ID   A0A0G1U3X6_9BACT        Unreviewed;       361 AA.
AC   A0A0G1U3X6;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=FemAB family protein {ECO:0000313|EMBL:KKU88766.1};
GN   ORFNames=UY16_C0002G0038 {ECO:0000313|EMBL:KKU88766.1};
OS   Candidatus Gottesmanbacteria bacterium GW2011_GWA2_47_9.
OC   Bacteria; Candidatus Gottesmanbacteria.
OX   NCBI_TaxID=1618445 {ECO:0000313|EMBL:KKU88766.1, ECO:0000313|Proteomes:UP000034739};
RN   [1] {ECO:0000313|EMBL:KKU88766.1, ECO:0000313|Proteomes:UP000034739}
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:KKU88766.1}.
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DR   EMBL; LCOY01000002; KKU88766.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1U3X6; -.
DR   Proteomes; UP000034739; 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; -; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR038740; BioF2-like_GNAT_dom.
DR   InterPro; IPR003447; FEMABX.
DR   PANTHER; PTHR36174; LIPID II:GLYCINE GLYCYLTRANSFERASE; 1.
DR   PANTHER; PTHR36174:SF1; LIPID II:GLYCINE GLYCYLTRANSFERASE; 1.
DR   Pfam; PF13480; Acetyltransf_6; 1.
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}.
FT   DOMAIN          175..299
FT                   /note="BioF2-like acetyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF13480"
SQ   SEQUENCE   361 AA;  42134 MW;  72078DCECED9A93D CRC64;
     MAKRNKWEKP IVYRQPGNWM RFLHRKYIVT HRKKWENTNM KDIDKTIRAW DNHASHPLQS
     WAWGEFRKAM GVDVVRFDRS LLTFHEIPHT PWTIGYFPKG PKPTAAMLAT LVKLAKQKNA
     IFIQLEPNVV KNPKLQTLSS KLLIPSHHPL FTKYTFVLDL TKSEDELLKA MHPKTRYNIR
     VAQKHGVTVA EDNSDSALGA YLKLNAETTQ RQGFYAHNET YHRTMWKILH EAGIAKLFTA
     THQGNVLAAW IVFVWKDTVY YPYGASSREH REVMAPTLLL WEISRWAKAQ GFKYFDLWGS
     LGRSPNPNDP WYGFHRFKEG FAPALVEFVG SYDLIINPLL YPLYTLADTI RWTLLKLKRV
     S
//