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Database: UniProt
Entry: A0A0S7C6J3_9BACT
LinkDB: A0A0S7C6J3_9BACT
Original site: A0A0S7C6J3_9BACT 
ID   A0A0S7C6J3_9BACT        Unreviewed;       311 AA.
AC   A0A0S7C6J3;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Protein containing acetyltransferase (GNAT) domain {ECO:0000313|EMBL:GAP44976.1};
GN   ORFNames=TBC1_12792 {ECO:0000313|EMBL:GAP44976.1};
OS   Lentimicrobium saccharophilum.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Lentimicrobiaceae;
OC   Lentimicrobium.
OX   NCBI_TaxID=1678841 {ECO:0000313|EMBL:GAP44976.1};
RN   [1] {ECO:0000313|EMBL:GAP44976.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TBC1 {ECO:0000313|EMBL:GAP44976.1};
RA   Tourlousse D.M., Matsuura N., Sun L., Toyonaga M., Kuroda K., Ohashi A.,
RA   Cruz R., Yamaguchi T., Sekiguchi Y.;
RT   "Draft Genome Sequence of Bacteroidales Strain TBC1, a Novel Isolate from a
RT   Methanogenic Wastewater Treatment System.";
RL   Genome Announc. 3:e01168-15(2015).
CC   -!- SIMILARITY: Belongs to the FemABX family.
CC       {ECO:0000256|ARBA:ARBA00009943}.
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DR   EMBL; DF968183; GAP44976.1; -; Genomic_DNA.
DR   RefSeq; WP_062044972.1; NZ_DF968183.1.
DR   AlphaFoldDB; A0A0S7C6J3; -.
DR   STRING; 1678841.TBC1_12792; -.
DR   OrthoDB; 9773932at2; -.
DR   Proteomes; UP000053091; 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); 1.
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:UP000053091};
KW   Transferase {ECO:0000313|EMBL:GAP44976.1}.
FT   DOMAIN          113..241
FT                   /note="BioF2-like acetyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF13480"
SQ   SEQUENCE   311 AA;  36029 MW;  666B231F7E4E95E7 CRC64;
     MSVKWPLIYQ HAGPVGWYRV KTVTGDRFMM MVNMDDILVS MPYFSYAHFS DQEPELVEKH
     PEFTLEEGKL QCSDPAIQWH VRMLKPVSGH FHTVKVVSWL PLETTAEKQL LRFSSNLRRK
     INKSVSREIK LEVGGSELIG KFYGVFSHNM HRLGAPAMSK SFYARVVTAF GRDASVLIAL
     YHGKAIGGAI LLKKGEFAET CWFSTLEDYN PFYTSYFLWW ECIRLSIERG CKVFSFGRST
     KDSGPHLYKQ QWGVKNTTLY WSFSYPLRND QYTIGPLKIP MPNRKILSFL WKISPCFIIR
     WLGPMVAGKF Y
//
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