ID   PEPD_BIFLO              Reviewed;         533 AA.
AC   Q8G6Z9;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Dipeptidase {ECO:0000303|PubMed:17601807, ECO:0000312|EMBL:AAN24310.1};
DE            EC=3.4.13.19 {ECO:0000269|PubMed:17601807};
GN   Name=pepD {ECO:0000303|PubMed:17601807, ECO:0000312|EMBL:AAN24310.1};
GN   OrderedLocusNames=BL0479;
OS   Bifidobacterium longum (strain NCC 2705).
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=206672;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCC 2705;
RX   PubMed=12381787; DOI=10.1073/pnas.212527599;
RA   Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G.,
RA   Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.;
RT   "The genome sequence of Bifidobacterium longum reflects its adaptation to
RT   the human gastrointestinal tract.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 231-239 AND 395-405, FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND MASS SPECTROMETRY.
RC   STRAIN=BORI {ECO:0000269|PubMed:17601807};
RX   PubMed=17601807; DOI=10.1128/aem.00642-07;
RA   Seo J.M., Ji G.E., Cho S.H., Park M.S., Lee H.J.;
RT   "Characterization of a Bifidobacterium longum BORI dipeptidase belonging to
RT   the U34 family.";
RL   Appl. Environ. Microbiol. 73:5598-5606(2007).
CC   -!- FUNCTION: Hydrolyzes a wide range of dipeptides. Highest activity
CC       against Ala-Gln. {ECO:0000269|PubMed:17601807}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an L-aminoacyl-L-amino acid + H2O = 2 an L-alpha-amino acid;
CC         Xref=Rhea:RHEA:48940, ChEBI:CHEBI:15377, ChEBI:CHEBI:59869,
CC         ChEBI:CHEBI:77460; EC=3.4.13.19;
CC         Evidence={ECO:0000269|PubMed:17601807};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.0-9.0 with Ala-Gln as substrate at 37 degrees
CC         Celsius. Activity is very low below pH 5.5 and at pH 10.0 is about
CC         50% of the maximum. {ECO:0000269|PubMed:17601807};
CC       Temperature dependence:
CC         Optimum temperature is 50 degrees Celsius with Ala-Gln as substrate
CC         at pH 8.0. Activity is 30% of maximum at 20 degrees Celsius and 50%
CC         of maximum at 70 degrees Celsius. Stable when incubated for 10
CC         minutes at temperatures of up to 70 degrees Celsius.
CC         {ECO:0000269|PubMed:17601807};
CC   -!- MASS SPECTROMETRY: Mass=49496; Method=MALDI; Note=The measured mass is
CC       that of the post-translationally modified protein, but the nature of
CC       the post-translational modifications has not been determined.;
CC       Evidence={ECO:0000269|PubMed:17601807};
CC   -!- SIMILARITY: Belongs to the peptidase C69 family. {ECO:0000255}.
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DR   EMBL; AE014295; AAN24310.1; -; Genomic_DNA.
DR   RefSeq; NP_695674.1; NC_004307.2.
DR   RefSeq; WP_007051601.1; NC_004307.2.
DR   AlphaFoldDB; Q8G6Z9; -.
DR   SMR; Q8G6Z9; -.
DR   STRING; 216816.GS08_00840; -.
DR   MEROPS; C69.001; -.
DR   EnsemblBacteria; AAN24310; AAN24310; BL0479.
DR   GeneID; 66504386; -.
DR   KEGG; blo:BL0479; -.
DR   PATRIC; fig|206672.9.peg.1222; -.
DR   HOGENOM; CLU_014823_4_1_11; -.
DR   OMA; DLTYSHE; -.
DR   PhylomeDB; Q8G6Z9; -.
DR   Proteomes; UP000000439; Chromosome.
DR   GO; GO:0070004; F:cysteine-type exopeptidase activity; IEA:InterPro.
DR   GO; GO:0016805; F:dipeptidase activity; IDA:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR   InterPro; IPR005322; Peptidase_C69.
DR   PANTHER; PTHR12994; PTHR12994; 1.
DR   Pfam; PF03577; Peptidase_C69; 1.
PE   1: Evidence at protein level;
KW   Dipeptidase; Direct protein sequencing; Hydrolase; Protease;
KW   Reference proteome.
FT   CHAIN           1..533
FT                   /note="Dipeptidase"
FT                   /id="PRO_0000352778"
FT   ACT_SITE        3
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   533 AA;  59751 MW;  272B5CB2FB5BB6A3 CRC64;
     MACTTILVGK DASYDGSTII ARNEDSANGE FNPKRFIVVK PEEQPREYKS VISHLTITLP
     DDPLQYTAVP NADLKEGIWG EAGVNEANVA MSATETLTTN ERVLGADPFV EYTPAKGDEP
     EVPGGIGEED FLTIVLPYVK TAREGVQRLG ALLEEFGTYE MNGVAFSDSN EIWWLETVGG
     HHWIAKRVPD EAYVTMPNQL GIDEFDLEDA LGDQEAHMCS EDLAEFIETN HLDLAVENTT
     PFNPRDAFGS HSDSDHVYNT PRAWYMQRFL NPYDEVWDGP DADHKPTSDD IPWARQPERK
     VTIEDIKYVL SSHYQGTPFD PYGQLGDERT RHMYRTIGIN RQSQLAVMQI RPYRPQASRA
     IQWMAYGSNP FNTLVPFFPN VDTTPAYLED TTTRVTSENF YWANRIIAAL CDGAFRSTSN
     AVERYQEKTG AMGHRLVAAT DEQIARLGLT AAEEAAQSAA EEEFEADNVD GDVQPMTPDE
     TIAALRNPEV REILAAANQT MADQLKEETE KLLDSVLYTR SMEMKNGFHM SDF