ID H0Q465_9RHOO Unreviewed; 345 AA.
AC H0Q465;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=BioF2-like acetyltransferase domain-containing protein {ECO:0000259|Pfam:PF13480};
GN ORFNames=AZKH_3619 {ECO:0000313|EMBL:BAL25904.1};
OS Azoarcus sp. KH32C.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Azoarcus.
OX NCBI_TaxID=748247 {ECO:0000313|EMBL:BAL25904.1, ECO:0000313|Proteomes:UP000007106};
RN [1] {ECO:0000313|EMBL:BAL25904.1, ECO:0000313|Proteomes:UP000007106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KH32C {ECO:0000313|EMBL:BAL25904.1,
RC ECO:0000313|Proteomes:UP000007106};
RA Nishizawa T., Tago T., Oshima K., Hattori M., Ishii S., Otsuka S.,
RA Senoo K.;
RT "Complete genome sequence of Azoarcus sp. KH32C.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the FemABX family.
CC {ECO:0000256|ARBA:ARBA00009943}.
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DR EMBL; AP012304; BAL25904.1; -; Genomic_DNA.
DR RefSeq; WP_015437206.1; NC_020516.1.
DR AlphaFoldDB; H0Q465; -.
DR STRING; 748247.AZKH_3619; -.
DR KEGG; aza:AZKH_3619; -.
DR PATRIC; fig|748247.4.peg.3579; -.
DR eggNOG; COG2348; Bacteria.
DR HOGENOM; CLU_042156_0_0_4; -.
DR OrthoDB; 9773932at2; -.
DR Proteomes; UP000007106; Chromosome.
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 InterPro; IPR017469; PEP-CTERM_FemAB-rel.
DR NCBIfam; TIGR03019; pepcterm_femAB; 1.
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:UP000007106}.
FT DOMAIN 154..281
FT /note="BioF2-like acetyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13480"
SQ SEQUENCE 345 AA; 39233 MW; DC2960FD52EA3743 CRC64;
MDRPSVVVKQ LSAGDRARWD AFVRACPEAT FFHLSAWEGI VREVFRHRTF FLFAERAGEI
IGVLPLAEVR SRLFGHALTS LPFCVYGGIA GFAEAVAPLE AEAEAIARRL GVQHLELRNV
MARHADWPRQ DLYVTFRKPI HADDDANMRE IPRKQRAMVR KGIANGLASE IDGDVERFFA
LYADNVHRHG TPALPKAFFA RLLKEFGPDC EVLTVTDSAG RPLSSVLSFY FRDEVLPYYA
GDAEAARELA ANDFKYWELM RRAAARGYRL FDFGRSKVGT GSFSFKKNWG FVPQPLSYEY
RLYKRDEVPQ NNPLNPKYRA FIALWRRLPR PVANALGPHI VRNLG
//
