ID   A3P5J3_BURP0            Unreviewed;       689 AA.
AC   A3P5J3;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   RecName: Full=oligopeptidase A {ECO:0000256|ARBA:ARBA00026100};
DE            EC=3.4.24.70 {ECO:0000256|ARBA:ARBA00026100};
GN   Name=prlC {ECO:0000313|EMBL:ABN94435.1};
GN   OrderedLocusNames=BURPS1106A_A1569 {ECO:0000313|EMBL:ABN94435.1};
OS   Burkholderia pseudomallei (strain 1106a).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=357348 {ECO:0000313|EMBL:ABN94435.1, ECO:0000313|Proteomes:UP000006738};
RN   [1] {ECO:0000313|Proteomes:UP000006738}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1106a {ECO:0000313|Proteomes:UP000006738};
RA   DeShazer D., Woods D.E., Nierman W.C.;
RL   Submitted (FEB-2007) 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}.
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DR   EMBL; CP000573; ABN94435.1; -; Genomic_DNA.
DR   RefSeq; WP_004536949.1; NC_009078.1.
DR   AlphaFoldDB; A3P5J3; -.
DR   GeneID; 56530411; -.
DR   KEGG; bpl:BURPS1106A_A1569; -.
DR   HOGENOM; CLU_001805_4_1_4; -.
DR   Proteomes; UP000006738; Chromosome II.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
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   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT   DOMAIN          32..149
FT                   /note="Oligopeptidase A N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF19310"
FT   DOMAIN          224..686
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   689 AA;  76788 MW;  91A32CADDC66E6FF CRC64;
     MTQITLANPL LDRSQLPRFE SIRDFHVRPA IDALLIDLDN AISRASAKNL SPNWGNVIEP
     VSLALESLDY AWGAVAHLVS VRDCAPLRAA YGACAGRVSA ALSRFRQNGA LLDRYRAVAA
     SAGFRALSPE RRQVVRNLIR DARLAGAELP PGPRARLNEL RERIAQLAAV YQDNIADATR
     AFARIVTTDE ELDGIPDYAR AAAARRAAAG FEFTLDFASY QPVMQFSTCR ALREEMYRAR
     STRASEFDAA GANDAARRDN APVMAEILKL RREQAALLGY RDFAQMSLEH KMARTPARAR
     AFLERLHRRV SPKASLEWQA LQSFARAELG LADVQPWDIA FVAERMRERC FGVSTQDVRR
     YFPEHAVLRG LFALVETLFD IRIRADEGSV WHQDVRRYRL ETLRGEPVAH LYLDLYARDG
     KREGAWAASG RSRGTGADGA IRTPVAYLMC NVAAPAAGMP ACFAFDQVLT LFHEMGHCLH
     HMLTGVAESA ISGTNGIEWD AIEFPSQFME HFCWDPEVAS TLSAHVDTGE PLSDAMFERM
     LAARHFNQGI EMAHQIALSM LDIALHSGES IESVNSMQNT MHEIYQKYEF TPLDRRARSA
     NTFSHIFSGG YAAAYYSYQW AQVLAADAYA AVEEARAERA DAGKREAGMR YRKEVLEPGG
     SRPALDSFVA FRGRAPSLDA LLRHCRIDR
//