEESPE
KNREGLDLLG GIENSLKVYI GRTKALNDPA FTAKLAKAEA DLKAKSAGND AIGDPWADVD
AAMQAYRSYY LPARFTDPTG DLYNYAQVLV LAAIESAKPN AERLPGFTDS ALPLTKKRLL
DERPIYPWLD ELKFGWSLSK AREYLGPDDS DTKLLLGKES PEQLAERLVA GTGLADPKMR
QKLWDGGLAA IEASDDPMIL YARKLEARQR ELKQQIDENY AGPLTNAGAK LADARFAAYG
DKLYPDATFT LRISYGQVKG WMERGNQVPI ATTLGGTFDR ATGNEPFDLA PAFVANKDKI
DPSITYDFVS TNDIIGGNSG SPVIDKAGTV IGAAFDGNIH SLGGNYGYDP ALNRTVSVSV
AAVQEALETI YPAPNLVKEL AGK
//