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Database: UniProt
Entry: A0A0G1K4S8_9BACT
LinkDB: A0A0G1K4S8_9BACT
Original site: A0A0G1K4S8_9BACT 
ID   A0A0G1K4S8_9BACT        Unreviewed;       345 AA.
AC   A0A0G1K4S8;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=FemAB family protein {ECO:0000313|EMBL:KKT78590.1};
GN   ORFNames=UW73_C0001G0037 {ECO:0000313|EMBL:KKT78590.1};
OS   Microgenomates group bacterium GW2011_GWB1_44_8.
OC   Bacteria.
OX   NCBI_TaxID=1618505 {ECO:0000313|EMBL:KKT78590.1, ECO:0000313|Proteomes:UP000034467};
RN   [1] {ECO:0000313|EMBL:KKT78590.1, ECO:0000313|Proteomes:UP000034467}
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:KKT78590.1}.
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DR   EMBL; LCJL01000001; KKT78590.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1K4S8; -.
DR   STRING; 1618505.UW73_C0001G0037; -.
DR   Proteomes; UP000034467; 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; IPR003447; FEMABX.
DR   PANTHER; PTHR36174; LIPID II:GLYCINE GLYCYLTRANSFERASE; 1.
DR   PANTHER; PTHR36174:SF1; LIPID II:GLYCINE GLYCYLTRANSFERASE; 1.
DR   Pfam; PF02388; FemAB; 2.
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   345 AA;  40181 MW;  B21C29AE0E2D012B CRC64;
     MRLKEVSESE KITYSKLAQH PLQSWEWGDF RNSYGTKTYR LGHYNGNKLL ATFELTSHPI
     PKTGYVILVC FRSSVPSPEV LREFQDFGKA KSALCIKFEP NVNKLVNGIE NKNFNRSKKY
     LLSNGCALGR AQFARYSFII DLGKKEDDIF TNFNSKTRYN VRLASKHGVK VVEDNSPAAW
     DAYWRLTQET TQRQHFYSHN LHYHRLLWEH LKPAGMAHLL TATFHGEVLS TWMLFLFNDL
     LYYPYGAWSG KHKEVMANNL MMWEAIRWGK AHGAKKFDLW GAAGPETPKD DPWQGFTRFK
     EGYGGDLVEF LGSYDLVINK PLYKIYRQAE SLRWSLLRLR KILPF
//
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