ID H6L1F6_SAPGL Unreviewed; 711 AA.
AC H6L1F6;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Dipeptidyl-peptidase {ECO:0000256|RuleBase:RU366067};
DE EC=3.4.14.- {ECO:0000256|RuleBase:RU366067};
GN OrderedLocusNames=SGRA_0759 {ECO:0000313|EMBL:AFC23497.1};
OS Saprospira grandis (strain Lewin).
OC Bacteria; Bacteroidota; Saprospiria; Saprospirales; Saprospiraceae;
OC Saprospira.
OX NCBI_TaxID=984262 {ECO:0000313|EMBL:AFC23497.1, ECO:0000313|Proteomes:UP000007519};
RN [1] {ECO:0000313|EMBL:AFC23497.1, ECO:0000313|Proteomes:UP000007519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lewin {ECO:0000313|EMBL:AFC23497.1,
RC ECO:0000313|Proteomes:UP000007519};
RX PubMed=22675601; DOI=10.4056/sigs.2445005;
RA Saw J.H., Yuryev A., Kanbe M., Hou S., Young A.G., Aizawa S., Alam M.;
RT "Complete genome sequencing and analysis of Saprospira grandis str. Lewin,
RT a predatory marine bacterium.";
RL Stand. Genomic Sci. 6:84-93(2012).
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; CP002831; AFC23497.1; -; Genomic_DNA.
DR RefSeq; WP_014373740.1; NC_016940.1.
DR AlphaFoldDB; H6L1F6; -.
DR STRING; 984262.SGRA_0759; -.
DR MEROPS; S46.002; -.
DR KEGG; sgn:SGRA_0759; -.
DR eggNOG; COG3591; Bacteria.
DR HOGENOM; CLU_013776_0_0_10; -.
DR OrthoDB; 9805367at2; -.
DR Proteomes; UP000007519; 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:UP000007519};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU366067}; Signal {ECO:0000256|RuleBase:RU366067}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|RuleBase:RU366067"
FT CHAIN 21..711
FT /note="Dipeptidyl-peptidase"
FT /evidence="ECO:0000256|RuleBase:RU366067"
FT /id="PRO_5023002255"
SQ SEQUENCE 711 AA; 80983 MW; 7E62B709ADC8D8EB CRC64;
MKKLLAFVVA LLLFMPMSWA GEGMWIPALI DMFYSDMKTY GLKLKPSQIY STNKSSLKDA
IVQFDGGCTA ELVSKQGLLL TNHHCGFDAI QQHSSLENDY LKHGFWAKNR SEELACPWMH
VTFVKEMREV TFDVLKGTTE SMTEEEKAAK VSANIKALEA AAAAEKGYKA KIKPFHKGNV
YYMLTTQDYN DIRLVGAPPS AIGKYGGDTD NWVWPRHTGD FSVFRIYADE DNAPADYSEA
NRPYKPAHFL PISMKDKKEG DFTMVYGFPG RTDQHYSAAK LGFYMQQERP ARIKMRETSL
GIIKPAMNSS DEIRIKYASK QASIANAWKK WIGQLGGLRD LKALDKKAHW EKKYNSRAQI
KEEWTEEFGT VLEDLAKLQE ENQKYEFARA LFIEYFFVGP EFLRFSYGFN NLANRYEELE
AAGKLEAEIA RLKEANTAFF KNYDLGIDQK IYEQLTPLYV NYMDNSLLPD DFAEAWAATG
KAIFADSKLL HEKKVAAILE NFDAKAAAEL AKDPALQLAA SLYSNYLQKV APSYGAFQAQ
EEELMETYVK GALTMFPKQR HWSDANSTLR IAYGKLEGSA PHDGMAYLPY TTIEGVMQKY
QKDHPDFDLP ERFMELYEAK DFGPYTQNGE LWVCFTASNH TTGGNSGSPV IDAKGRLMGI
NFDRSWESTM SDFMFDESRC RNIAVDIRYV LWVIDRYGQA SWLIDEMKLV K
//
