LIPB_EHRCJ
ID LIPB_EHRCJ Reviewed; 214 AA.
AC Q3YRI1;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=Ecaj_0640;
OS Ehrlichia canis (strain Jake).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Ehrlichia.
OX NCBI_TaxID=269484;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Jake;
RX PubMed=16707693; DOI=10.1128/jb.01837-05;
RA Mavromatis K., Doyle C.K., Lykidis A., Ivanova N., Francino M.P., Chain P.,
RA Shin M., Malfatti S., Larimer F., Copeland A., Detter J.C., Land M.,
RA Richardson P.M., Yu X.J., Walker D.H., McBride J.W., Kyrpides N.C.;
RT "The genome of the obligately intracellular bacterium Ehrlichia canis
RT reveals themes of complex membrane structure and immune evasion
RT strategies.";
RL J. Bacteriol. 188:4015-4023(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}.
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; CP000107; AAZ68674.1; -; Genomic_DNA.
DR RefSeq; WP_011304751.1; NC_007354.1.
DR AlphaFoldDB; Q3YRI1; -.
DR SMR; Q3YRI1; -.
DR STRING; 269484.Ecaj_0640; -.
DR EnsemblBacteria; AAZ68674; AAZ68674; Ecaj_0640.
DR KEGG; ecn:Ecaj_0640; -.
DR eggNOG; COG0321; Bacteria.
DR HOGENOM; CLU_035168_3_0_5; -.
DR OMA; GEVTYHC; -.
DR OrthoDB; 1806796at2; -.
DR UniPathway; UPA00538; UER00592.
DR Proteomes; UP000000435; 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 3: Inferred from homology;
KW Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT CHAIN 1..214
FT /note="Octanoyltransferase"
FT /id="PRO_0000242718"
FT DOMAIN 34..214
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01067"
FT ACT_SITE 176
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00013"
FT BINDING 73..80
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00013"
FT BINDING 145..147
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00013"
FT BINDING 158..160
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00013"
FT SITE 142
FT /note="Lowers pKa of active site Cys"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00013"
SQ SEQUENCE 214 AA; 24450 MW; 927ED9B6EA6C2810 CRC64;
MSCDLVEWKI ESSPIDYQEA VYFMQRKVDS ISDGLQKELV WLLEHPALYT AGTGATVEDL
LASNLLPVYS TNRGGKYTYH GPGQRIAYVM LNLKTRNKCN VRLYVKTLGD WIINTLSHFS
IKSYFNPDLI GVWVTHNGIE KKIAAFGIRI RKWITYHGVS VNIYTDLSHY LGIVPCGIKE
YGVTSFKQLG VNVSYEEFDI VLEKKFNEIF SSFN