ID   IUCB_ECOLX              Reviewed;         315 AA.
AC   Q47317;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=N(6)-hydroxylysine O-acetyltransferase;
DE            EC=2.3.1.102 {ECO:0000269|PubMed:3521734};
DE   AltName: Full=N(6)-hydroxylysine acetylase;
GN   Name=iucB;
OS   Escherichia coli.
OG   Plasmid IncFI ColV3-K30.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8003107; DOI=10.1006/jmbi.1994.1290;
RA   Martinez J.L., Herrero M., de Lorenzo V.;
RT   "The organization of intercistronic regions of the aerobactin operon of
RT   pColV-K30 may account for the differential expression of the iucABCD iutA
RT   genes.";
RL   J. Mol. Biol. 238:288-293(1994).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-7, FUNCTION, CATALYTIC ACTIVITY, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=3521734; DOI=10.1021/bi00357a030;
RA   Coy M., Paw B.H., Bindereif A., Neilands J.B.;
RT   "Isolation and properties of N epsilon-hydroxylysine:acetyl coenzyme A N
RT   epsilon-transacetylase from Escherichia coli pABN11.";
RL   Biochemistry 25:2485-2489(1986).
RN   [3]
RP   FUNCTION IN AEROBACTIN BIOSYNTHESIS, AND NOMENCLATURE.
RX   PubMed=2935523; DOI=10.1128/jb.165.2.570-578.1986;
RA   de Lorenzo V., Bindereif A., Paw B.H., Neilands J.B.;
RT   "Aerobactin biosynthesis and transport genes of plasmid ColV-K30 in
RT   Escherichia coli K-12.";
RL   J. Bacteriol. 165:570-578(1986).
CC   -!- FUNCTION: Catalyzes the transfer of acetyl from acetyl-CoA to the N-
CC       hydroxylysine. Involved in the biosynthesis of the siderophore
CC       aerobactin which is a chelator that mediates the high-affinity iron
CC       transport systems induced under iron-stressed conditions.
CC       {ECO:0000269|PubMed:2935523, ECO:0000269|PubMed:3521734}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + N(6)-hydroxy-L-lysine = CoA + N(6)-acetyl-N(6)-
CC         hydroxy-L-lysine; Xref=Rhea:RHEA:22388, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57288, ChEBI:CHEBI:57820, ChEBI:CHEBI:58122;
CC         EC=2.3.1.102; Evidence={ECO:0000269|PubMed:3521734};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.043 mM for N(6)-hydroxy-L-lysine {ECO:0000269|PubMed:3521734};
CC         KM=0.079 mM for N(5)-hydroxy-L-ornithine
CC         {ECO:0000269|PubMed:3521734};
CC         KM=0.099 mM for 1-amino-5-(hydroxyamino)pentane
CC         {ECO:0000269|PubMed:3521734};
CC         KM=0.101 mM for N-methylhydroxylamine {ECO:0000269|PubMed:3521734};
CC         KM=1.8 mM for hydroxylamine {ECO:0000269|PubMed:3521734};
CC       pH dependence:
CC         Optimum pH is 7. {ECO:0000269|PubMed:3521734};
CC       Temperature dependence:
CC         Optimum temperature is 40 degrees Celsius.
CC         {ECO:0000269|PubMed:3521734};
CC   -!- PATHWAY: Siderophore biosynthesis; aerobactin biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the IucB family. {ECO:0000305}.
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DR   EMBL; X76100; CAA53708.1; -; Genomic_DNA.
DR   PIR; S44019; S44019.
DR   AlphaFoldDB; Q47317; -.
DR   SMR; Q47317; -.
DR   KEGG; ag:CAA53708; -.
DR   BioCyc; MetaCyc:MON-11591; -.
DR   UniPathway; UPA00014; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0050133; F:N6-hydroxylysine O-acetyltransferase activity; IMP:UniProtKB.
DR   GO; GO:0019270; P:aerobactin biosynthetic process; IMP:UniProtKB.
DR   GO; GO:0055072; P:iron ion homeostasis; IMP:UniProtKB.
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   1: Evidence at protein level;
KW   Cell membrane; Cytoplasm; Direct protein sequencing; Membrane; Plasmid;
KW   Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:3521734"
FT   CHAIN           2..315
FT                   /note="N(6)-hydroxylysine O-acetyltransferase"
FT                   /id="PRO_0000084275"
SQ   SEQUENCE   315 AA;  37029 MW;  E438853056E61729 CRC64;
     MSGPNIVHSG YGLRCEKLDK PLNLGWGLDN SAVLHWPGEL PTGWLCDALD QIFIAAPQLS
     AVVLPWSEWC EEPQALTLFG QVQSDIIHRS AFWQLPLWLS SPANRASGEM VFDAEREIYF
     PQRPPRPQGE VYRRYDPRIR RMLSFRIADP VSDAERFTRW MNDPRVEYFW EQSGSLEVQI
     AYLERQLTSK HAFPLIGCFD DRPVSNIEIY WAAEDRIGRH YSWQPFDRGL HLLVGEQQWR
     GAHYVQSWLR GVTHYLLLNE PRTQRTVLEP RTDNQRLFRH LEPAGYRTIK EFDFPHKRSR
     MVMADRHHFF TEVGL