ID A0A0P8BCW0_9SPHN Unreviewed; 712 AA.
AC A0A0P8BCW0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Dipeptidyl-peptidase {ECO:0000256|RuleBase:RU366067};
DE EC=3.4.14.- {ECO:0000256|RuleBase:RU366067};
GN ORFNames=HLUCCX21_03575 {ECO:0000313|EMBL:KPQ31409.1};
OS Porphyrobacter sp. HL-46.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Porphyrobacter.
OX NCBI_TaxID=1479239 {ECO:0000313|EMBL:KPQ31409.1, ECO:0000313|Proteomes:UP000054043};
RN [1] {ECO:0000313|EMBL:KPQ31409.1, ECO:0000313|Proteomes:UP000054043}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HL-46 {ECO:0000313|EMBL:KPQ31409.1};
RA Nelson W.C., Romine M.F., Lindemann S.R.;
RT "Identification and resolution of microdiversity through metagenomic
RT sequencing of parallel consortia.";
RL Submitted (OCT-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 -!- 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:KPQ31409.1}.
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DR EMBL; LLEX01000130; KPQ31409.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P8BCW0; -.
DR STRING; 1479239.GCA_000744895_02155; -.
DR PATRIC; fig|1479239.6.peg.722; -.
DR eggNOG; COG3591; Bacteria.
DR OrthoDB; 9805367at2; -.
DR Proteomes; UP000054043; 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 InterPro; IPR019500; Pep_S46.
DR InterPro; IPR009003; Peptidase_S1_PA.
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..21
FT /evidence="ECO:0000256|RuleBase:RU366067"
FT CHAIN 22..712
FT /note="Dipeptidyl-peptidase"
FT /evidence="ECO:0000256|RuleBase:RU366067"
FT /id="PRO_5023027195"
SQ SEQUENCE 712 AA; 78124 MW; AC186158FED79043 CRC64;
MKKFLLAGAS ALIISAPAAL MAEEGMWLPS QTGAIADEMK AAGLELDAAT LGDLDRPPLT
AIASLGGCSA AFLSPQGLVA TNHHCVAGSL QYNSSPENDY LTDGFLAKTL ADEIPAAPGS
RVYVIEDLRD VTTAMMKGAG ALEGRARYDR LQANRTALIE ACERQANRRC DVRAYFGGQQ
YWLQQQLEIK DVRLAYAPAA GVGNFGGEKD NWMWPRHTGD FAFYRAYVAP DGSSATYAKE
NVPFKPKAWL PIAETGVKEG DFIMVAGFPG TTERLRTAEE ARFYYEELYP YQQKMLTEYG
DRIDALTEGN QAAKIAYAAT LQGVENYEKK IAGQLAGADA ISLIDKKQTE EAAFRAWIAA
DPERQAQYGA ALAELDRLIA EGNAEALADT KRGMLGRSQL YGAARQLYRW ANEQAKPDKD
REPGYQERDR AFMTQGMQRI ERRFVPEIDK ALWEDGIAEY RTLPADQRNE SFDAFMQGRE
LASFYAATGL GDTAKRLEWM DKSVADFKAS DDPFIQLAVA TYDEAMADEA EGKARSGHVQ
KARSQVMEAR LAYAASQGKA MYPDANGSLR FTYGKVTGKT VDGQIWPPFT TAEGIVAKHT
GRGEFDAPDT MIDLIKAKDY GRYVAPELGT LPVDFLSTVD ITNGNSGSST LNARGEFVGL
AFDGTIEGVV SDWMYNPAIN RTIHVDSRFM LWTMDKVDGA QRLLDEMGVA DQ
//
