ID   C5F106_9HELI            Unreviewed;       337 AA.
AC   C5F106;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=BioF2-like acetyltransferase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=HPMG_01367 {ECO:0000313|EMBL:EEQ63910.1};
OS   Helicobacter pullorum MIT 98-5489.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=537972 {ECO:0000313|EMBL:EEQ63910.1};
RN   [1] {ECO:0000313|EMBL:EEQ63910.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=MIT 98-5489 {ECO:0000313|EMBL:EEQ63910.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Fox J.G., Shen Z., Charoenlap N., Schauer D.B., Ward D., Mehta T.,
RA   Young S., Jaffe D., Gnerre S., Berlin A., Heiman D., Hepburn T., Shea T.,
RA   Sykes S., Alvarado L., Kodira C., Borodovsky M., Lander E., Galagan J.,
RA   Nusbaum C., Birren B.;
RT   "Annotation of Helicobacter pullorum strain MIT 98-5489.";
RL   Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the FemABX family.
CC       {ECO:0000256|ARBA:ARBA00009943}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DS990444; EEQ63910.1; -; Genomic_DNA.
DR   AlphaFoldDB; C5F106; -.
DR   eggNOG; COG2348; Bacteria.
DR   HOGENOM; CLU_803209_0_0_7; -.
DR   Proteomes; UP000003953; 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; 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}.
SQ   SEQUENCE   337 AA;  39485 MW;  228D292B581B7DDD CRC64;
     MGLPMQILEL EAQLSIAYSQ FLNQCSGSMI YYSLPYKCLL EDFLKCNSRY LVVYDNGKIH
     GVLPLMYRKG KYGEILNSLP FYGSHGGILA TNDDAYDLLI EYYNSIVGNY ASANYISNPL
     VKYDGAKKPV YDFLDKRIGQ WTFLVEQNEL IKSFDSSATR NIYKAQCKNI EIIKTDSIEF
     LYKTHKANIS QLNGVYKEKE FFEKISKNFG SENYTIYIAL YDKIPIAALL LFYFGEIVEY
     YTPATLFEYR TLQALPLLIF NAMNEAFEKG YKMWNWGGTW KSQEGVYRFK KKFGAKEREY
     KYYVKINNKE ILDASREELL KEYPYFYVIP FEKLNRV
//