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Database: UniProt
Entry: G5SLU3_9BACT
LinkDB: G5SLU3_9BACT
Original site: G5SLU3_9BACT 
ID   G5SLU3_9BACT            Unreviewed;       721 AA.
AC   G5SLU3;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, 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   ORFNames=HMPREF9441_00315 {ECO:0000313|EMBL:EHH01859.1};
OS   Paraprevotella clara YIT 11840.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Paraprevotella.
OX   NCBI_TaxID=762968 {ECO:0000313|EMBL:EHH01859.1, ECO:0000313|Proteomes:UP000003598};
RN   [1] {ECO:0000313|EMBL:EHH01859.1, ECO:0000313|Proteomes:UP000003598}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIT 11840 {ECO:0000313|EMBL:EHH01859.1,
RC   ECO:0000313|Proteomes:UP000003598};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (MAR-2011) 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:EHH01859.1}.
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DR   EMBL; AFFY01000003; EHH01859.1; -; Genomic_DNA.
DR   RefSeq; WP_008617136.1; NZ_JH376579.1.
DR   AlphaFoldDB; G5SLU3; -.
DR   STRING; 762968.HMPREF9441_00315; -.
DR   MEROPS; S46.001; -.
DR   GeneID; 78581597; -.
DR   PATRIC; fig|762968.3.peg.281; -.
DR   eggNOG; COG0265; Bacteria.
DR   HOGENOM; CLU_013776_0_0_10; -.
DR   OrthoDB; 9805367at2; -.
DR   Proteomes; UP000003598; 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   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}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000256|RuleBase:RU366067};
KW   Protease {ECO:0000256|RuleBase:RU366067};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW   ECO:0000256|RuleBase:RU366067}.
FT   COILED          350..383
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   721 AA;  82439 MW;  D89FB8CD32ED32C4 CRC64;
     MKKKFLTLLA FVCGLNGIKA DEGMWMLSHI SPKSMKVMKD LGLQMSEKEL YNTKGTSLKD
     AVVSFGGFCS GVVVSPDGLV FTNHHCGFGN IQALATPEND ILKNGFVAHT QAEELPAKGL
     YVQILQRTED ITKRVNKALD KYYKEHAAEM AQLGENAKEK MRWNSVDSIC LAIENEYAKK
     YPELICEVSP YYTGNAFYVN VYKQYDDIRL VFAPPQSLGK FGGETDNWMW PRQTCDFSVF
     RIYADKDNQP AEYSADNRPL KAERYAKVSL EGFKKGDYCM TIGYPGRTNR YLSSYGIVER
     MENTNESRIN VRGVKQGIWK KWMDSDPKIR LQYASKYANS SNYWKNSIGM NKALKELKVV
     EQKKKQEQQI NEWAQKSKKR QERFGNLAPE LEKAYAARKD GNRAIAFLNE SFLGGPDLMR
     IAFYFDNLQN AGGETGKATW KNRLRQQYKD WNEEVDKETM TALIDNYAKQ VKPEYLPDFY
     QTIEKEYNND IRTYVDAMFK QSVLTDTNCV NLTLTQEQKD NDMALKCLKS VMELGGKVSD
     QISQYNMDVA EKERLLCEAI LEMEMDQPHY SDANSTMRLS YGFVDDYTSA AGHQNYFTTM
     PSLLDKVKQS DRIDEYKVEP EVKALFEKGE FGPYKDKESG EMQLCFLTNN DITGGNSGSP
     MFNGKGELIG LAFDGNWDAL SSDITFTQDL TRCIGVDIRY VLYIIDRWGK AERLIQEIGA
     R
//
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