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Database: UniProt
Entry: D4U132_9ACTO
LinkDB: D4U132_9ACTO
Original site: D4U132_9ACTO 
ID   D4U132_9ACTO            Unreviewed;       341 AA.
AC   D4U132;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=BioF2-like acetyltransferase domain-containing protein {ECO:0000259|Pfam:PF13480};
GN   ORFNames=HMPREF0970_01931 {ECO:0000313|EMBL:EFF79130.1};
OS   Schaalia odontolytica F0309.
OC   Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC   Schaalia.
OX   NCBI_TaxID=649742 {ECO:0000313|EMBL:EFF79130.1, ECO:0000313|Proteomes:UP000003150};
RN   [1] {ECO:0000313|EMBL:EFF79130.1, ECO:0000313|Proteomes:UP000003150}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0309 {ECO:0000313|EMBL:EFF79130.1,
RC   ECO:0000313|Proteomes:UP000003150};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (OCT-2009) 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:EFF79130.1}.
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DR   EMBL; ACYT02000073; EFF79130.1; -; Genomic_DNA.
DR   RefSeq; WP_003796474.1; NZ_GG753641.1.
DR   AlphaFoldDB; D4U132; -.
DR   PATRIC; fig|649742.3.peg.1677; -.
DR   HOGENOM; CLU_050488_0_0_11; -.
DR   OrthoDB; 3185680at2; -.
DR   Proteomes; UP000003150; 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}.
FT   DOMAIN          157..289
FT                   /note="BioF2-like acetyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF13480"
SQ   SEQUENCE   341 AA;  38385 MW;  087753390046246C CRC64;
     MTTTALVPIS QEDKIAAVSG FQDRSLPIEQ TCVWEAFEES QGHGVWGRYA WCEDDSKVAF
     ITLYKYSVRG VHYLWAKWGP AWVKEATPER EAALRADLLR EIKAKDKTVA FVRLHAIYQH
     PDLCMPLQTI SYDRTVVIDT SGKTEEAILA AMPKAGKRSI RSGLKKGKAE GVTFHEDTAN
     AEAVIDEYYA VMEETAKRDG FRPHPKEYYL SLLQTLGPKH ARIFSMRDAD GNILCWDFCL
     VEGIRAQAEY GASTEAGRRL RQPPVLDFLA AEFLARDGVR EFDLMGAHSP RCPDLYSVGK
     YKSAFATQFT DVPGGWDMPI KKSTYRAMIA AKAVKDWRAR S
//
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