ID A0A0P6X7D0_9CHLR Unreviewed; 331 AA.
AC A0A0P6X7D0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=BioF2-like acetyltransferase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=ADN00_18530 {ECO:0000313|EMBL:KPL70053.1};
OS Ornatilinea apprima.
OC Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC Ornatilinea.
OX NCBI_TaxID=1134406 {ECO:0000313|EMBL:KPL70053.1, ECO:0000313|Proteomes:UP000050417};
RN [1] {ECO:0000313|EMBL:KPL70053.1, ECO:0000313|Proteomes:UP000050417}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P3M-1 {ECO:0000313|EMBL:KPL70053.1,
RC ECO:0000313|Proteomes:UP000050417};
RA Hemp J., Ward L.M., Pace L.A., Fischer W.W.;
RT "Genome sequence of Ornatilinea apprima DSM 23815.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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:KPL70053.1}.
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DR EMBL; LGCL01000045; KPL70053.1; -; Genomic_DNA.
DR RefSeq; WP_075064531.1; NZ_LGCL01000045.1.
DR AlphaFoldDB; A0A0P6X7D0; -.
DR STRING; 1134406.ADN00_18530; -.
DR OrthoDB; 9785911at2; -.
DR Proteomes; UP000050417; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000050417}.
SQ SEQUENCE 331 AA; 37891 MW; EE988E813B93C821 CRC64;
MPELTFSEWD QFLTQYPQAH VLQTSAWGIL KSKFSWQAVP VVSGLAGALV LFRRLPLGFS
IAYIPKGPLG DNWNDLWPEI DRACRRRRAI FLQVEPDAFE PASASLLERL SGFKQVEKTI
QPRQTIVVSL EGGEEDWLQR MKQKTRYNVR LAAKKEVVVR ETNDVAQFHA LMSTTGERDQ
FGVHSLAYYQ AAYDLFSARG ECALLQAEYA GKPLAAVMVF ARGKRSWYFY GASSNEERNR
MPAYLVQWEA MRWASARGCS EYDLWGIPDL PEETLEADFT QREDGLWSVY RFKRGFGGQI
HRSTGAWDRV YMPLLYRAYQ IAARARSGGE N
//
