ID K4QTU8_STRDJ Unreviewed; 274 AA.
AC K4QTU8;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Lysine N-acyltransferase MbtK {ECO:0000256|ARBA:ARBA00020586};
DE AltName: Full=Mycobactin synthase protein K {ECO:0000256|ARBA:ARBA00031122};
GN ORFNames=BN159_2647 {ECO:0000313|EMBL:CCK27026.1};
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:CCK27026.1, ECO:0000313|Proteomes:UP000008043};
RN [1] {ECO:0000313|EMBL:CCK27026.1, 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 -!- FUNCTION: Acyltransferase required for the direct transfer of
CC medium- to long-chain fatty acyl moieties from a carrier protein (MbtL)
CC on to the epsilon-amino group of lysine residue in the mycobactin core.
CC {ECO:0000256|ARBA:ARBA00003818}.
CC -!- PATHWAY: Siderophore biosynthesis; mycobactin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005102}.
CC -!- SIMILARITY: Belongs to the lysine N-acyltransferase MbtK family.
CC {ECO:0000256|ARBA:ARBA00009893}.
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DR EMBL; HE971709; CCK27026.1; -; Genomic_DNA.
DR RefSeq; WP_015657418.1; NC_020504.1.
DR AlphaFoldDB; K4QTU8; -.
DR STRING; 1214101.BN159_2647; -.
DR KEGG; sdv:BN159_2647; -.
DR PATRIC; fig|1214101.3.peg.2688; -.
DR eggNOG; COG1670; Bacteria.
DR HOGENOM; CLU_039848_2_1_11; -.
DR OrthoDB; 9087497at2; -.
DR UniPathway; UPA00011; -.
DR Proteomes; UP000008043; Chromosome.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR GO; GO:0019290; P:siderophore biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.630.30; -; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR019432; Acyltransferase_MbtK/IucB-like.
DR InterPro; IPR000182; GNAT_dom.
DR PANTHER; PTHR31438; LYSINE N-ACYLTRANSFERASE C17G9.06C-RELATED; 1.
DR PANTHER; PTHR31438:SF1; LYSINE N-ACYLTRANSFERASE C17G9.06C-RELATED; 1.
DR Pfam; PF13523; Acetyltransf_8; 1.
DR SMART; SM01006; AlcB; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR PROSITE; PS51186; GNAT; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW Reference proteome {ECO:0000313|Proteomes:UP000008043}.
FT DOMAIN 104..269
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 57..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 274 AA; 28612 MW; 15B3AD3D18492FEB CRC64;
MAPNDASTDA GIDPAASVST DTAPGAHPGG DSEDTLDLRL PEEFFALIAA TEEAVIEAGD
GGGGGGGGAG TATLTQPATA PPSGDDLLDS VVDWGPIKTA AGMLHLVPVR VERDLPLISR
WMNDPAVTAF WELAGPPSVT EEHVRSQLDG DGRSVPCVGV LDGTPMSYWE IYRADLDPLA
RHYPARPHDT GIHLLIGDVA DRGRGLGSAL LRAVADCALD RRLACARVIA EPDLRNTPSV
AAFLSAGFRF AAEVDLPAKQ AALMVRDRAL RDLL
//
