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Database: UniProt
Entry: A0A0G1UVC5_9BACT
LinkDB: A0A0G1UVC5_9BACT
Original site: A0A0G1UVC5_9BACT 
ID   A0A0G1UVC5_9BACT        Unreviewed;       340 AA.
AC   A0A0G1UVC5;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Methicillin resistance protein {ECO:0000313|EMBL:KKU61645.1};
GN   ORFNames=UX85_C0002G0025 {ECO:0000313|EMBL:KKU61645.1};
OS   Candidatus Beckwithbacteria bacterium GW2011_GWB1_47_15.
OC   Bacteria; Candidatus Beckwithbacteria.
OX   NCBI_TaxID=1618371 {ECO:0000313|EMBL:KKU61645.1, ECO:0000313|Proteomes:UP000033860};
RN   [1] {ECO:0000313|EMBL:KKU61645.1, ECO:0000313|Proteomes:UP000033860}
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:KKU61645.1}.
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DR   EMBL; LCNT01000002; KKU61645.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1UVC5; -.
DR   Proteomes; UP000033860; Unassembled WGS sequence.
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; -; 2.
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; 3.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 2.
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   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984}.
SQ   SEQUENCE   340 AA;  39283 MW;  C96CD03783269289 CRC64;
     MSQITAKLVE NKDVWEDFVL NSPESNFLHS FNWGKFNQSL GFAVFRLGFY RQGKLKGVAL
     LVKKTARRGT YLECPAGPLI PWGEPGFFDH FLSSVKDIAA QEKASFVRVR PNLKDAPENH
     RLFKSRGFIR APMHLHAETT LVLDLTQSEE ELLRAMRKNT RYSIKKAQKM GVAIEMSASD
     ADVKNLYDLQ AEVVKRVKFV PFSLQYLLKQ FQTFKPDNQI QLIKASYQGQ LLAISFFIFY
     KDEAVYHYSG SSSRLREVPA SYLLQWAAIK KAKARGKTRY NLWGIAPDDN PKHRFAGVTL
     FKKGFGGERV DYLPAHDLPL KWTYWVTFIF ENLRRKQRQL
//
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