ID M0C587_9EURY Unreviewed; 353 AA.
AC M0C587;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=BioF2-like acetyltransferase domain-containing protein {ECO:0000259|Pfam:PF13480};
GN ORFNames=C477_11497 {ECO:0000313|EMBL:ELZ17833.1};
OS Haloterrigena salina JCM 13891.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Haloterrigena.
OX NCBI_TaxID=1227488 {ECO:0000313|EMBL:ELZ17833.1, ECO:0000313|Proteomes:UP000011657};
RN [1] {ECO:0000313|EMBL:ELZ17833.1, ECO:0000313|Proteomes:UP000011657}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 13891 {ECO:0000313|EMBL:ELZ17833.1,
RC ECO:0000313|Proteomes:UP000011657};
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:ELZ17833.1}.
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DR EMBL; AOIS01000037; ELZ17833.1; -; Genomic_DNA.
DR RefSeq; WP_008894598.1; NZ_AOIS01000037.1.
DR AlphaFoldDB; M0C587; -.
DR STRING; 1227488.C477_11497; -.
DR PATRIC; fig|1227488.3.peg.2284; -.
DR eggNOG; arCOG03319; Archaea.
DR OrthoDB; 135106at2157; -.
DR Proteomes; UP000011657; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000011657}.
FT DOMAIN 179..307
FT /note="BioF2-like acetyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13480"
SQ SEQUENCE 353 AA; 40810 MW; 69B0C87D1309160D CRC64;
MSALEPTLYR SIEPINENQW NNVVTQSDRG TVYQRYEWVR AIEEAFDYEP RHVVVEKSGN
PIALMPNFQV DLPVPDTVTE TLPVAPPLKQ LVSLPTGFGG PVVLTDEADA LDLLFDGLEE
TSERTVVNHA IETYDLEYVR YGQYLQTRGY DPSFDSCLFL IDLEDGWDAI LDGMDKGRRR
DIRKGNEQEY RIEIDPLGTD LETTYDWYVK NLKRVDGSPL PKAFFESLAD RLEDRLRVFR
AIIEGEEVGR YVYLLDDEGD VLHHWLSAIP DSDNYQYHPS ELLHERGIKW GIEQGYERYN
FGKTGSHFSN SVFRFKHKYG GTAVPVFKVE KGYSRVAWPL YQLGREKYVE KSL
//
