ID   F8N8J9_9BACT            Unreviewed;       710 AA.
AC   F8N8J9;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   SubName: Full=Peptidyl-dipeptidase Dcp {ECO:0000313|EMBL:EGN56566.1};
DE            EC=3.4.15.5 {ECO:0000313|EMBL:EGN56566.1};
GN   ORFNames=Premu_1126 {ECO:0000313|EMBL:EGN56566.1};
OS   Hallella multisaccharivorax DSM 17128.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Hallella.
OX   NCBI_TaxID=688246 {ECO:0000313|EMBL:EGN56566.1, ECO:0000313|Proteomes:UP000002772};
RN   [1] {ECO:0000313|Proteomes:UP000002772}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17128 {ECO:0000313|Proteomes:UP000002772};
RX   PubMed=22180809; DOI=10.4056/sigs.2164949;
RA   Pati A., Gronow S., Lu M., Lapidus A., Nolan M., Lucas S., Hammon N.,
RA   Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S.,
RA   Liolios K., Pagani I., Mavromatis K., Mikhailova N., Huntemann M., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Detter J.C., Brambilla E.M., Rohde M.,
RA   Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Ivanova N.;
RT   "Non-contiguous finished genome sequence of the opportunistic oral pathogen
RT   Prevotella multisaccharivorax type strain (PPPA20).";
RL   Stand. Genomic Sci. 5:41-49(2011).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU003435};
CC       Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC   -!- SIMILARITY: Belongs to the peptidase M3 family.
CC       {ECO:0000256|ARBA:ARBA00006040, ECO:0000256|RuleBase:RU003435}.
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DR   EMBL; GL945017; EGN56566.1; -; Genomic_DNA.
DR   AlphaFoldDB; F8N8J9; -.
DR   STRING; 688246.Premu_1126; -.
DR   eggNOG; COG0339; Bacteria.
DR   HOGENOM; CLU_001805_4_0_10; -.
DR   Proteomes; UP000002772; Unassembled WGS sequence.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd06456; M3A_DCP; 1.
DR   Gene3D; 1.10.1370.40; -; 1.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 1.10.1370.10; Neurolysin, domain 3; 1.
DR   InterPro; IPR034005; M3A_DCP.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR024077; Neurolysin/TOP_dom2.
DR   InterPro; IPR045090; Pept_M3A_M3B.
DR   InterPro; IPR001567; Pept_M3A_M3B_dom.
DR   PANTHER; PTHR43660; DIPEPTIDYL CARBOXYPEPTIDASE; 1.
DR   PANTHER; PTHR43660:SF1; DIPEPTIDYL CARBOXYPEPTIDASE; 1.
DR   Pfam; PF01432; Peptidase_M3; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000313|EMBL:EGN56566.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003435};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU003435};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU003435};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003435};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002772};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT   DOMAIN          257..707
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   710 AA;  82147 MW;  495E54A22677D25A CRC64;
     MVVSKKKYTF VVDMESKNNS DNRTSIPTRT NPFMESYGTL HDTVPFDKIQ FEDFEPAFLE
     GIRRDNEAIL RIVDNFEAPT FDNTIAWTDD SKGEHYYDLL DRVSNTFSCL MNAETNPQME
     ALAQKLSPVL TKHENDVTLN PRLFARIKQV YEHHRKLTAE EQMLLDKEYD AFVRSGALLD
     EAGKDRLRKL TEEASMLALQ FSQNLLKENK AYILHLTDRR QLDGLPDTAV DAAAMAAKEK
     GLEGWVFTLD FPSYSPFMTY STQRDLRKQI YMARSTECTH DNDANNLDIC RRLVNVRREI
     AQMLGYDTFA DYVLKHRMAS NVENVYKLIH DLINAYKPAA IEEVKAVEEG ARRAEGPDFK
     LEPWDFSFYS HKLQMEKYNL DAEMLRPYFQ LDNVVKGVFG LANRLYGITF KENKQIPVYH
     PDVKAYEVFD KDGSYLAVFY ADFYPREGKQ GGAWMTEFQG QWITKKGKNV RPHVSVVTNF
     TKPTATKPAL LSLGEVETFL HEFGHSLHGM FANTRFESLS GTNVWWDFVE MPSQFMENYA
     VEPDFLHTFA FHYQTGEPIP DELISRIVRS RNFNVAYACM RQVSFCLLDM AYYTQREPFT
     QDIIPFEKQA WKEAMVTPQL PDTCMTAQFS HIMAGGYAAG YYSYKWAEVL DADAFSVFKR
     EGIFNRATAQ RFRDCILSRG GTEHPMTLFK RFRGQEPTIE ALLQRNGIRK
//