ID A0A2B2BWE9_9BACI Unreviewed; 380 AA.
AC A0A2B2BWE9;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=Acyltransferase {ECO:0000313|EMBL:PFP24261.1};
GN ORFNames=COJ96_23405 {ECO:0000313|EMBL:PFP24261.1};
OS Bacillus sp. AFS073361.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=2033511 {ECO:0000313|EMBL:PFP24261.1, ECO:0000313|Proteomes:UP000223997};
RN [1] {ECO:0000313|EMBL:PFP24261.1, ECO:0000313|Proteomes:UP000223997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AFS073361 {ECO:0000313|EMBL:PFP24261.1,
RC ECO:0000313|Proteomes:UP000223997};
RG Agbiome Team Llc;
RA Bleich R.M., Grubbs K.J., Santa Maria K.C., Allen S.E., Farag S.,
RA Shank E.A., Bowers A.;
RT "Large-scale bioinformatics analysis of Bacillus genomes uncovers conserved
RT roles of natural products in bacterial physiology.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the acyltransferase 3 family.
CC {ECO:0000256|ARBA:ARBA00007400}.
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:PFP24261.1}.
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DR EMBL; NUZU01000042; PFP24261.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B2BWE9; -.
DR OrthoDB; 9807022at2; -.
DR Proteomes; UP000223997; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR InterPro; IPR002656; Acyl_transf_3_dom.
DR PANTHER; PTHR40074; O-ACETYLTRANSFERASE WECH; 1.
DR PANTHER; PTHR40074:SF2; O-ACETYLTRANSFERASE WECH; 1.
DR Pfam; PF01757; Acyl_transf_3; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000313|EMBL:PFP24261.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000223997};
KW Transferase {ECO:0000313|EMBL:PFP24261.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 57..78
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 99..118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 173..192
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 198..223
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 244..266
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 278..297
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 309..328
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 334..359
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 18..356
FT /note="Acyltransferase 3"
FT /evidence="ECO:0000259|Pfam:PF01757"
SQ SEQUENCE 380 AA; 45061 MW; A3A19A308E16EE84 CRC64;
MMKKKNEFQF SKKMTSQAKG LAILLMVYHH LFTFPDRISS VDYAPLMMFN GQPLDQLIGA
FGKICVSIFL FTSGYGLYQN FLKNNSFTFK VSLKKIIQFL KTYWIIFIIF IPIGLIWFHN
QPRYVFNLKN FLLNFTSLTN TYNREWWFVP LYLELIIIFP ILIKLIEKIP LIVNYLSFIS
LFFAGFFQNA ILLFPNNILI QLLMNHLSVL LLWQVVFIVG IYFSKYSVFE KINQFLNRLK
LENILFYLIV LFICFYIRQF TLPWIIEVRG AKISGIYTYA DFILTPILIF SFVKIVSYTN
IFSKLFATLG KHSNNIWLTH TFFIYYYYQK IIFLPYFSIL IVGWVFILTI VVSICVNFIS
NKINFLDIKK QSTVNKSLLH
//
