PEPX_STRP3
ID PEPX_STRP3 Reviewed; 760 AA.
AC P0DD36; Q8K5X7;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Xaa-Pro dipeptidyl-peptidase {ECO:0000255|HAMAP-Rule:MF_00698};
DE EC=3.4.14.11 {ECO:0000255|HAMAP-Rule:MF_00698};
DE AltName: Full=X-Pro dipeptidyl-peptidase {ECO:0000255|HAMAP-Rule:MF_00698};
DE AltName: Full=X-prolyl-dipeptidyl aminopeptidase {ECO:0000255|HAMAP-Rule:MF_00698};
DE Short=X-PDAP {ECO:0000255|HAMAP-Rule:MF_00698};
GN Name=pepX {ECO:0000255|HAMAP-Rule:MF_00698}; Synonyms=pepXP;
GN OrderedLocusNames=SpyM3_1603;
OS Streptococcus pyogenes serotype M3 (strain ATCC BAA-595 / MGAS315).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=198466;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-595 / MGAS315;
RX PubMed=12122206; DOI=10.1073/pnas.152298499;
RA Beres S.B., Sylva G.L., Barbian K.D., Lei B., Hoff J.S., Mammarella N.D.,
RA Liu M.-Y., Smoot J.C., Porcella S.F., Parkins L.D., Campbell D.S.,
RA Smith T.M., McCormick J.K., Leung D.Y.M., Schlievert P.M., Musser J.M.;
RT "Genome sequence of a serotype M3 strain of group A Streptococcus: phage-
RT encoded toxins, the high-virulence phenotype, and clone emergence.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:10078-10083(2002).
CC -!- FUNCTION: Removes N-terminal dipeptides sequentially from polypeptides
CC having unsubstituted N-termini provided that the penultimate residue is
CC proline. {ECO:0000255|HAMAP-Rule:MF_00698}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolyzes Xaa-Pro-|- bonds to release unblocked, N-terminal
CC dipeptides from substrates including Ala-Pro-|-p-nitroanilide and
CC (sequentially) Tyr-Pro-|-Phe-Pro-|-Gly-Pro-|-Ile.; EC=3.4.14.11;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00698};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00698}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00698}.
CC -!- SIMILARITY: Belongs to the peptidase S15 family. {ECO:0000255|HAMAP-
CC Rule:MF_00698}.
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DR EMBL; AE014074; AAM80210.1; -; Genomic_DNA.
DR RefSeq; WP_011054979.1; NC_004070.1.
DR AlphaFoldDB; P0DD36; -.
DR SMR; P0DD36; -.
DR EnsemblBacteria; AAM80210; AAM80210; SpyM3_1603.
DR KEGG; spg:SpyM3_1603; -.
DR HOGENOM; CLU_011800_0_0_9; -.
DR OMA; LYTASPY; -.
DR Proteomes; UP000000564; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008239; F:dipeptidyl-peptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR HAMAP; MF_00698; Aminopeptidase_S15; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR008252; Pept_S15_Xpro.
DR InterPro; IPR015251; PepX_N_dom.
DR InterPro; IPR036313; PepX_N_dom_sf.
DR InterPro; IPR000383; Xaa-Pro-like_dom.
DR InterPro; IPR013736; Xaa-Pro_dipept_C.
DR Pfam; PF02129; Peptidase_S15; 1.
DR Pfam; PF08530; PepX_C; 1.
DR Pfam; PF09168; PepX_N; 1.
DR PRINTS; PR00923; LACTOPTASE.
DR SMART; SM00939; PepX_C; 1.
DR SMART; SM00940; PepX_N; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR SUPFAM; SSF81761; SSF81761; 1.
PE 3: Inferred from homology;
KW Aminopeptidase; Cytoplasm; Hydrolase; Protease; Serine protease.
FT CHAIN 1..760
FT /note="Xaa-Pro dipeptidyl-peptidase"
FT /id="PRO_0000220232"
FT ACT_SITE 349
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00698"
FT ACT_SITE 469
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00698"
FT ACT_SITE 499
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00698"
SQ SEQUENCE 760 AA; 86719 MW; B9F9119217A71ACD CRC64;
MRYNQFSYIP TSLERAAEEL KELGFDLDLQ KTAKANLESF LRKLFFHYPD SDYPLSHLIA
KNDMDALSFF QSEQELSKEV FDLLALQVLG FIPGVDFTEA DAFLDKLAFP IHFDETEIIK
HIHHLLATRC KSGMTLIDDL VSQGMLTMDN DYHFFNGKSL ATFDTSQLIR EVVYVEAPLD
TDQDGQLDLI KVNIIRPQSQ KPLPTLMTPS PYHQGINEVA NDKKLYRMEK ELVVKKRRQI
TVEDRDFIPL ETQPCKLPIG QNLESFSYIN SYSLNDYFLA RGFANIYVSG VGTAGSTGFM
TSGDYAQIES FKAVIDWLNG RATAYTSHSK THQVRADWAN GLVCTTGKSY LGTMSTGLAT
TGVDGLAMII AESAISSWYN YYRENGLVCS PGGYPGEDLD VLTELTYSRN LLAGDYLRHN
DRYQELLNQQ SQALDRQSGD YNQFWHDRNY LKNAHQIKCD VVYTHGLQDW NVKPRQVYEI
VNALPSTINK HLFLHQGEHV YMHNWQSIDF RESMNALLCQ KLLGLANDFS LPEMIWQDNT
CPQNWQERKV FGTSTIKELD LGQELLLIDN HYGEDEFKAY GKDFRAFKAA LFKGKANQAL
VDILLEEDLL INGEIVLQLK VKSSENKGLL SAQILDYGKK KRLGDLPIAL TQSSIDNGQN
FSREPLKELP FRENSYRVIS KGFMNLQNRN NLSSIETIPN NKWMTVRLPL QPTIYHLEKG
DTLRVILYTT DFEHTVRDNS NYALTIDLSQ SQLIVPIASN