LIPB_THET8
ID LIPB_THET8 Reviewed; 217 AA.
AC Q5SLQ3;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
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=TTHA0240;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 1-210.
RX PubMed=18076036; DOI=10.1002/prot.21843;
RA Kim do J., Lee S.J., Kim H.S., Kim K.H., Lee H.H., Yoon H.J., Suh S.W.;
RT "Structural basis of octanoic acid recognition by lipoate-protein ligase
RT B.";
RL Proteins 70:1620-1625(2008).
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}.
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 -!- 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 {ECO:0000255|HAMAP-Rule:MF_00013}.
CC -!- SIMILARITY: Belongs to the LipB family. {ECO:0000255|HAMAP-
CC Rule:MF_00013}.
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DR EMBL; AP008226; BAD70063.1; -; Genomic_DNA.
DR RefSeq; WP_011174104.1; NC_006461.1.
DR RefSeq; YP_143506.1; NC_006461.1.
DR PDB; 2QHS; X-ray; 1.50 A; A=1-217.
DR PDB; 2QHT; X-ray; 1.50 A; A=1-210.
DR PDB; 2QHU; X-ray; 1.90 A; A=1-210.
DR PDB; 2QHV; X-ray; 1.60 A; A=1-210.
DR PDBsum; 2QHS; -.
DR PDBsum; 2QHT; -.
DR PDBsum; 2QHU; -.
DR PDBsum; 2QHV; -.
DR AlphaFoldDB; Q5SLQ3; -.
DR SMR; Q5SLQ3; -.
DR STRING; 300852.55771622; -.
DR EnsemblBacteria; BAD70063; BAD70063; BAD70063.
DR GeneID; 3168876; -.
DR KEGG; ttj:TTHA0240; -.
DR PATRIC; fig|300852.9.peg.240; -.
DR eggNOG; COG0321; Bacteria.
DR HOGENOM; CLU_035168_1_3_0; -.
DR OMA; GEVTYHC; -.
DR PhylomeDB; Q5SLQ3; -.
DR UniPathway; UPA00538; UER00592.
DR EvolutionaryTrace; Q5SLQ3; -.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0033819; F:lipoyl(octanoyl) transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009249; P:protein lipoylation; IEA:InterPro.
DR CDD; cd16444; LipB; 1.
DR Gene3D; 3.30.930.10; -; 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 PIRSF; PIRSF016262; LPLase; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00214; lipB; 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..217
FT /note="Octanoyltransferase"
FT /id="PRO_0000242777"
FT DOMAIN 30..209
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01067"
FT ACT_SITE 170
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00013"
FT BINDING 75..82
FT /ligand="substrate"
FT BINDING 139..141
FT /ligand="substrate"
FT BINDING 152..154
FT /ligand="substrate"
FT SITE 136
FT /note="Lowers pKa of active site Cys"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00013"
FT STRAND 2..10
FT /evidence="ECO:0007829|PDB:2QHS"
FT HELIX 13..28
FT /evidence="ECO:0007829|PDB:2QHS"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:2QHS"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:2QHS"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:2QHS"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:2QHS"
FT HELIX 60..65
FT /evidence="ECO:0007829|PDB:2QHS"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:2QHS"
FT STRAND 75..82
FT /evidence="ECO:0007829|PDB:2QHS"
FT STRAND 86..92
FT /evidence="ECO:0007829|PDB:2QHS"
FT HELIX 99..116
FT /evidence="ECO:0007829|PDB:2QHS"
FT STRAND 125..132
FT /evidence="ECO:0007829|PDB:2QHS"
FT STRAND 135..145
FT /evidence="ECO:0007829|PDB:2QHS"
FT STRAND 148..158
FT /evidence="ECO:0007829|PDB:2QHS"
FT HELIX 161..166
FT /evidence="ECO:0007829|PDB:2QHS"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:2QHS"
FT HELIX 180..184
FT /evidence="ECO:0007829|PDB:2QHS"
FT HELIX 190..205
FT /evidence="ECO:0007829|PDB:2QHS"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:2QHS"
SQ SEQUENCE 217 AA; 23924 MW; 4139DD00A18692C5 CRC64;
MEFLVEDLGL VPYGEAWAYQ KRVHREVVAG NRPPTLLLLE HPRVITLGRK ATGENLLFPE
SWYRENGFEL YWVERGGDVT YHGPGQLVGY PIFPVGREVR RFLRQIEEAI VRVAAGYGIS
AYPTPGYAGV WVGEDKLCAI GVAVKEGVSF HGFALNVNTD LNDFTVIVPC GLKGKGVTSL
EKLLGRKVPM EEAKARVVAA FAEVFGLRPV EGSVHEA
