ID K4R925_STRDJ Unreviewed; 414 AA.
AC K4R925;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=UPF0256 protein {ECO:0000313|EMBL:CCK29189.1};
GN ORFNames=BN159_4810 {ECO:0000313|EMBL:CCK29189.1};
OS Streptomyces davaonensis (strain DSM 101723 / JCM 4913 / KCC S-0913 / 768).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1214101 {ECO:0000313|EMBL:CCK29189.1, ECO:0000313|Proteomes:UP000008043};
RN [1] {ECO:0000313|EMBL:CCK29189.1, ECO:0000313|Proteomes:UP000008043}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 101723 / JCM 4913 / KCC S-0913 / 768
RC {ECO:0000313|Proteomes:UP000008043};
RX PubMed=23043000; DOI=10.1128/JB.01592-12;
RA Jankowitsch F., Schwarz J., Ruckert C., Gust B., Szczepanowski R., Blom J.,
RA Pelzer S., Kalinowski J., Mack M.;
RT "Genome sequence of the bacterium Streptomyces davawensis JCM 4913 and
RT heterologous production of the unique antibiotic roseoflavin.";
RL J. Bacteriol. 194:6818-6827(2012).
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}.
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DR EMBL; HE971709; CCK29189.1; -; Genomic_DNA.
DR RefSeq; WP_015659531.1; NC_020504.1.
DR AlphaFoldDB; K4R925; -.
DR STRING; 1214101.BN159_4810; -.
DR KEGG; sdv:BN159_4810; -.
DR PATRIC; fig|1214101.3.peg.4874; -.
DR eggNOG; COG4552; Bacteria.
DR HOGENOM; CLU_050659_0_0_11; -.
DR OrthoDB; 8399956at2; -.
DR Proteomes; UP000008043; Chromosome.
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}; Reference proteome {ECO:0000313|Proteomes:UP000008043};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01812}.
FT DOMAIN 7..158
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 414 AA; 45735 MW; D315CBBE00DDA2CA CRC64;
MTRAADIDVR PITEAELAGW HRAVNTGFLR EPTLSEEQLA ARDPWFVPGR LLGAFDRDRC
VATFRSFDQR LTTVGGTAVP SDAITNVTVS PTHRRRGLLS RMMERDLTAA KERGDAVATL
IAAEYPIYGR YGFGPATTMA EWTIDVPRTG LDPRWSGPED GGRIDLIDAP DVRKLGPELH
ERLRRTQPGA VSRDDLWWQL TTGAVRFFNT FKEPHYAVYR SQSGEVEGMV AYTSDDHWGD
GKQPLNTATV KWLIGVTPAA ERALWQYLCS IDWITTVKTG WRAPDDLLPH FLPDPRAARI
TSQADWMWVR ILDVVRAMEA RTYAGAGSVV LDVVDGGGRY RLEAAADGTG ACAATTDTAD
LGITLSDLAT LWLGDESAVR LAALGRVREE RAGAARVADA LLRTSRRPWC PDLF
//
