PEPX_STRP1
ID PEPX_STRP1 Reviewed; 760 AA.
AC Q99Y58; Q48WT0;
DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 136.
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=SPy_1858, M5005_Spy1577;
OS Streptococcus pyogenes serotype M1.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=301447;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700294 / SF370 / Serotype M1;
RX PubMed=11296296; DOI=10.1073/pnas.071559398;
RA Ferretti J.J., McShan W.M., Ajdic D.J., Savic D.J., Savic G., Lyon K.,
RA Primeaux C., Sezate S., Suvorov A.N., Kenton S., Lai H.S., Lin S.P.,
RA Qian Y., Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L., White J., Yuan X.,
RA Clifton S.W., Roe B.A., McLaughlin R.E.;
RT "Complete genome sequence of an M1 strain of Streptococcus pyogenes.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4658-4663(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-947 / MGAS5005 / Serotype M1;
RX PubMed=16088826; DOI=10.1086/432514;
RA Sumby P., Porcella S.F., Madrigal A.G., Barbian K.D., Virtaneva K.,
RA Ricklefs S.M., Sturdevant D.E., Graham M.R., Vuopio-Varkila J., Hoe N.P.,
RA Musser J.M.;
RT "Evolutionary origin and emergence of a highly successful clone of serotype
RT M1 group A Streptococcus involved multiple horizontal gene transfer
RT events.";
RL J. Infect. Dis. 192:771-782(2005).
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; AE004092; AAK34574.1; -; Genomic_DNA.
DR EMBL; CP000017; AAZ52195.1; -; Genomic_DNA.
DR RefSeq; NP_269853.1; NC_002737.2.
DR AlphaFoldDB; Q99Y58; -.
DR SMR; Q99Y58; -.
DR STRING; 1314.HKU360_01698; -.
DR ESTHER; strpy-PEPXP; Lactobacillus_peptidase.
DR PaxDb; Q99Y58; -.
DR EnsemblBacteria; AAK34574; AAK34574; SPy_1858.
DR KEGG; spy:SPy_1858; -.
DR KEGG; spz:M5005_Spy1577; -.
DR PATRIC; fig|160490.10.peg.1612; -.
DR HOGENOM; CLU_011800_0_0_9; -.
DR OMA; LYTASPY; -.
DR Proteomes; UP000000750; 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; Reference proteome;
KW Serine protease.
FT CHAIN 1..760
FT /note="Xaa-Pro dipeptidyl-peptidase"
FT /id="PRO_0000220231"
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"
FT CONFLICT 198
FT /note="Q -> P (in Ref. 2; AAZ52195)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 760 AA; 86738 MW; CEDD166D156053A0 CRC64;
MRYNQFSYIP TSLERAAEEL KELGFDLDLQ KTAKASLESF 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
TSGNYAQIES FKAVIDWLNG RATAYTSHSK THQVRADWAN GLVCTTGKSY LGTMSTGLAT
TGVDGLAMII AESAISSWYN YYRENGLVCS PGGYPGEDLD VLTELTYSRN LLAGDYLRHN
DRYQELLNQQ SQALDRQSGD YNQFWHDRNY LKNAHQIKCD VVYTHGLQDW NVKPRQVYEI
FNALPSTINK HLFLHQGEHV YMHNWQSIDF RESMNALLCQ KLLGLANDFS LPEMIWQDNT
CPQNWQERKV FGTSTIKELD LGQELLLIDN HYGEDEFKAY GKDFRAFKAA LFKGKANQAL
IDILLEEDLP INGEIVLQLK VKSSENKGLL SAQILDYGKK KRLGDLPIAL TQSSIDNGQN
FSREPLKELP FREDSYRVIS KGFMNLQNRN NLSSIETIPN NKWMTVRLPL QPTIYHLEKG
DTLRVILYTT DFEHTVRDNS NYALTIDLSQ SQLIVPIASN
