ID A0A109JNA2_9BRAD Unreviewed; 475 AA.
AC A0A109JNA2;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Peptidase M20 {ECO:0000313|EMBL:KWV51854.1};
GN ORFNames=AS156_11435 {ECO:0000313|EMBL:KWV51854.1};
OS Bradyrhizobium macuxiense.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=1755647 {ECO:0000313|EMBL:KWV51854.1, ECO:0000313|Proteomes:UP000057737};
RN [1] {ECO:0000313|EMBL:KWV51854.1, ECO:0000313|Proteomes:UP000057737}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BR 10303 {ECO:0000313|EMBL:KWV51854.1,
RC ECO:0000313|Proteomes:UP000057737};
RA Zelli J.E., Simoes-Araujo J.L., Barauna A.C., Silva K.;
RT "Draft Genome Sequence of the Strain BR 10303 (Bradyrhizobium sp.) isolated
RT from nodules of Centrolobium paraense.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M20A family.
CC {ECO:0000256|ARBA:ARBA00006247}.
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:KWV51854.1}.
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DR EMBL; LNCU01000088; KWV51854.1; -; Genomic_DNA.
DR RefSeq; WP_066510604.1; NZ_LNCU01000088.1.
DR AlphaFoldDB; A0A109JNA2; -.
DR OrthoDB; 9809784at2; -.
DR Proteomes; UP000057737; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.150.900; -; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR001261; ArgE/DapE_CS.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR047177; Pept_M20A.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR PANTHER; PTHR45962; N-FATTY-ACYL-AMINO ACID SYNTHASE/HYDROLASE PM20D1; 1.
DR PANTHER; PTHR45962:SF1; N-FATTY-ACYL-AMINO ACID SYNTHASE_HYDROLASE PM20D1; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|ARBA:ARBA00022670}; Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..475
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007137007"
FT DOMAIN 224..370
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 475 AA; 51607 MW; 8145A3CCE377B51D CRC64;
MSHKSKKTSR SLLLSSAVFG PLLLATGAAA QGLTEQQQFA RGIYQELVEI NTTTATGDTQ
KAAEAMGARL RAAGFSEDDV HVFSPAPHKG DLVARLRGSG AKKPILLLAH IDVVPANRED
WSVDPFKLTE QDGYFYGRGS SDDKYMAASF ITNLIRYKKE GYKPDRDIIV ALETDEEILD
ANGLGIQWLI KNHRDLIDAE FALNEGGGVG LKNGKAIRNS VQTSEKVSIG YQLTVKDRGG
HSSLPRKDNA IYRLAEGLIR LSNYSFPLNL NETTRIYFTR TAETESKQNA DDIRAVLAPQ
PDPAALARLS EHPGYNAQLR TTCVATMLQG GHALNALPQL ATAKVNCRIM PGEPVEGVQT
AIERVLADKQ IAVTPTGKAV LSPPSPLNEE VMGSIEKLSK EFWPDAAIVP VMSTGATDGS
YLRNAGIPTY GHSGLAADVD DNRNHGRDER VLVKSFYEGQ DYLYRLVKML AGGKS
//
