ID G2ZLR8_9RALS Unreviewed; 706 AA.
AC G2ZLR8;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 03-MAY-2023, entry version 41.
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:CCA80012.1};
GN ORFNames=BDB_80399 {ECO:0000313|EMBL:CCA80012.1};
OS blood disease bacterium R229.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=741978 {ECO:0000313|EMBL:CCA80012.1};
RN [1] {ECO:0000313|EMBL:CCA80012.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=R229 {ECO:0000313|EMBL:CCA80012.1};
RX PubMed=21931687; DOI=10.1371/journal.pone.0024356;
RA Remenant B., de Cambiaire J.C., Cellier G., Jacobs J.M., Mangenot S.,
RA Barbe V., Lajus A., Vallenet D., Medigue C., Fegan M., Allen C., Prior P.;
RT "Ralstonia syzygii, the Blood Disease Bacterium and some Asian R.
RT solanacearum strains form a single genomic species despite divergent
RT lifestyles.";
RL PLoS ONE 6:e24356-e24356(2011).
RN [2] {ECO:0000313|EMBL:CCA80012.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=R229 {ECO:0000313|EMBL:CCA80012.1};
RA Genoscope - CEA;
RL Submitted (APR-2011) 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; FR854064; CCA80012.1; -; Genomic_DNA.
DR AlphaFoldDB; G2ZLR8; -.
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; 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 40..160
FT /note="Oligopeptidase A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF19310"
FT DOMAIN 235..696
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 706 AA; 78460 MW; F411AB9FD6D0115F CRC64;
MTVISPEVAT PATNPLLDFS GLPRFAEIRP EHITPALDAL LERATAAVAR VKDPSTPSTW
DSVVAALEDA TEPLGRAWGI VSHLSAVADT PALREAHAAN LPRVTEFWSG LGQDLALFKK
YKAIAESAEY ATLTPPRKKL LDNELRGFRL GGAELPEDQK PRFAAIQEQQ AQLTKAFSDH
VLDATNGYAL LIDDEARLSG LPDDARQAAR ETARRDNPAS TGWKFTLHFP SYFPVLQYAD
DRALRRTLYE ANVTRASELG PQHGGGKPEW DNTANMAEQL ALRAEEAHML GYRNFGEVSL
VPKMADSPEE VLRFLGELAD RARPFAEKDW AELQAFAKTT LGIDKLEPWD MAYASEKLRE
ARYAFSEQEV KQYFPEPAVL DGLFDVVQTL FSVKIRPEPA EVWHPDVRFF RVESAQGELL
AQFYIDLYAR EGKRGGAWMD DARGRKALAD AHVQTPVAYL TCNFSGPVGD KPALFTHDEV
ITLFHEFGHG LHHMLTQVDE LGVSGINGVE WDAVELPSQF MENFCWEWEV LPRMTRHVES
GESLPRALFE RMLAAKNFQN GMATLRQIVF STFDMHLHTD FDPKGATPVL ALSRQINDRF
HVVPQAALSR WPNTFSHIFA GGYAAGYYSY KWAEVLSADA YAAFEEASRL TGSVLDAETG
ARYRREVLAV GGSRPAIDSF TAFRGRAPTI DALLRHGGMV VTAEPA
//
