ID A2SHP9_METPP Unreviewed; 677 AA.
AC A2SHP9;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE RecName: Full=oligopeptidase A {ECO:0000256|ARBA:ARBA00026100};
DE EC=3.4.24.70 {ECO:0000256|ARBA:ARBA00026100};
GN OrderedLocusNames=Mpe_A2132 {ECO:0000313|EMBL:ABM95088.1};
OS Methylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Methylibium.
OX NCBI_TaxID=420662 {ECO:0000313|EMBL:ABM95088.1, ECO:0000313|Proteomes:UP000000366};
RN [1] {ECO:0000313|EMBL:ABM95088.1, ECO:0000313|Proteomes:UP000000366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1232 / LMG 22953 / PM1
RC {ECO:0000313|Proteomes:UP000000366};
RX PubMed=17158667; DOI=10.1128/JB.01259-06;
RA Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W.,
RA Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M.,
RA Hristova K.R.;
RT "Whole-genome analysis of the methyl tert-butyl ether-degrading beta-
RT proteobacterium Methylibium petroleiphilum PM1.";
RL J. Bacteriol. 189:1931-1945(2007).
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; CP000555; ABM95088.1; -; Genomic_DNA.
DR RefSeq; WP_011829725.1; NC_008825.1.
DR AlphaFoldDB; A2SHP9; -.
DR STRING; 420662.Mpe_A2132; -.
DR MEROPS; M03.004; -.
DR KEGG; mpt:Mpe_A2132; -.
DR eggNOG; COG0339; Bacteria.
DR HOGENOM; CLU_001805_4_1_4; -.
DR Proteomes; UP000000366; Chromosome.
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 Reference proteome {ECO:0000313|Proteomes:UP000000366};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 28..149
FT /note="Oligopeptidase A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF19310"
FT DOMAIN 221..674
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 677 AA; 74919 MW; 0EE1C48D5BC8E4B5 CRC64;
MSNPLLDTAA LPRFGEIRPE HVEPAVEALL AEANVALERA TGADVPADYD ALSAVLDVAT
ERLGRAWGAV SHLNAVADTP ELRAAYTEAL PRVTEFYTNL GADERLYAKY KAVAGSPAAA
ALNAARRKAL SNAMRDFVLS GAELQGAAKE RFAAIQARQA ELGQAFSEHV LDATDGWSFI
ASEAELAGVP EDVKAATRAA ARADGQDGHK LSLHMPVYLP VLQYAQDRAL RERVYRAHVT
RASEAGPTER DNSAVMGEIL TLRQEEAELL GYRNFAEVSL VAKMADSPAQ VQGFLRDLAR
RARPHAERDL AELREFARTE LGLADLQAWD MAYAAERLKE ARYAFSDTEV KQYFTEPKVL
AGLFRIIETL FEVAIRPDTA PVWNEHVRFF RIERGTQLVG QFYLDPYARP GKRPGAWMDD
VRGRWARPEG RVQTPVAHLV CNFAAPVGDR PALLSHDDVT TLFHEFGHGL HHMLTQVDEI
GVAGISGVEW DAVELPSQFM ENFCWEWEVV KHMTAHVDSG EPLPRTLFDK MLAAKNFQSG
LQTLRQVEFS LFDMLIHDGA SAAPYGADAI QRVLDGVRRE IAVIVPPAFN RFQHSFSHIF
AGGYAAGYYS YKWAEVLSAD AYAAFEEEGV FNPAVGRRYR EAILEAGGSR PAMESFKAFR
GREPRIDALL RHQGMAD
//
