MBTK_MYCTU
ID MBTK_MYCTU Reviewed; 210 AA.
AC P9WK15; L0T804; P64819; Q11017;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 38.
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=Rv1347c; ORFNames=MTCY02B10.11c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP INDUCTION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=12065475; DOI=10.1128/iai.70.7.3371-3381.2002;
RA Rodriguez G.M., Voskuil M.I., Gold B., Schoolnik G.K., Smith I.;
RT "IdeR, an essential gene in Mycobacterium tuberculosis: role of IdeR in
RT iron-dependent gene expression, iron metabolism, and oxidative stress
RT response.";
RL Infect. Immun. 70:3371-3381(2002).
RN [3]
RP FUNCTION, ROLE IN MYCOBACTIN BIOSYNTHESIS, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=16461464; DOI=10.1073/pnas.0507924103;
RA Krithika R., Marathe U., Saxena P., Ansari M.Z., Mohanty D., Gokhale R.S.;
RT "A genetic locus required for iron acquisition in Mycobacterium
RT tuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:2069-2074(2006).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), AND SUBUNIT.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=15695811; DOI=10.1074/jbc.m413904200;
RA Card G.L., Peterson N.A., Smith C.A., Rupp B., Schick B.M., Baker E.N.;
RT "The crystal structure of Rv1347c, a putative antibiotic resistance protein
RT from Mycobacterium tuberculosis, reveals a GCN5-related fold and suggests
RT an alternative function in siderophore biosynthesis.";
RL J. Biol. Chem. 280:13978-13986(2005).
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:0000269|PubMed:16461464}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.72 uM for lauroyl-ACP {ECO:0000269|PubMed:16461464};
CC KM=19.50 uM for palmitoyl-CoA {ECO:0000269|PubMed:16461464};
CC KM=33.93 uM for lauroyl-CoA {ECO:0000269|PubMed:16461464};
CC KM=86.12 uM for decanoyl-CoA {ECO:0000269|PubMed:16461464};
CC KM=166.20 uM for hexanoyl-CoA {ECO:0000269|PubMed:16461464};
CC -!- PATHWAY: Siderophore biosynthesis; mycobactin biosynthesis.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15695811}.
CC -!- INDUCTION: Induced by iron starvation conditions. Transcriptionally
CC repressed by IdeR and iron. {ECO:0000269|PubMed:12065475}.
CC -!- SIMILARITY: Belongs to the lysine N-acyltransferase MbtK family.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP44105.1; -; Genomic_DNA.
DR PIR; B70740; B70740.
DR RefSeq; NP_215863.1; NC_000962.3.
DR RefSeq; WP_003406956.1; NZ_NVQJ01000031.1.
DR PDB; 1YK3; X-ray; 2.20 A; A/B/C/D/E/F/G/H=1-210.
DR PDBsum; 1YK3; -.
DR AlphaFoldDB; P9WK15; -.
DR SMR; P9WK15; -.
DR STRING; 83332.Rv1347c; -.
DR PaxDb; P9WK15; -.
DR DNASU; 886846; -.
DR GeneID; 45425325; -.
DR GeneID; 886846; -.
DR KEGG; mtu:Rv1347c; -.
DR TubercuList; Rv1347c; -.
DR eggNOG; COG1670; Bacteria.
DR OMA; MALYALH; -.
DR PhylomeDB; P9WK15; -.
DR BioCyc; MetaCyc:G185E-5526-MON; -.
DR SABIO-RK; P9WK15; -.
DR UniPathway; UPA00011; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0047617; F:acyl-CoA hydrolase activity; IDA:MTBBASE.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IDA:MTBBASE.
DR GO; GO:0016410; F:N-acyltransferase activity; IDA:MTBBASE.
DR GO; GO:0019540; P:catechol-containing siderophore biosynthetic process; TAS:MTBBASE.
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 3D-structure; Acyltransferase; Reference proteome; Transferase.
FT CHAIN 1..210
FT /note="Lysine N-acyltransferase MbtK"
FT /id="PRO_0000103819"
FT ACT_SITE 168
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 130
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT HELIX 26..29
FT /evidence="ECO:0007829|PDB:1YK3"
FT STRAND 43..47
FT /evidence="ECO:0007829|PDB:1YK3"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:1YK3"
FT HELIX 53..60
FT /evidence="ECO:0007829|PDB:1YK3"
FT HELIX 63..69
FT /evidence="ECO:0007829|PDB:1YK3"
FT HELIX 75..86
FT /evidence="ECO:0007829|PDB:1YK3"
FT STRAND 88..98
FT /evidence="ECO:0007829|PDB:1YK3"
FT STRAND 101..110
FT /evidence="ECO:0007829|PDB:1YK3"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:1YK3"
FT HELIX 115..118
FT /evidence="ECO:0007829|PDB:1YK3"
FT STRAND 127..134
FT /evidence="ECO:0007829|PDB:1YK3"
FT HELIX 136..139
FT /evidence="ECO:0007829|PDB:1YK3"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:1YK3"
FT HELIX 143..158
FT /evidence="ECO:0007829|PDB:1YK3"
FT STRAND 164..167
FT /evidence="ECO:0007829|PDB:1YK3"
FT HELIX 174..183
FT /evidence="ECO:0007829|PDB:1YK3"
FT STRAND 186..192
FT /evidence="ECO:0007829|PDB:1YK3"
FT STRAND 197..204
FT /evidence="ECO:0007829|PDB:1YK3"
SQ SEQUENCE 210 AA; 23799 MW; 2ADDBB5D0BE81561 CRC64;
MTKPTSAGQA DDALVRLARE RFDLPDQVRR LARPPVPSLE PPYGLRVAQL TDAEMLAEWM
NRPHLAAAWE YDWPASRWRQ HLNAQLEGTY SLPLIGSWHG TDGGYLELYW AAKDLISHYY
DADPYDLGLH AAIADLSKVN RGFGPLLLPR IVASVFANEP RCRRIMFDPD HRNTATRRLC
EWAGCKFLGE HDTTNRRMAL YALEAPTTAA
