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
//