ID   Q1D5W7_MYXXD            Unreviewed;       714 AA.
AC   Q1D5W7;
DT   11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2006, sequence version 1.
DT   27-MAR-2024, entry version 99.
DE   RecName: Full=Dipeptidyl-peptidase {ECO:0000256|RuleBase:RU366067};
DE            EC=3.4.14.- {ECO:0000256|RuleBase:RU366067};
GN   OrderedLocusNames=MXAN_3774 {ECO:0000313|EMBL:ABF92735.1};
OS   Myxococcus xanthus (strain DK1622).
OC   Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC   Myxococcaceae; Myxococcus.
OX   NCBI_TaxID=246197 {ECO:0000313|EMBL:ABF92735.1, ECO:0000313|Proteomes:UP000002402};
RN   [1] {ECO:0000313|EMBL:ABF92735.1, ECO:0000313|Proteomes:UP000002402}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DK1622 {ECO:0000313|Proteomes:UP000002402};
RX   PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA   Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S.,
RA   Eisen J.A., Ronning C.M., Barbazuk W.B., Blanchard M., Field C.,
RA   Halling C., Hinkle G., Iartchuk O., Kim H.S., Mackenzie C., Madupu R.,
RA   Miller N., Shvartsbeyn A., Sullivan S.A., Vaudin M., Wiegand R.,
RA   Kaplan H.B.;
RT   "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006).
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}.
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DR   EMBL; CP000113; ABF92735.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1D5W7; -.
DR   STRING; 246197.MXAN_3774; -.
DR   EnsemblBacteria; ABF92735; ABF92735; MXAN_3774.
DR   KEGG; mxa:MXAN_3774; -.
DR   eggNOG; COG3591; Bacteria.
DR   HOGENOM; CLU_013776_0_0_7; -.
DR   OrthoDB; 9805367at2; -.
DR   Proteomes; UP000002402; Chromosome.
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; IPR027267; AH/BAR_dom_sf.
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; SSF103657; BAR/IMD domain-like; 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}; Hydrolase {ECO:0000256|RuleBase:RU366067};
KW   Protease {ECO:0000256|RuleBase:RU366067};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002402};
KW   Serine protease {ECO:0000256|RuleBase:RU366067};
KW   Signal {ECO:0000256|RuleBase:RU366067}.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000256|RuleBase:RU366067"
FT   CHAIN           36..714
FT                   /note="Dipeptidyl-peptidase"
FT                   /evidence="ECO:0000256|RuleBase:RU366067"
FT                   /id="PRO_5023101611"
SQ   SEQUENCE   714 AA;  78851 MW;  123ACE75D62E5013 CRC64;
     MSFPQNRDTH GPGKDRFMKR LFVIATLLGA APAMADEGMW TYNNFPSAKV KEKYGFEPSQ
     QWLDNVRLSS ARLAGGCSAS FVSANGLVMT NHHCARGCID QLSTAKKDYI ANGFYAKAQG
     EETQCPAMEI NQLVKITDVT ETLNKATQGL TGKKYADTLK AKMSELEQAC SAGNAKARCD
     VVTLYQGGQY NLYEYKRFQD VRLVMAPEHA IAFFGGDPDN FEFPRYDLDV TFLRVYEDGK
     PATTNNFFKW SDKGAQEGEL TFISGHPGRT SRGLTIAELE FQRDVVLPKT LMTLSEMRGM
     LTEFGRRGAE QRRISTNLLF GVENSVKALK GRHEALLDKT FFAQKVAAEQ DLRKKVEANP
     EMKKKYAAAW DEIAKAQAQL RNIRQDLTFM ENGGGLSSTL FQVARTLVRG AEEFPKANGE
     RLREFNQANV PALEAQLFSP APVYPELEIA RLTFSLTKMR EELGSDHPFV KKVLGKESPE
     KLAARLVKGT KLRDVKARQA LYKGGKAAIA ASKDPMIQLA VALDPDMRAV RKSYEENVES
     VIRKNSELVA KSKFEIYGTN QYPDATFSLR LSYGAVKGYS ENGKQVSPIT QMAGTFEHAT
     GEEPFALPKS WLKNEKALDG TTPMNFVSTN DIIGGNSGSP VINKDAEIVG IVFDGNIQSL
     GGEYGFDESV NRSVSVHSQA IIESLTKIYG ATRLLEELRP GSTKVPPVKA SPAK
//