ID LIPB_MYCTU Reviewed; 230 AA.
AC P9WK83; L0T8Z0; Q10404;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Octanoyltransferase {ECO:0000255|HAMAP-Rule:MF_00013};
DE EC=2.3.1.181 {ECO:0000255|HAMAP-Rule:MF_00013};
DE AltName: Full=Lipoate-protein ligase B {ECO:0000255|HAMAP-Rule:MF_00013};
DE AltName: Full=Lipoyl/octanoyl transferase {ECO:0000255|HAMAP-Rule:MF_00013};
DE AltName: Full=Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase {ECO:0000255|HAMAP-Rule:MF_00013};
GN Name=lipB {ECO:0000255|HAMAP-Rule:MF_00013}; OrderedLocusNames=Rv2217;
GN ORFNames=MTCY190.28;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011445;
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 [3]
RP X-RAY CRYSTALLOGRAPHY (1.08 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG,
RP FUNCTION, REACTION MECHANISM, SUBUNIT, AND MUTAGENESIS OF LYS-142 AND
RP CYS-176.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=16735476; DOI=10.1073/pnas.0510436103;
RA Ma Q., Zhao X., Eddine A.N., Geerlof A., Li X., Cronan J.E.,
RA Kaufmann S.H.E., Wilmanns M.;
RT "The Mycobacterium tuberculosis LipB enzyme functions as a cysteine/lysine
RT dyad acyltransferase.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:8662-8667(2006).
CC -!- FUNCTION: Catalyzes the transfer of endogenously produced octanoic acid
CC from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-
CC dependent enzymes. Lipoyl-ACP can also act as a substrate although
CC octanoyl-ACP is likely to be the physiological substrate.
CC {ECO:0000255|HAMAP-Rule:MF_00013, ECO:0000269|PubMed:16735476}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl-[protein] + octanoyl-[ACP] = H(+) + holo-[ACP] + N(6)-
CC octanoyl-L-lysyl-[protein]; Xref=Rhea:RHEA:17665, Rhea:RHEA-
CC COMP:9636, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9752, Rhea:RHEA-
CC COMP:9928, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78463, ChEBI:CHEBI:78809; EC=2.3.1.181;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00013};
CC -!- PATHWAY: Protein modification; protein lipoylation via endogenous
CC pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-
CC protein]: step 1/2. {ECO:0000255|HAMAP-Rule:MF_00013}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16735476}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00013}.
CC -!- MISCELLANEOUS: In the reaction, the free carboxyl group of octanoic
CC acid is attached via an amide linkage to the epsilon-amino group of a
CC specific lysine residue of lipoyl domains of lipoate-dependent enzymes.
CC -!- SIMILARITY: Belongs to the LipB family. {ECO:0000255|HAMAP-
CC Rule:MF_00013}.
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DR EMBL; AL123456; CCP44994.1; -; Genomic_DNA.
DR PIR; B70787; B70787.
DR RefSeq; NP_216733.1; NC_000962.3.
DR RefSeq; WP_003411458.1; NZ_NVQJ01000008.1.
DR PDB; 1W66; X-ray; 1.08 A; A=3-230.
DR PDBsum; 1W66; -.
DR AlphaFoldDB; P9WK83; -.
DR SMR; P9WK83; -.
DR STRING; 83332.Rv2217; -.
DR DrugBank; DB03600; Capric acid.
DR PaxDb; 83332-Rv2217; -.
DR DNASU; 887626; -.
DR GeneID; 45426193; -.
DR GeneID; 887626; -.
DR KEGG; mtu:Rv2217; -.
DR TubercuList; Rv2217; -.
DR eggNOG; COG0321; Bacteria.
DR InParanoid; P9WK83; -.
DR OrthoDB; 9787061at2; -.
DR PhylomeDB; P9WK83; -.
DR BRENDA; 2.3.1.181; 3445.
DR BRENDA; 6.3.1.20; 3445.
DR UniPathway; UPA00538; UER00592.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0033819; F:lipoyl(octanoyl) transferase activity; IDA:MTBBASE.
DR GO; GO:0009107; P:lipoate biosynthetic process; IMP:MTBBASE.
DR GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR CDD; cd16444; LipB; 1.
DR HAMAP; MF_00013; LipB; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004143; BPL_LPL_catalytic.
DR InterPro; IPR000544; Octanoyltransferase.
DR InterPro; IPR020605; Octanoyltransferase_CS.
DR NCBIfam; TIGR00214; lipB; 1.
DR PANTHER; PTHR10993:SF7; LIPOYLTRANSFERASE 2, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR10993; OCTANOYLTRANSFERASE; 1.
DR PIRSF; PIRSF016262; LPLase; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
DR PROSITE; PS01313; LIPB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT CHAIN 1..230
FT /note="Octanoyltransferase"
FT /id="PRO_0000062851"
FT DOMAIN 38..215
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01067"
FT ACT_SITE 176
FT /note="Acyl-thioester intermediate"
FT BINDING 76..83
FT /ligand="substrate"
FT BINDING 145..147
FT /ligand="substrate"
FT BINDING 158..160
FT /ligand="substrate"
FT SITE 142
FT /note="Lowers pKa of active site Cys"
FT MUTAGEN 142
FT /note="K->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:16735476"
FT MUTAGEN 176
FT /note="C->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:16735476"
FT STRAND 13..19
FT /evidence="ECO:0007829|PDB:1W66"
FT HELIX 22..37
FT /evidence="ECO:0007829|PDB:1W66"
FT STRAND 43..48
FT /evidence="ECO:0007829|PDB:1W66"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:1W66"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:1W66"
FT STRAND 75..83
FT /evidence="ECO:0007829|PDB:1W66"
FT STRAND 87..93
FT /evidence="ECO:0007829|PDB:1W66"
FT HELIX 102..119
FT /evidence="ECO:0007829|PDB:1W66"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:1W66"
FT STRAND 130..135
FT /evidence="ECO:0007829|PDB:1W66"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:1W66"
FT STRAND 141..151
FT /evidence="ECO:0007829|PDB:1W66"
FT STRAND 154..164
FT /evidence="ECO:0007829|PDB:1W66"
FT HELIX 168..172
FT /evidence="ECO:0007829|PDB:1W66"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:1W66"
FT STRAND 179..183
FT /evidence="ECO:0007829|PDB:1W66"
FT HELIX 186..190
FT /evidence="ECO:0007829|PDB:1W66"
FT HELIX 196..211
FT /evidence="ECO:0007829|PDB:1W66"
SQ SEQUENCE 230 AA; 24211 MW; E967D3EBD338FE61 CRC64;
MTGSIRSKLS AIDVRQLGTV DYRTAWQLQR ELADARVAGG ADTLLLLEHP AVYTAGRRTE
THERPIDGTP VVDTDRGGKI TWHGPGQLVG YPIIGLAEPL DVVNYVRRLE ESLIQVCADL
GLHAGRVDGR SGVWLPGRPA RKVAAIGVRV SRATTLHGFA LNCDCDLAAF TAIVPCGISD
AAVTSLSAEL GRTVTVDEVR ATVAAAVCAA LDGVLPVGDR VPSHAVPSPL
//
