ID A0A069JXV6_9ACTN Unreviewed; 241 AA.
AC A0A069JXV6;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Lysine N-acyltransferase MbtK {ECO:0000256|ARBA:ARBA00020586};
DE AltName: Full=Mycobactin synthase protein K {ECO:0000256|ARBA:ARBA00031122};
GN ORFNames=DT87_22735 {ECO:0000313|EMBL:KDQ69904.1};
OS Streptomyces sp. NTK 937.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1487711 {ECO:0000313|EMBL:KDQ69904.1, ECO:0000313|Proteomes:UP000027475};
RN [1] {ECO:0000313|EMBL:KDQ69904.1, ECO:0000313|Proteomes:UP000027475}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NTK 937 {ECO:0000313|EMBL:KDQ69904.1,
RC ECO:0000313|Proteomes:UP000027475};
RA Olano C., Cano-Prieto C., Losada A., Mendez C., Salas J.A.;
RT "Draft genome sequence of marine actinomycete Streptomyces sp. NTK 937,
RT producer of the benzoxazol antibiotic caboxamycin.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KDQ69904.1}.
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DR EMBL; JJOB01000001; KDQ69904.1; -; Genomic_DNA.
DR RefSeq; WP_028441199.1; NZ_JJOB01000001.1.
DR AlphaFoldDB; A0A069JXV6; -.
DR OrthoDB; 9087497at2; -.
DR UniPathway; UPA00011; -.
DR Proteomes; UP000027475; Unassembled WGS sequence.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
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}.
FT DOMAIN 84..236
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 39..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 241 AA; 26041 MW; EF52EF3288D4F471 CRC64;
MHQADAHPDA AARAEPGDGA GAEDTLELRL TEELLAVLGD EPQPAGTRRD TSDLVGDPAS
WRPAATPAGE FRLVPVELTR DLGVLTRWMN DPAVAAFWEL AGPESTTAGH LRRQLDGDGR
SVPCLGVLDG RPMSYWEIYR ADLDPLARHY PARPHDIGLH LLVGGVANRG RGIGTLLLKA
VADLVLDNHP RCARVVAEPD LRNTPSVAAF LGAGFRFSAE VELPDKRAAL MIRERAHRAQ
L
//