ID A0A0G3X924_9SPHN Unreviewed; 683 AA.
AC A0A0G3X924;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Dipeptidyl-peptidase {ECO:0000256|RuleBase:RU366067};
DE EC=3.4.14.- {ECO:0000256|RuleBase:RU366067};
DE Flags: Precursor;
GN ORFNames=AM2010_1958 {ECO:0000313|EMBL:AKM08020.1};
OS Pelagerythrobacter marensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Pelagerythrobacter.
OX NCBI_TaxID=543877 {ECO:0000313|EMBL:AKM08020.1, ECO:0000313|Proteomes:UP000037643};
RN [1] {ECO:0000313|EMBL:AKM08020.1, ECO:0000313|Proteomes:UP000037643}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 22370 {ECO:0000313|EMBL:AKM08020.1,
RC ECO:0000313|Proteomes:UP000037643};
RA Kim K.M.;
RL Submitted (JUN-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}.
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DR EMBL; CP011805; AKM08020.1; -; Genomic_DNA.
DR RefSeq; WP_047806914.1; NZ_LMVG01000004.1.
DR AlphaFoldDB; A0A0G3X924; -.
DR STRING; 543877.AM2010_1958; -.
DR KEGG; amx:AM2010_1958; -.
DR PATRIC; fig|543877.4.peg.1987; -.
DR OrthoDB; 9805367at2; -.
DR Proteomes; UP000037643; 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; 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:UP000037643};
KW Serine protease {ECO:0000256|RuleBase:RU366067};
KW Signal {ECO:0000256|RuleBase:RU366067}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|RuleBase:RU366067"
FT CHAIN 21..683
FT /note="Dipeptidyl-peptidase"
FT /evidence="ECO:0000256|RuleBase:RU366067"
FT /id="PRO_5023154734"
SQ SEQUENCE 683 AA; 73449 MW; AE8863AD5A6497C4 CRC64;
MTTRTALLAA ASFAAIPLLA APAAADEGMW TFDGFPADQV RESYGWAPDQ AWLDEVRNSS
VRLTGGCSAS FVSPEGLILT NHHCIASCLY DNSTDAKDYL ADGFTARQRE DELTCPGQQA
EVVTAISDVT GDVMGAIGNL SGEALTKARD AKIAEIESAN CTDTETTRCQ VVTLFGGGQY
KLYTYRKYSD VRLAWAPEAR AATFGGDPDN FNFPRYSLDA SFLRAYEDGQ PVSNPAHLKW
NPRAPEEGEI TFVVGNPGST SRLFTQSQLA FEREVRLPLT LATLSELRGR LIRAMDESPE
HAREGQDLLS GVENSLKVYI GRTRALNDPA FTGKLAAAEA DLKAKSADNG DIGDPWGAVE
EAVSAYRALY LPLRFTQPSG DLYGYAQTLV FAAQERAKPN AQRLPGYTDS ALPLTGKRLL
DERPVYPWLD EMTMEWSLSK AREYLGVDDS DSKLLLGSES PEQRAARLVN GTKLADPAVR
KALWDGGLEA IEASDDPMIR YALALAPRQR ELKALSDAQY SGPLAAAGAS LADARFAAYG
DALYPDATFT LRISYGQVKG WTERGNAVPI RTTMGGTFDR ATGNPPFDLP PAFAANEARI
DKDTTYDFVT TNDIIGGNSG SPVIDRAGTV IGAAFDGNIH SLGGNYGYDG TLNRTVAVST
AAVQEALETI YPAPALVAEL AGE
//
