ID N8RDL1_9GAMM Unreviewed; 679 AA.
AC N8RDL1;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=oligopeptidase A {ECO:0000256|ARBA:ARBA00026100};
DE EC=3.4.24.70 {ECO:0000256|ARBA:ARBA00026100};
GN ORFNames=F989_01350 {ECO:0000313|EMBL:ENU33503.1};
OS Acinetobacter parvus NIPH 1103.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1217671 {ECO:0000313|EMBL:ENU33503.1, ECO:0000313|Proteomes:UP000018426};
RN [1] {ECO:0000313|EMBL:ENU33503.1, ECO:0000313|Proteomes:UP000018426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIPH 1103 {ECO:0000313|EMBL:ENU33503.1,
RC ECO:0000313|Proteomes:UP000018426};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter parvus NIPH 1103.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ENU33503.1}.
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DR EMBL; APOL01000024; ENU33503.1; -; Genomic_DNA.
DR RefSeq; WP_004678552.1; NZ_KB849226.1.
DR AlphaFoldDB; N8RDL1; -.
DR STRING; 134533.GCA_001485085_00211; -.
DR PATRIC; fig|1217671.3.peg.1341; -.
DR HOGENOM; CLU_001805_4_1_6; -.
DR Proteomes; UP000018426; Unassembled WGS sequence.
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; 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 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 Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 36..149
FT /note="Oligopeptidase A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF19310"
FT DOMAIN 221..670
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 679 AA; 77309 MW; D8AEC97D9A9B107D CRC64;
MTLQQATLPV PQFDQIQLAD LKQQIEQTIQ NGQNFLNQLK EVPQNSEAQL ATLTEVDQLE
NNMSESWGIL SHLNAVMNNA ETREVYQSLL PSLSEYYTQL GQHTALYQTY QQIHDTPVFQ
TLSEAQQSAI KLALRDFKLS GVALQGEAKK RYAEISARLS QLSSDFSNHV LDATQAYFKP
LTEAQLKGLP QSSVELLKQY GQQRELEQAV ATLDFPAYFA IMTYADDLEL REELYKAYVT
RASDQSDKTE FDNTPVMEEI LSLRQEMAQL LGFNNFAEYS LASKMAPDVE TVDKFLVDLA
EHARTPALAE IAELKSIAQQ DGIEELKPWD ATYYSEKLKQ QKFNLSQEAL KPYFPAPKVV
DGLFQIVQRL YGIQIIERQA PVWQDDVRYF EFEDQGQVVG GFYFDLYARN GKRGGAWMSG
FRSRVQTANG LQKPICYMVC NFTPPIGNQP ALLTHDEVIT LFHEFGHGLH HMLTEVDNIS
VAGTHGVAWD AVELPSQFME FWAWDNESLD VLSEHTETKQ TLPQELLSAL LNARFFQSGM
QTLRQIEFAL FDLTIHRQTP ALNSQQIQET LNDIRAKFAV VPTVPYNRFQ HSFSHIFAGG
YAAGYYSYKW AEVLASDAFD RFESEGIFNT ETGKEFRKFI LAVGGKNTAL DAFRNFRKRE
PKIDALLRHQ GWTNTDKTA
//
