ID A0A0G0DWC1_9BACT Unreviewed; 161 AA.
AC A0A0G0DWC1;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Methicillin resistance protein {ECO:0000313|EMBL:KKP59407.1};
GN ORFNames=UR53_C0002G0021 {ECO:0000313|EMBL:KKP59407.1};
OS Candidatus Magasanikbacteria bacterium GW2011_GWC2_34_16.
OC Bacteria; Candidatus Magasanikbacteria.
OX NCBI_TaxID=1619045 {ECO:0000313|EMBL:KKP59407.1, ECO:0000313|Proteomes:UP000034927};
RN [1] {ECO:0000313|EMBL:KKP59407.1, ECO:0000313|Proteomes:UP000034927}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
CC -!- SIMILARITY: Belongs to the FemABX family.
CC {ECO:0000256|ARBA:ARBA00009943}.
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:KKP59407.1}.
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DR EMBL; LBPO01000002; KKP59407.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0DWC1; -.
DR Proteomes; UP000034927; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016755; F:aminoacyltransferase activity; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 3.40.630.30; -; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR003447; FEMABX.
DR PANTHER; PTHR36174; LIPID II:GLYCINE GLYCYLTRANSFERASE; 1.
DR PANTHER; PTHR36174:SF1; LIPID II:GLYCINE GLYCYLTRANSFERASE; 1.
DR Pfam; PF02388; FemAB; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR PROSITE; PS51191; FEMABX; 1.
PE 3: Inferred from homology;
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 79..98
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 161 AA; 18856 MW; 1A33FB3958125EEA CRC64;
MQQTDEALLD AMRKNTRYSI RFAGKQNLVV KEEKNLAVFW DLLQQTAKHD NFTTHVKKHY
EAIFNFNSIY QLTAFKDDIA IATAVFVGFG NTFTYLFAAS DYKRHQLLAP YLLQWEAIKL
GQKLGYKYYD FFGIAPRMKG VKSKEKGISE HEYDERHLVV R
//