ID   ORF5_STRGR              Reviewed;         416 AA.
AC   Q54238;
DT   11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Uncharacterized N-acetyltransferase ORF5 {ECO:0000255|HAMAP-Rule:MF_01812};
DE            EC=2.3.1.- {ECO:0000255|HAMAP-Rule:MF_01812};
OS   Streptomyces griseus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=IFO 13350 / CBS 651.72;
RX   PubMed=7592414; DOI=10.1128/jb.177.22.6401-6410.1995;
RA   Kudo N., Kimura M., Beppu T., Horinouchi S.;
RT   "Cloning and characterization of a gene involved in aerial mycelium
RT   formation in Streptomyces griseus.";
RL   J. Bacteriol. 177:6401-6410(1995).
CC   -!- SUBUNIT: Homohexamer; trimer of dimers. {ECO:0000255|HAMAP-
CC       Rule:MF_01812}.
CC   -!- SIMILARITY: Belongs to the acetyltransferase Eis family.
CC       {ECO:0000255|HAMAP-Rule:MF_01812}.
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DR   EMBL; D63706; BAA09837.1; -; Genomic_DNA.
DR   RefSeq; WP_012380280.1; NZ_UAVD01000012.1.
DR   AlphaFoldDB; Q54238; -.
DR   SMR; Q54238; -.
DR   GeneID; 6209377; -.
DR   PATRIC; fig|455632.4.peg.4048; -.
DR   OMA; RRPWCPD; -.
DR   GO; GO:0008080; F:N-acetyltransferase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.1050.10; -; 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   Pfam; PF17668; Acetyltransf_17; 1.
DR   Pfam; PF13530; SCP2_2; 1.
DR   SUPFAM; SSF55718; SSF55718; 1.
DR   SUPFAM; SSF55729; SSF55729; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Transferase.
FT   CHAIN           1..416
FT                   /note="Uncharacterized N-acetyltransferase ORF5"
FT                   /id="PRO_0000220267"
FT   DOMAIN          3..150
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01812"
FT   ACT_SITE        124
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01812"
FT   ACT_SITE        416
FT                   /note="Proton acceptor; via carboxylate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01812"
FT   BINDING         83..85
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01812"
FT   BINDING         91..96
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01812"
SQ   SEQUENCE   416 AA;  44975 MW;  11F0CA64704A2A61 CRC64;
     MSLDVRTITP SESAEWMRAV STGFLTAGTP SEELVADRFA GADLSRTQGA FEAGRCVATF
     RSFAQELTVV GGATVAADAI SGVTVTPTHR RRGLLSRMMA TDLAAAKERG EPVASLIAAE
     YPIYGRYGFG PAAWTSVWEV SVYRAGLDAR RSGQPADGGR IEMVDGADVR KLGPEVHGAL
     AARQPGVVTR DERWWRQRTG AAPSSAHEKW TEPFYVVHRA ADGTVDGLMT YGTDDTWGDA
     KQPLNTASVR DMIALNPAAE RALWHYLCSI DWITTIRSGY RAPDDLLPLL LPDPRAARMI
     TNADWLWLRM LDVPRALEAR TYGTEASLVL EVRDDAGLAG GRFLLDASTG GARCVSTTRS
     ADLVLGVAEL ATLYLGDESV RRLVDLGRAE ESRAGAATTA DAVFRTGRRP WCPDVF