ID A0A0F0CJ69_9BACT Unreviewed; 434 AA.
AC A0A0F0CJ69;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Beta-lactamase domain-containing protein {ECO:0000313|EMBL:KJJ83252.1};
GN ORFNames=OMAG_002926 {ECO:0000313|EMBL:KJJ83252.1};
OS Candidatus Omnitrophus magneticus.
OC Bacteria; Candidatus Omnitrophota; Omnitrophus.
OX NCBI_TaxID=1609969 {ECO:0000313|EMBL:KJJ83252.1, ECO:0000313|Proteomes:UP000033428};
RN [1] {ECO:0000313|EMBL:KJJ83252.1, ECO:0000313|Proteomes:UP000033428}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SKK-01 {ECO:0000313|EMBL:KJJ83252.1};
RA Kolinko S., Richter M., Glockner F.O., Brachmann A., Schuler D.;
RT "Single-cell genomics of uncultivated deep-branching MTB reveals a
RT conserved set of magnetosome genes.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
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:KJJ83252.1}.
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DR EMBL; JYNY01000634; KJJ83252.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F0CJ69; -.
DR PATRIC; fig|1609969.3.peg.3130; -.
DR Proteomes; UP000033428; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050313; F:sulfur dioxygenase activity; IEA:InterPro.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR CDD; cd07724; POD-like_MBL-fold; 1.
DR CDD; cd00158; RHOD; 1.
DR Gene3D; 6.10.140.1340; -; 1.
DR Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR044528; POD-like_MBL-fold.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR021309; YgaP-like_TM.
DR PANTHER; PTHR43084; PERSULFIDE DIOXYGENASE ETHE1; 1.
DR PANTHER; PTHR43084:SF1; PERSULFIDE DIOXYGENASE ETHE1, MITOCHONDRIAL; 1.
DR Pfam; PF00753; Lactamase_B; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR Pfam; PF11127; YgaP-like_TM; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000033428};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 388..413
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 264..353
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 434 AA; 48126 MW; 60F3404AD43D06A9 CRC64;
MFLIKRNILV LLKNEFHLTR RANMDQFKMK QFAAGSCFSY ILSSQEEALI IDPHISLLEE
YAGYLAKEKL SLKFIVDTHT HADHFSLAAV MKKKYNAQIL MHEKAVSSVA DKRLKNDDKI
ALGSGSIRVI YTPGHTDDSV SFYADSRLFT GDVLLIGSVG RTDFQNGSPE SMFNTLQKIK
ALPNATMIFP GHDYHEKRSS LLATEKNENP FLKENDKETF IKNMRAKVIP KPFNIDNIVR
VNQKGEAALL EMISPKEAAS LAQKNQRVKF LDVRSALEFA EVHIKDSINV PIDMISAKIN
DLSASGQAYI VLCRTGNRSP MAADMLIQSG IHDVKVMQGG MTRWQKEGLP VIKGQGGISL
ERQVRVIAGS LVLLGTLLSL TVHQGFVVIP IFVSCGLLFA GLTDNCLMGM LLMKLPYNKK
LYKTKLGGGT CAMG
//
