ID M0GZB2_HALL2 Unreviewed; 339 AA.
AC M0GZB2;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=BioF2-like acetyltransferase domain-containing protein {ECO:0000259|Pfam:PF13480};
GN ORFNames=C456_02211 {ECO:0000313|EMBL:ELZ77540.1};
OS Haloferax lucentense (strain DSM 14919 / JCM 9276 / NCIMB 13854 / Aa 2.2)
OS (Haloferax alicantei).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=1230452 {ECO:0000313|EMBL:ELZ77540.1, ECO:0000313|Proteomes:UP000011535};
RN [1] {ECO:0000313|EMBL:ELZ77540.1, ECO:0000313|Proteomes:UP000011535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14919 / CCM 7023 / CIP 107410 / JCM 9276 / NCIMB 13854 / Aa
RC 2.2 {ECO:0000313|Proteomes:UP000011535};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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:ELZ77540.1}.
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DR EMBL; AOLH01000003; ELZ77540.1; -; Genomic_DNA.
DR RefSeq; WP_004061824.1; NZ_AOLH01000003.1.
DR AlphaFoldDB; M0GZB2; -.
DR PATRIC; fig|1230452.3.peg.422; -.
DR Proteomes; UP000011535; Unassembled WGS sequence.
DR GO; GO:0016755; F:aminoacyltransferase activity; IEA:InterPro.
DR GO; GO:0044038; P:cell wall macromolecule biosynthetic process; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; 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 169..305
FT /note="BioF2-like acetyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13480"
SQ SEQUENCE 339 AA; 38539 MW; 0D6A1F0329569705 CRC64;
MSIEVRRATG DDVHGWDAFV EQSPHGNAFH QYDALEIQAA HAGAELVPLV GRKGEEVVGL
FPVFRINKGP IATVFSPPPE LRVASLGPVL LNMDHMKQRK REGRHHEFID DCLAWVRDEI
RPRYAHIRLD GRYDDLRAFS WNDYAITPQY TYHVDLSPGV DDVFMSFSSD ARSNIRNAPD
DAYTIEEGGP EAIERIVEQV ASRYEAQGIS YRSSPEFVTD LYATLPEGQI RPYVLRIDGE
FAGGILAVDY KETVSRWQGG VRADVDSDLA INDLLDWRIM RDAMDRGRTT YDLVGANNRR
INRYKAKFNP ELHPFYSLER NAPGMKTLAH LYKTIREGV
//
