ID G0EUN6_CUPNN Unreviewed; 515 AA.
AC G0EUN6;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Zn-dependent peptidase, M16B subfamily {ECO:0000313|EMBL:AEI75747.1};
DE EC=3.4.-.- {ECO:0000313|EMBL:AEI75747.1};
GN OrderedLocusNames=CNE_1c03810 {ECO:0000313|EMBL:AEI75747.1};
OS Cupriavidus necator (strain ATCC 43291 / DSM 13513 / CCUG 52238 / LMG 8453
OS / N-1) (Ralstonia eutropha).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=1042878 {ECO:0000313|EMBL:AEI75747.1, ECO:0000313|Proteomes:UP000006798};
RN [1] {ECO:0000313|EMBL:AEI75747.1, ECO:0000313|Proteomes:UP000006798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43291 / DSM 13513 / CCUG 52238 / LMG 8453 / N-1
RC {ECO:0000313|Proteomes:UP000006798};
RX PubMed=21742890; DOI=10.1128/JB.05660-11;
RA Poehlein A., Kusian B., Friedrich B., Daniel R., Bowien B.;
RT "Complete genome sequence of the type strain Cupriavidus necator N-1.";
RL J. Bacteriol. 193:5017-5017(2011).
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR EMBL; CP002877; AEI75747.1; -; Genomic_DNA.
DR RefSeq; WP_013955458.1; NC_015726.1.
DR AlphaFoldDB; G0EUN6; -.
DR MEROPS; M16.019; -.
DR KEGG; cnc:CNE_1c03810; -.
DR HOGENOM; CLU_009902_1_0_4; -.
DR Proteomes; UP000006798; Chromosome 1.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR001431; Pept_M16_Zn_BS.
DR InterPro; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR43690; NARDILYSIN; 1.
DR PANTHER; PTHR43690:SF17; PROTEIN YHJJ; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
DR PROSITE; PS00143; INSULINASE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AEI75747.1};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 96..240
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 250..430
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 496..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 515 AA; 57712 MW; A7832B5C4EE4E174 CRC64;
MNHCAVLTAA GAQGTKACVQ TRIQRLSQPS NPLPARAARL ARRVIPTLLL ALLPWSMPAG
AQEAVPSPRP GTQTALAGAT AQGTTEYRLS NGLRLIVKED HRAPTVAHQI WYRVGGIDEV
SGTTGVAHML EHMMFKGTPK VGVGEFSKQV AALGGRENAM TNRDFTMYYQ QIGKQYLPRM
MELEADRMAN LIITKDEFER EMKVVMEERR LRTDDSARGT VYEQLLATVY TAAAYRHPVI
GWMDDLVNMR VDDVKEWYRH WYVPNNAMVI VTGDVKAEEV RALAERYYGK VKPRTLPLRK
DQEEPAQKGI KRIWVKAPAE NQYMVMAYKV PRLRDIEKDV DPYALEVLSA VLNGYDNARL
TRELVREQRL ADDVNVGYDS INRGESLFVL DGTPATGHNT DEIERALRAE VQRIAKEGVS
PEELKRVKAQ VVAGQIYKRD SVFGQGMEIG VSEISDISWR QIDRMLDKIK AVTPAQVQAV
AAKYFNDDNL TVATLVPQPI DPNKPKPQAP SGLRH
//
