ID A0A069PNM4_9BURK Unreviewed; 679 AA.
AC A0A069PNM4;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=Peptidyl-dipeptidase {ECO:0000313|EMBL:KDR42175.1};
GN ORFNames=BG61_11090 {ECO:0000313|EMBL:KDR42175.1};
OS Caballeronia glathei.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Caballeronia.
OX NCBI_TaxID=60547 {ECO:0000313|EMBL:KDR42175.1, ECO:0000313|Proteomes:UP000027466};
RN [1] {ECO:0000313|EMBL:KDR42175.1, ECO:0000313|Proteomes:UP000027466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 50014 {ECO:0000313|EMBL:KDR42175.1,
RC ECO:0000313|Proteomes:UP000027466};
RA Liu X.Y., Li C.X., Xu J.H.;
RT "Draft Genome Sequences of Four Burkholderia Strains.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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:KDR42175.1}.
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DR EMBL; JFHC01000019; KDR42175.1; -; Genomic_DNA.
DR RefSeq; WP_035934534.1; NZ_JFHC01000019.1.
DR AlphaFoldDB; A0A069PNM4; -.
DR STRING; 60547.GCA_000751215_04008; -.
DR Proteomes; UP000027466; 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; 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 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:UP000027466};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 230..675
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 679 AA; 76089 MW; 610F28DFDD572DA4 CRC64;
MTDHGNPLLR DWQEHYGLPP FEQIRVEHFA PAFAVLFEQH LAEIDALAEN PSVPTFGNTV
AAFDAAGAAL DRVRLTFENL CSSESPPALQ AVEREMAPLL AAHDSKVTMH AGFFARLDAV
HRQADALELN EEQRRLLQRL HTDFVRTGAT LQGAARECFA AIATQLADLH TRFSQNILAD
ESSFQLPLAS DADLAGLPDF LRQAARGAAQ ERGVEGYVIT LSRSLVQPFL TWSTRRDLRE
AAWRAWTARG ETPGRDNRPL AREILALRQE QARLLGYETF ADYALSDRMA GSASAVHELL
GRVWEPAKAS VERERQALVS QAAALGEPTD VEPWDWYYLA EKVRASRFAL DDAQVKPYFS
LDAMLNAMFD CAQRLFGVQF VEQTGAPLYH PDVRLWEVRR GNERVGLFLG DNFARPNKQG
GAWMHVYRRQ TRNGGRVEPI VVNNNNFSRV DDGPTLLSFD DVRTLFHEFG HGLHGLLSDV
NYGRLSGTNV PRDYVELPSQ LMENWATVPE VLTRHARHVT TGEPIPAALV ERIRASQTFN
QGFETVAYTA SALIDMALHL QSDPAGVDIA RFETEERAHL GVPPEVGMRH RLPHFGHVFS
GAYYAAGYYV YMWAEVLEAE AFDAFEEAGN AFDPVLADKL KRCIYSAGDS REQRAAFRAF
RGRDPRVEPM LRKRGLLPQ
//
