Y3033_CUPNH
ID Y3033_CUPNH Reviewed; 228 AA.
AC Q0K7B3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=UPF0758 protein H16_A3033;
GN OrderedLocusNames=H16_A3033;
OS Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS / H16 / Stanier 337) (Ralstonia eutropha).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=381666;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
RX PubMed=16964242; DOI=10.1038/nbt1244;
RA Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R.,
RA Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I.,
RA Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.;
RT "Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia
RT eutropha H16.";
RL Nat. Biotechnol. 24:1257-1262(2006).
CC -!- SIMILARITY: Belongs to the UPF0758 family. {ECO:0000305}.
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DR EMBL; AM260479; CAJ94108.1; -; Genomic_DNA.
DR RefSeq; WP_010814979.1; NZ_CP039287.1.
DR AlphaFoldDB; Q0K7B3; -.
DR SMR; Q0K7B3; -.
DR STRING; 381666.H16_A3033; -.
DR EnsemblBacteria; CAJ94108; CAJ94108; H16_A3033.
DR GeneID; 57645158; -.
DR KEGG; reh:H16_A3033; -.
DR eggNOG; COG2003; Bacteria.
DR HOGENOM; CLU_073529_0_0_4; -.
DR OMA; AMPDYEL; -.
DR OrthoDB; 1833204at2; -.
DR Proteomes; UP000008210; Chromosome 1.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd08071; MPN_DUF2466; 1.
DR InterPro; IPR037518; MPN.
DR InterPro; IPR025657; RadC_JAB.
DR InterPro; IPR010994; RuvA_2-like.
DR InterPro; IPR001405; UPF0758.
DR PANTHER; PTHR30471; PTHR30471; 1.
DR Pfam; PF04002; RadC; 1.
DR SUPFAM; SSF47781; SSF47781; 1.
DR TIGRFAMs; TIGR00608; radc; 1.
DR PROSITE; PS50249; MPN; 1.
PE 3: Inferred from homology;
KW Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome;
KW Zinc.
FT CHAIN 1..228
FT /note="UPF0758 protein H16_A3033"
FT /id="PRO_1000001685"
FT DOMAIN 102..224
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT MOTIF 173..186
FT /note="JAMM motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 173
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 186
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
SQ SEQUENCE 228 AA; 24919 MW; 9D334EE3CABFDBDF CRC64;
MTIANWPACE RPREKLMESG AAALSDAELL AILLRVGAAG KSAVDLAREL LHRFGSLTAL
FAAEGRALTS VRGMGETKYA QLQAIPELAR RALAESLRLP TGFDGPAAVR NYLRLTLAPL
PHEVFLCLFL DPRNRMVASE EMFRGTLTRT AVYPREVARQ ALVHNAAGII VAHNHPRGTT
APSQSDIRLT HELARTLDLI DVRLLDHFIV AGQEIRSLAD CCDRLPGL