ID L0DB69_SINAD Unreviewed; 696 AA.
AC L0DB69;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Dipeptidyl-peptidase {ECO:0000256|RuleBase:RU366067};
DE EC=3.4.14.- {ECO:0000256|RuleBase:RU366067};
GN OrderedLocusNames=Sinac_1501 {ECO:0000313|EMBL:AGA25881.1};
OS Singulisphaera acidiphila (strain ATCC BAA-1392 / DSM 18658 / VKM B-2454 /
OS MOB10).
OC Bacteria; Planctomycetota; Planctomycetia; Isosphaerales; Isosphaeraceae;
OC Singulisphaera.
OX NCBI_TaxID=886293 {ECO:0000313|EMBL:AGA25881.1, ECO:0000313|Proteomes:UP000010798};
RN [1] {ECO:0000313|EMBL:AGA25881.1, ECO:0000313|Proteomes:UP000010798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1392 / DSM 18658 / VKM B-2454 / MOB10
RC {ECO:0000313|Proteomes:UP000010798};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Chertkov O.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Tindall B., Pomrenke H., Brambilla E., Klenk H.-P.,
RA Eisen J.A.;
RT "Complete sequence of chromosome of Singulisphaera acidiphila DSM 18658.";
RL Submitted (FEB-2012) 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; CP003364; AGA25881.1; -; Genomic_DNA.
DR RefSeq; WP_015245051.1; NZ_JH621477.1.
DR AlphaFoldDB; L0DB69; -.
DR STRING; 886293.Sinac_1501; -.
DR KEGG; saci:Sinac_1501; -.
DR eggNOG; COG3591; Bacteria.
DR HOGENOM; CLU_013776_0_0_0; -.
DR OrthoDB; 9805367at2; -.
DR Proteomes; UP000010798; 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:UP000010798};
KW Serine protease {ECO:0000256|RuleBase:RU366067};
KW Signal {ECO:0000256|RuleBase:RU366067}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|RuleBase:RU366067"
FT CHAIN 25..696
FT /note="Dipeptidyl-peptidase"
FT /evidence="ECO:0000256|RuleBase:RU366067"
FT /id="PRO_5023153613"
SQ SEQUENCE 696 AA; 77038 MW; 09A3CB8911066CB5 CRC64;
MSARQRILAL SVISVLSMGG AVFADEGMWV FDNLPLKALK QRYNFEPTPG WVERLRSSAV
RFNSGGSGSF VSADGLVMTN HHVGADMLQK ISTAGKNYHK EGFLAKTRAD EIKAPDLELN
VLVDIQDVTD RVLAAVKPGM GDSEAGTAKR KAMATIEKES LDKSGLRSDV VTLYQGGKYA
LYTYKKYTDV RLVFAPEFDI AFFGGDPDNF EFPRYDLDVC FFRAYENDKP AQPKHYLNWS
AAGSKDGDLI FVAGHPGKTS RLNTVAHLEY LRDVSFPFSL EILHDREAFL QEYGKKGPEQ
ARQAMDELFG YQNSRKARAG GLKGLKDEAL MARKREAENA LRERIKADHA AQVAYGSAWD
KIATAHQVST KIAKRYNFLE RGFAFDSSLF HIARTLVRLA QEQEKPNADR LREFRESAIE
SLQLALFSDA PIYPEFEEAK LAHSLAFWKK WMGDIDPLVA RVLHGRTPEE VAKDFVQGTK
LTDVSVRRDL AKGGLKALLE VDDPMIKLAL AVDADARTLR TQYEDEVEAV LSAQYAGIAK
ATFEAQGDSV YPDATFTLRL AFGTVKGYEA GGKVIPPYTT IGGAFQHADA HGNTPPYVLP
LSWHQAKKEG RLNLETAMNF VSTADIIGGN SGSPVVNRDN EVVGLIFDGN VDSLVLDFAF
DDRSARAISV DSRAIYEALK SVYHADDLAK ELMDKP
//