ID   MBTK_MYCSS              Reviewed;         244 AA.
AC   Q1BBA4;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Lysine N-acyltransferase MbtK;
DE            Short=N-acyltransferase MbtK;
DE            EC=2.3.1.-;
DE   AltName: Full=Mycobactin synthase protein K;
GN   Name=mbtK; OrderedLocusNames=Mmcs_1721;
OS   Mycobacterium sp. (strain MCS).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; unclassified Mycobacterium.
OX   NCBI_TaxID=164756;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCS;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Miller C.D., Hughes J.E., Anderson A.J., Sims R.C., Richardson P.;
RT   "Complete sequence of chromosome of Mycobacterium sp. MCS.";
RL   Submitted (JUN-2006) 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:0000250}.
CC   -!- PATHWAY: Siderophore biosynthesis; mycobactin biosynthesis.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the lysine N-acyltransferase MbtK family.
CC       {ECO:0000305}.
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DR   EMBL; CP000384; ABG07830.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1BBA4; -.
DR   SMR; Q1BBA4; -.
DR   KEGG; mmc:Mmcs_1721; -.
DR   HOGENOM; CLU_039848_4_0_11; -.
DR   OMA; MALYALH; -.
DR   UniPathway; UPA00011; -.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0019290; P:siderophore biosynthetic process; IEA:InterPro.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR019432; Acyltransferase_MbtK/IucB-like.
DR   SMART; SM01006; AlcB; 1.
DR   SUPFAM; SSF55729; SSF55729; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Transferase.
FT   CHAIN           1..244
FT                   /note="Lysine N-acyltransferase MbtK"
FT                   /id="PRO_0000278303"
FT   REGION          224..244
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        184
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255"
FT   BINDING         146
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   244 AA;  27271 MW;  33A382A88DB59D50 CRC64;
     MQHRDVGKPT LSYSGRLIAQ MTEIDEALKP VLPRELTTVS DEVRAVPAPP LPVLAEPFAL
     RPADPDADAE MISEWMNRPH LVEAWEYPWP PQRWRRHLKA QIDGEYSRPL IGSFKGADVV
     YVELYRAAKD SIAPRYAADP HDIGIHAAIA DLRFVNRGFA PLLLPRVVAS VFEIDPRCRR
     IMFDPDHRNT GARRVCEFAG CTFLGEHDMA NRRMALYALP RTPADAPPTG DLQSSPVGES
     ISSS