ID A0A0Q5HJ83_9BURK Unreviewed; 694 AA.
AC A0A0Q5HJ83;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=oligopeptidase A {ECO:0000256|ARBA:ARBA00026100};
DE EC=3.4.24.70 {ECO:0000256|ARBA:ARBA00026100};
GN ORFNames=ASF77_14290 {ECO:0000313|EMBL:KQQ87899.1};
OS Massilia sp. Leaf139.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1736272 {ECO:0000313|EMBL:KQQ87899.1, ECO:0000313|Proteomes:UP000051760};
RN [1] {ECO:0000313|EMBL:KQQ87899.1, ECO:0000313|Proteomes:UP000051760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf139 {ECO:0000313|EMBL:KQQ87899.1,
RC ECO:0000313|Proteomes:UP000051760};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQQ87899.1, ECO:0000313|Proteomes:UP000051760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf139 {ECO:0000313|EMBL:KQQ87899.1,
RC ECO:0000313|Proteomes:UP000051760};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQQ87899.1}.
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DR EMBL; LMOJ01000024; KQQ87899.1; -; Genomic_DNA.
DR RefSeq; WP_056341690.1; NZ_LMOJ01000024.1.
DR AlphaFoldDB; A0A0Q5HJ83; -.
DR STRING; 1736272.ASF77_14290; -.
DR OrthoDB; 9773538at2; -.
DR Proteomes; UP000051760; 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; 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; PTHR11804:SF79; MITOCHONDRIAL INTERMEDIATE PEPTIDASE; 1.
DR PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 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 Reference proteome {ECO:0000313|Proteomes:UP000051760};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 30..152
FT /note="Oligopeptidase A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF19310"
FT DOMAIN 229..691
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 694 AA; 78284 MW; A5953AC3BD54B16A CRC64;
METNASNPLL DFSGLPRFDA FRPEHVTPAI EQLIGEATAV VARLEAPSDQ VTWDNFVVPL
EEATERLGRA WGIVNHLNHV ADTPELRATY NENQPKVTEF WTTLGQNEVL FDKYKAIRAG
ADYDSLSPAR KRIVENALRD FRLGGAELPA DKKERFAAIQ EQHAAISTRF SENVLDATND
YKLIVDDESE LTGLPEDAKA AARAAAEAAG KSGFQFTLHF PSYFPLLQFA DNRKLRETIY
RASATKASDM GVVFSELEKW DNSSNIAQLL SLRDEEAKLL DYRNFAEVSL VPKMAESPEH
VINFLEDLAR RARPFAEKDL AELRAFAKEE LGIEDMQAWD VAYASEKLRE KRYAFSAQEV
KEYFPEPKVI EGLFKVVQTL FSVEIKPDTA PVWHPDVRFY RIERDGQLVG QFYFDLYARA
GKGQGAWMDD ARGRRMTTGG IVQTPVAYLT CNFTPPASVD GKLQPSLFTH DEVTTLFHEF
GHGLHHMLTE VEELSVSGIS GVEWDAVELP SQFMENFCWE WDVLQGMTAH FRSGEPLPRA
LYDKMLAAKN FQSGMQTLRQ VEFSLIDMHL HYDFDPRSQR TVQELIDDVR SKFSVMIPPS
FNRFQHSFGH IFAGGYAAGY YSYKWAEVLS ADAYAAFEEA LEAGGGELSA ETGRRFQREI
LAVGGSRPAL ESFKAFRGRE PSIDALLRHN GMNA
//
