ID A0A0S8I268_9CHLR Unreviewed; 356 AA.
AC A0A0S8I268;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=N-acetyltransferase domain-containing protein {ECO:0000259|PROSITE:PS51186};
GN ORFNames=AMJ88_13895 {ECO:0000313|EMBL:KPK91385.1};
OS Anaerolineae bacterium SM23_ 63.
OC Bacteria; Chloroflexota; Anaerolineae.
OX NCBI_TaxID=1703387 {ECO:0000313|EMBL:KPK91385.1, ECO:0000313|Proteomes:UP000051685};
RN [1] {ECO:0000313|EMBL:KPK91385.1, ECO:0000313|Proteomes:UP000051685}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_ 63 {ECO:0000313|EMBL:KPK91385.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(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:KPK91385.1}.
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DR EMBL; LJUS01000053; KPK91385.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8I268; -.
DR PATRIC; fig|1703387.3.peg.2976; -.
DR Proteomes; UP000051685; Unassembled WGS sequence.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
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 InterPro; IPR000182; GNAT_dom.
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.
DR PROSITE; PS51186; GNAT; 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 177..335
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 356 AA; 40694 MW; A68F566D6EC02C2D CRC64;
MITNLPGGHL LQSWEWGDLK EKYGWRAERW IWAKEGSKPS AAAQILSRAL HLPGIGTGFE
ILYCPRGPIL DWSDETIRRP VVSDLAVMAK QRGAISIKID PHVIVGYSIP GESDAVNTTS
GQSITEDLLE IGWRESNEQI QFRNTLVLDI QDSEEALLAG MKQKTRYNIR LARRREIDVR
PGGMEDLDVL YQMYAETSLR DGFVIRKPEY YQDAWGSFIH AGLAQPFIAT FDGEPVAALI
AFRFGEVATF LYGMSRTAHR EKMPNHLLQW EAIRWAKEQG CIVYDFWGSP DRLEPGDPMW
GVYRFKQGFG ARLVRTIGAW DFPVRGTMYW LYNIVKPWLM SVLRTRGHAQ TRALLE
//
