DPP6_LYSSH
ID DPP6_LYSSH Reviewed; 271 AA.
AC P39043;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Dipeptidyl-peptidase 6;
DE EC=3.4.22.-;
DE AltName: Full=Dipeptidyl-peptidase VI;
DE Short=DPP VI;
DE AltName: Full=Endopeptidase II;
DE AltName: Full=Gamma-D-glutamyl-L-diamino acid endopeptidase II;
DE AltName: Full=Gamma-D-glutamyl-MESO-diaminopimelate peptidase II;
OS Lysinibacillus sphaericus (Bacillus sphaericus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=1421;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 396 / NCTC 9602;
RX PubMed=1587462; DOI=10.1111/j.1574-6968.1992.tb05203.x;
RA Hourdou M.-L., Duez C., Joris B., Vacheron M.-J., Guinand M., Michel G.,
RA Ghuysen J.-M.;
RT "Cloning and nucleotide sequence of the gene encoding the gamma-D-glutamyl-
RT L-diamino acid endopeptidase II of Bacillus sphaericus.";
RL FEMS Microbiol. Lett. 70:165-170(1992).
RN [2]
RP PROTEIN SEQUENCE OF 1-38, AND CHARACTERIZATION.
RC STRAIN=DSM 396 / NCTC 9602;
RX PubMed=1551459; DOI=10.1016/0020-711x(92)90041-x;
RA Bourgogne T., Vacheron M.-J., Guinand M., Michel G.;
RT "Purification and partial characterization of the gamma-D-glutamyl-L-di-
RT amino acid endopeptidase II from Bacillus sphaericus.";
RL Int. J. Biochem. 24:471-476(1992).
CC -!- FUNCTION: Involved in cell sporulation. Hydrolyzes gamma-D-Glu-L-
CC (meso)A2pm linkages only in those peptide units that have a free N-
CC terminal L-alanine.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- DEVELOPMENTAL STAGE: Expressed at onset of, and throughout sporulation.
CC -!- SIMILARITY: Belongs to the peptidase C40 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01284, ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X83680; CAA58651.1; -; Genomic_DNA.
DR EMBL; X64809; CAA46030.1; -; Genomic_DNA.
DR PIR; S26056; S26056.
DR AlphaFoldDB; P39043; -.
DR SMR; P39043; -.
DR MEROPS; C40.001; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR InterPro; IPR000064; NLP_P60_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR003646; SH3-like_bac-type.
DR InterPro; IPR041382; SH3_16.
DR Pfam; PF00877; NLPC_P60; 1.
DR Pfam; PF18348; SH3_16; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS51935; NLPC_P60; 1.
DR PROSITE; PS51781; SH3B; 2.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Hydrolase; Protease; Sporulation;
KW Thiol protease.
FT CHAIN 1..271
FT /note="Dipeptidyl-peptidase 6"
FT /id="PRO_0000213726"
FT DOMAIN 1..64
FT /note="SH3b 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01117"
FT DOMAIN 72..140
FT /note="SH3b 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01117"
FT DOMAIN 148..268
FT /note="NlpC/P60"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT ACT_SITE 178
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT ACT_SITE 224
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT ACT_SITE 236
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
SQ SEQUENCE 271 AA; 30604 MW; 08C46547548AAB0E CRC64;
MNAIVIAMMA NLYAEPDLHA ELVDEILYGM PVQIIEELEN DWLYVRTAYR YEGYCQRNDV
LFDDAITNTW IQKAQHVIGQ RFADVLQEPK IQSTKIITLV KGSILYNVDS DTTSNTPWTA
VQLATGEIGY LRSQWLHPKI AEHTFEEHAF RENVVQTALS YIATPYRWGG KSPLGIDCSG
LCSMAYLLNG VIIFRDARIV EGFPIKEITI DRMQKGDLLF FPGHVALYLG QTLYVHASLG
GNEVNVNSLD EQHPLYRQDL ATTITAIGSL F
