ID   PEPX_RHOBA              Reviewed;         626 AA.
AC   P59825;
DT   22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2003, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Putative Xaa-Pro dipeptidyl-peptidase;
DE            Short=X-Pro dipeptidyl-peptidase;
DE            EC=3.4.14.11;
DE   AltName: Full=X-prolyl-dipeptidyl aminopeptidase;
DE            Short=X-PDAP;
GN   OrderedLocusNames=RB9674;
OS   Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC   Bacteria; Planctomycetes; Planctomycetia; Pirellulales; Pirellulaceae;
OC   Rhodopirellula.
OX   NCBI_TaxID=243090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10527 / NCIMB 13988 / SH1;
RX   PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA   Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA   Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA   Reinhardt R.;
RT   "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT   1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
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   -!- SIMILARITY: Belongs to the peptidase S15 family. {ECO:0000305}.
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DR   EMBL; BX294150; CAD76400.1; -; Genomic_DNA.
DR   RefSeq; NP_869015.1; NC_005027.1.
DR   AlphaFoldDB; P59825; -.
DR   SMR; P59825; -.
DR   STRING; 243090.RB9674; -.
DR   ESTHER; rhoba-pepx; Lactobacillus_peptidase.
DR   EnsemblBacteria; CAD76400; CAD76400; RB9674.
DR   KEGG; rba:RB9674; -.
DR   PATRIC; fig|243090.15.peg.4652; -.
DR   eggNOG; COG2936; Bacteria.
DR   HOGENOM; CLU_011800_1_0_0; -.
DR   InParanoid; P59825; -.
DR   OMA; LYTASPY; -.
DR   OrthoDB; 327988at2; -.
DR   Proteomes; UP000001025; Chromosome.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008239; F:dipeptidyl-peptidase activity; IEA:UniProtKB-EC.
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; -; 2.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR005674; CocE/Ser_esterase.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR008252; Pept_S15_Xpro.
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   PRINTS; PR00923; LACTOPTASE.
DR   SMART; SM00939; PepX_C; 1.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   TIGRFAMs; TIGR00976; NonD; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase; Hydrolase; Protease; Reference proteome; Serine protease.
FT   CHAIN           1..626
FT                   /note="Putative Xaa-Pro dipeptidyl-peptidase"
FT                   /id="PRO_0000220238"
FT   ACT_SITE        231
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        348
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        379
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   626 AA;  70020 MW;  5A28A963A5665B45 CRC64;
     MTKLVRSRLD LTWVFTTMKR LRLPVLAVLF LAISPVQGGE IQIPVIKDGE AQVIKELEDS
     DYWIRHDLWV ETEFDLDGDG KLDRMHVSVT RPTQTDTQSL KLPVIYNSSP YFAGTTGGDE
     SYFWDARQEL GDEPPKRSAA PAIEREGTRP IISKRHVKDW LPRGFVVVHS SAPGTGLSQG
     CPTVGDDPEA LAPKAVIDWL CGRAKGFTEP FGGEPVEAYW SSGKVGMTGT SYNGTIPLAA
     ATTGVEGLEV IIPVAPNTSY YHYYRSNGLV RHPGGYLGED IDILYDFIHS GGDEETRAYC
     DCHIRDEQMM ANQDRATGDY NDFWYSRDYL NRVDGVKAAV LMAHAFNDWN VVPEHSIRIY
     EALKKNGVET QLFMHQGGHG GPPPISMMNR WFTHYLYGED NGVEKGSKSW IVREKDERTK
     PTEYPQYPHP EAKDVVVYPV PGAPQRGRLQ TAPLTEPITE TLVDNFSFAG ETLAQAEYTE
     HRLIYTTPEL SEAVHLSGTP RIKLRLACDR PAANLSVWLV SLPWNTQKNS KITDNIITRG
     WADPQNIESM RESKPLVPGQ FYDIEFDLQP DDQVIAKGQQ IGLMVFSSDR DYTLHPTPGT
     KLTIDLQHTQ LSLPVVGGTI PLESQD