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Database: UniProt
Entry: F2RGI0_STRVP
LinkDB: F2RGI0_STRVP
Original site: F2RGI0_STRVP 
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}.
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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
//
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