ID B8J5F7_ANAD2 Unreviewed; 706 AA.
AC B8J5F7;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Dipeptidyl-peptidase {ECO:0000256|RuleBase:RU366067};
DE EC=3.4.14.- {ECO:0000256|RuleBase:RU366067};
DE Flags: Precursor;
GN OrderedLocusNames=A2cp1_3489 {ECO:0000313|EMBL:ACL66819.1};
OS Anaeromyxobacter dehalogenans (strain 2CP-1 / ATCC BAA-258).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Anaeromyxobacteraceae; Anaeromyxobacter.
OX NCBI_TaxID=455488 {ECO:0000313|EMBL:ACL66819.1, ECO:0000313|Proteomes:UP000007089};
RN [1] {ECO:0000313|Proteomes:UP000007089}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2CP-1 / ATCC BAA-258 {ECO:0000313|Proteomes:UP000007089};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA Beliaev A.S., Richardson P.;
RT "Complete sequence of Anaeromyxobacter dehalogenans 2CP-1.";
RL Submitted (JAN-2009) 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; CP001359; ACL66819.1; -; Genomic_DNA.
DR RefSeq; WP_015934616.1; NC_011891.1.
DR AlphaFoldDB; B8J5F7; -.
DR KEGG; acp:A2cp1_3489; -.
DR HOGENOM; CLU_013776_0_0_7; -.
DR Proteomes; UP000007089; 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 Serine protease {ECO:0000256|RuleBase:RU366067};
KW Signal {ECO:0000256|RuleBase:RU366067}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|RuleBase:RU366067"
FT CHAIN 19..706
FT /note="Dipeptidyl-peptidase"
FT /evidence="ECO:0000256|RuleBase:RU366067"
FT /id="PRO_5023159019"
SQ SEQUENCE 706 AA; 76700 MW; CFF04C4EC8B88D15 CRC64;
MKRLLLALLL ASPLAGRADE GMWTYDAFPS DRVARKYGFD PSTAWLDRAR LASARLARGC
SASFVSDGGL VMTNHHCVHE CVEELSSAGK DLVATGFLAR TGADELRCPA MQVDQLLRIT
DVTKRVHGAL AGLQGARFNA ALYAQKAAIE KECQGTDPGL RCELVELYHG GVYSLYQYRR
YDDVRLVFAP EFAIAFFGGD PDNFMFPRYD LDVAFIRVYQ GGKPARTADH FTWSPAGAPA
GALTFVSGNP GKTERLLTVA QLAYVRDHAL PDALERLAEE RGLLTGFQLT GPEAKRVSTS
RLFYNENSVK ARRGQLAALR DPAFFATKVA EENKLRAALR RDPAKARKYL PAWDRIAAAQ
VRALSLEIPY DWLELLPSGR SRIGGDLFWM ARHLVRAADE RRKPDGERLK EYRDTALPSL
ADSVTSTAPI DAAYETVRLG FWLEKVRERL GTDHAAVKHA LGSASPAEVA RKVVAGTALR
DPAVRKALWE GGAAAVDASK DPLLALARAA DADARAVRKQ WEDEVDSVEI QNQALIAQAR
FAVYGRSIYP DATFSPRLSY GQVKGWKQDG REVAPFTTFA GAFERHTGSE PYALPKSWLD
AKPRLDLATP LDFVTDNDII GGNSGSPVFD RDLRIVGLAF DGNLASLGGD YGFDDSANRA
VAVHSSAIVH ALARIYGADR LVSELGAAPA GAAGAAPPPG ATRSTK
//
