ID B0TSY2_SHEHH Unreviewed; 718 AA.
AC B0TSY2;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Dipeptidyl-peptidase {ECO:0000256|RuleBase:RU366067};
DE EC=3.4.14.- {ECO:0000256|RuleBase:RU366067};
GN OrderedLocusNames=Shal_0732 {ECO:0000313|EMBL:ABZ75307.1};
OS Shewanella halifaxensis (strain HAW-EB4).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=458817 {ECO:0000313|EMBL:ABZ75307.1, ECO:0000313|Proteomes:UP000001317};
RN [1] {ECO:0000313|EMBL:ABZ75307.1, ECO:0000313|Proteomes:UP000001317}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HAW-EB4 {ECO:0000313|EMBL:ABZ75307.1,
RC ECO:0000313|Proteomes:UP000001317};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Kim E., Zhao J.-S., Richardson P.;
RT "Complete sequence of Shewanella halifaxensis HAW-EB4.";
RL Submitted (JAN-2008) 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; CP000931; ABZ75307.1; -; Genomic_DNA.
DR RefSeq; WP_012275861.1; NC_010334.1.
DR AlphaFoldDB; B0TSY2; -.
DR STRING; 458817.Shal_0732; -.
DR MEROPS; S46.003; -.
DR KEGG; shl:Shal_0732; -.
DR eggNOG; COG3591; Bacteria.
DR HOGENOM; CLU_013776_0_0_6; -.
DR OrthoDB; 9805367at2; -.
DR Proteomes; UP000001317; 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 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..18
FT /evidence="ECO:0000256|RuleBase:RU366067"
FT CHAIN 19..718
FT /note="Dipeptidyl-peptidase"
FT /evidence="ECO:0000256|RuleBase:RU366067"
FT /id="PRO_5023100676"
SQ SEQUENCE 718 AA; 80975 MW; 0DF136F5AE245057 CRC64;
MKKWLLTAAI ATSFGAVADE GMWQPHQLPA MADELKAKGL EIDVNSISKL TEFPMNAVIS
LGGCTASFVS PKGLVVTNHH CAYGSIQYNS TPENNLLRDG FLAKTFADEL PATPGSRVYV
TESVVDVTDK VKDGLENKIG NAFYKGVEQK EKGLVAECEK EDGYRCKVYS FHGGLEYYLV
KQLEIRDVRL VYNPAASVGK YGGDVDNWMW PRHTGDYSFY RAYVSKDGKP ADFSKDNVPF
EPKSFLKVSA KGVSEGDFVM VAGYPGRTNR YRTAYEVENQ FEWSYPEGKV LRERLIEIIK
ETAPEGSDER IKYESSIAGL ANYAKNFTSM IEFYGKSTML DDRKALEQKL ANWINADSKR
KQQYGKVLAE LDKLIAKSQQ DQERDLLLGY MGYSTMMSTA NRLYRLANEK ALPDMEREPG
YQDRDMTRFT SGMERIERRY AASVDKAMLA DLITRYAALP KDQRLPAFDK AFGITDNFDA
AKLNKTLDKM YANTSLSDKE VRLAWMEKSV VEFNNSKDPF IQYAVATYDE RMKREKEKKQ
LAGELMKVRP MYMDAIIAYN RELGKPVYAD ANSSLRVTVG HVKGYSPEDG LYAEPFTRLE
GILAKDTGVE PFNAPAKELE LIANKQYGDY YVKSLDSVPV NFLSTLDTTG GNSGSPTLNG
RAELVGLLFD GVYESIIGDW GYDTETNRSI QVDSRYMLWV MKYLDNADNL LEEMEIVN
//
