ID I0AI85_IGNAJ Unreviewed; 700 AA.
AC I0AI85;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=oligopeptidase A {ECO:0000256|ARBA:ARBA00026100};
DE EC=3.4.24.70 {ECO:0000256|ARBA:ARBA00026100};
GN Name=dcp {ECO:0000313|EMBL:AFH48692.1};
GN OrderedLocusNames=IALB_0980 {ECO:0000313|EMBL:AFH48692.1};
OS Ignavibacterium album (strain DSM 19864 / JCM 16511 / NBRC 101810 /
OS Mat9-16).
OC Bacteria; Ignavibacteriota; Ignavibacteria; Ignavibacteriales;
OC Ignavibacteriaceae; Ignavibacterium.
OX NCBI_TaxID=945713 {ECO:0000313|EMBL:AFH48692.1, ECO:0000313|Proteomes:UP000007394};
RN [1] {ECO:0000313|EMBL:AFH48692.1, ECO:0000313|Proteomes:UP000007394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19864 / JCM 16511 / NBRC 101810 / Mat9-16
RC {ECO:0000313|Proteomes:UP000007394};
RX PubMed=22661972; DOI=10.3389/fmicb.2012.00185;
RA Liu Z., Frigaard N.-U., Vogl K., Iino T., Ohkuma M., Overmann J.,
RA Bryant D.A.;
RT "Complete genome of Ignavibacterium album, a metabolically versatile,
RT flagellated, facultative anaerobe from the phylum Chlorobi.";
RL Front. Microbiol. 3:185-185(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of oligopeptides, with broad specificity. Gly or
CC Ala commonly occur as P1 or P1' residues, but more distant residues
CC are also important, as is shown by the fact that Z-Gly-Pro-Gly-|-Gly-
CC Pro-Ala is cleaved, but not Z-(Gly)(5).; EC=3.4.24.70;
CC Evidence={ECO:0000256|ARBA:ARBA00024603};
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}.
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; CP003418; AFH48692.1; -; Genomic_DNA.
DR RefSeq; WP_014559847.1; NC_017464.1.
DR AlphaFoldDB; I0AI85; -.
DR STRING; 945713.IALB_0980; -.
DR GeneID; 78242708; -.
DR KEGG; ial:IALB_0980; -.
DR PATRIC; fig|945713.3.peg.985; -.
DR eggNOG; COG0339; Bacteria.
DR HOGENOM; CLU_001805_4_0_10; -.
DR OrthoDB; 9773538at2; -.
DR Proteomes; UP000007394; Chromosome.
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; IPR045666; OpdA_N.
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 Pfam; PF19310; TOP_N; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
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:UP000007394};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 57..176
FT /note="Oligopeptidase A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF19310"
FT DOMAIN 250..697
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
FT COILED 130..192
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 700 AA; 80937 MW; 9E7F13FCEE72951A CRC64;
MRYIISGILL ITFISTVMLA QTISNNPFFE EWNTPFQTPP FSKIKNEHFL PALEEGIKQQ
RAELEQIINN SEAPTFQNTI AALEKSGKLL NKVTRVFFNL TGANTNDELQ KVAETITPQL
TKLNNDIYLN EKLYQRIKSI YEQKENLNLN KEELRLLENY YTDFTRAGIG LSEDKKKRLR
DINEQLSSLQ LKFGDNLRKE TNALGLVIDK EEDLIGLPDA VIKAAAELAE ANGLKGKWAF
NLQRPSWTPF LQYSQKRELR EKLYKAYLNR GNNNNEFDNK EIIKKIVELR IEKAKLLGYE
TYAHFKLEKN MAKTPENVLK FLNELWLPSI NQAKVEAAEM QKLIDDEGGN FKLAGWDWWY
YAEKVKKAKY ALDEEMLRPY FKMENVRKGA FDVASKLYGI KFIKRDDIEV YDNDVEVYEV
QEADGSLVGI LYTDYYPRNG KRAGAWMSYY RGQSNMEGEM IYPLVVNVGN FTKPTSDKPA
LLSFDDVNTL FHEFGHALNG LFARSTYPGS KRSPVDFVEL PSQIMENWAS HPDVLKMYAR
HYQTNEPITD ELIQKIQNSQ YFNKGFEQTE YLAASFLDMD WHTLKAPVQT DVNKFEEESL
NRIGLIPEIA SRYQSTNFNH IFGGDGYSAG YYGYSWAAVL DADAFEAFLE TDLFNQQVAK
SFRENILEKS GSDDPMELYK KFRGREPKVD ALLKRLGFKK
//
