ID A0A1A2B8J2_9MYCO Unreviewed; 412 AA.
AC A0A1A2B8J2;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Acetyltransferase {ECO:0000313|EMBL:OBF64747.1};
GN ORFNames=A5753_02265 {ECO:0000313|EMBL:OBF64747.1};
OS Mycobacterium sp. 852002-51971_SCH5477799-a.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1834106 {ECO:0000313|EMBL:OBF64747.1, ECO:0000313|Proteomes:UP000091887};
RN [1] {ECO:0000313|EMBL:OBF64747.1, ECO:0000313|Proteomes:UP000091887}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=852002-51971_SCH5477799-a {ECO:0000313|EMBL:OBF64747.1,
RC ECO:0000313|Proteomes:UP000091887};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Homohexamer; trimer of dimers. {ECO:0000256|HAMAP-
CC Rule:MF_01812}.
CC -!- SIMILARITY: Belongs to the acetyltransferase Eis family.
CC {ECO:0000256|ARBA:ARBA00009213, ECO:0000256|HAMAP-Rule:MF_01812}.
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:OBF64747.1}.
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DR EMBL; LZIF01000086; OBF64747.1; -; Genomic_DNA.
DR RefSeq; WP_067127998.1; NZ_LZIF01000086.1.
DR AlphaFoldDB; A0A1A2B8J2; -.
DR STRING; 1834106.A5753_02265; -.
DR OrthoDB; 8399956at2; -.
DR Proteomes; UP000091887; Unassembled WGS sequence.
DR GO; GO:0044161; C:host cell cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0008080; F:N-acetyltransferase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.630.30; -; 2.
DR Gene3D; 3.30.1050.10; SCP2 sterol-binding domain; 1.
DR HAMAP; MF_01812; Eis; 1.
DR InterPro; IPR041380; Acetyltransf_17.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR025559; Eis_dom.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR022902; NAcTrfase_Eis.
DR InterPro; IPR036527; SCP2_sterol-bd_dom_sf.
DR PANTHER; PTHR37817; N-ACETYLTRANSFERASE EIS; 1.
DR PANTHER; PTHR37817:SF1; N-ACETYLTRANSFERASE EIS; 1.
DR Pfam; PF17668; Acetyltransf_17; 1.
DR Pfam; PF13527; Acetyltransf_9; 1.
DR Pfam; PF13530; SCP2_2; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF55718; SCP-like; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315, ECO:0000256|HAMAP-
KW Rule:MF_01812}; Host cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00022488};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01812}.
FT DOMAIN 8..157
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 412 AA; 45146 MW; B988C4726321D5F5 CRC64;
MDEKGDSTNI RHPTEDDWQS VFENQARAFG DPVGPEDLEA WRSRVSLDNI LIAEDVSDPE
HPNLVGTSII YPSRLTVPGG ANLRVAWLTM IAVASTHQGK GLWAQLSAQG LGILLDRGYP
VVCGVPTQTA MYDGFGAGVS SYSHTYSIDR RFAKLRDAPS RIRGREVNAA EARRRLPEIY
ERWCAATPGT ISRDDAWWAD YLDDRPTQRG NGSALHYTIH PDGFLTYRVV GSQQHAFRPP
LGTVVVEDFC PITDEAHTEL LQTLLVLEMF YRIEVDVAAD DPLPLKLVDQ RAAETKGVSD
FLWVRINDVP ETLGARSYAA DADIVLEVTD PLGLAGGTFA LHSHDGIGKC TPHDGSPDIK
IGLADLATVY MGAHRASQLA RANRITEARQ GALRELDAAF GTDRTPYTGT VL
//
