ID   A0A0G1TMK1_9BACT        Unreviewed;       337 AA.
AC   A0A0G1TMK1;
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=Aminoacyltransferase FemX {ECO:0000313|EMBL:KKU83034.1};
GN   ORFNames=UY10_C0016G0008 {ECO:0000313|EMBL:KKU83034.1};
OS   Microgenomates group bacterium GW2011_GWA2_47_8.
OC   Bacteria.
OX   NCBI_TaxID=1618503 {ECO:0000313|EMBL:KKU83034.1, ECO:0000313|Proteomes:UP000034016};
RN   [1] {ECO:0000313|EMBL:KKU83034.1, ECO:0000313|Proteomes:UP000034016}
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:KKU83034.1}.
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DR   EMBL; LCOS01000016; KKU83034.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1TMK1; -.
DR   Proteomes; UP000034016; 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   Acyltransferase {ECO:0000313|EMBL:KKU83034.1};
KW   Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW   Transferase {ECO:0000313|EMBL:KKU83034.1}.
SQ   SEQUENCE   337 AA;  38384 MW;  90614E565AD7EB6C CRC64;
     MKLRIDAILD RPVWEYFWEA HGPQAFFQSW LWGEVMKRQS VPLTRFGLYD AAHLVGIFQV
     ATIRARRGTH LHVRHGPIVV GSELALWKHA VAFLKGQAKN DGASFVRISP QLEDSHTSRA
     LLRAFGMIPA AVHEVDAERC WVLDITPSED VLMAGMRKTT RYEIKRAIKE GIVIDKSEDP
     EALQSFFDLY RQTAARHRFV PHKGVKEEFS VFAKEHRGLI FSGSDHGETT AVAIVLFSGN
     EAIYHHGASR LSRLPVNYAI QWEAIRTAKK RGMSVYNFWG VAPDGNLKHP WWGHSQFKKG
     FGGSERKTIH AYDLPLSPTY HISRTIEFVR TRLRGYG
//