ID F2RGI0_STRVP Unreviewed; 189 AA.
AC F2RGI0;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, 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 OrderedLocusNames=SVEN_1504 {ECO:0000313|EMBL:CCA54791.1};
OS Streptomyces venezuelae (strain ATCC 10712 / CBS 650.69 / DSM 40230 / JCM
OS 4526 / NBRC 13096 / PD 04745).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=953739 {ECO:0000313|EMBL:CCA54791.1, ECO:0000313|Proteomes:UP000006854};
RN [1] {ECO:0000313|EMBL:CCA54791.1, ECO:0000313|Proteomes:UP000006854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10712 {ECO:0000313|EMBL:CCA54791.1};
RX PubMed=21463507; DOI=10.1186/1471-2164-12-175;
RA Pullan S.T., Bibb M.J., Merrick M.;
RT "Genome-wide analysis of the role of GlnR in Streptomyces venezuelae
RT provides new insights into global nitrogen regulation in actinomycetes.";
RL BMC Genomics 12:175-175(2011).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FR845719; CCA54791.1; -; Genomic_DNA.
DR RefSeq; WP_015032709.1; NZ_JABVZO010000341.1.
DR AlphaFoldDB; F2RGI0; -.
DR STRING; 953739.SVEN_1504; -.
DR GeneID; 69863686; -.
DR KEGG; sve:SVEN_1504; -.
DR PATRIC; fig|953739.5.peg.3616; -.
DR eggNOG; COG1670; Bacteria.
DR HOGENOM; CLU_039848_5_0_11; -.
DR OrthoDB; 5177616at2; -.
DR UniPathway; UPA00011; -.
DR Proteomes; UP000006854; 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:UP000006854};
KW Transferase {ECO:0000313|EMBL:CCA54791.1}.
FT DOMAIN 18..182
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 189 AA; 20929 MW; 288C1A30785D93FE CRC64;
MTTATAAYVH RIEGFGTVTV RPVEPERDAP LLHAWVNEER SRFWGMVGTT VEQVRDVYAH
LDSLTTHHGF LVSLDGEPVA LLQTYDPEAD RVSECYEVEP GDVGAHFLVA PNPAPRPGFT
GMLLTALIAF ALKDRTRLVV EPDAANEKAI ARMVRAGFEL GPEVVLPEVD LPEVFIPEKK
ARLAFLTRR
//