ID LIPB_THEPX Reviewed; 228 AA.
AC B0K3J8;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 01-MAY-2013, entry version 42.
DE RecName: Full=Octanoyltransferase;
DE EC=2.3.1.181;
DE AltName: Full=Lipoate-protein ligase B;
DE AltName: Full=Lipoyl/octanoyl transferase;
DE AltName: Full=Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase;
GN Name=lipB; OrderedLocusNames=Teth514_2037;
OS Thermoanaerobacter sp. (strain X514).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Thermoanaerobacter.
OX NCBI_TaxID=399726;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=X514;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA Dalin E., Tice H., Pitluck S., Bruce D., Goodwin L., Saunders E.,
RA Brettin T., Detter J.C., Han C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Hemme C., Fields M.W., He Z., Zhou J.,
RA Richardson P.;
RT "Complete sequence of Thermoanaerobacter sp. X514.";
RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the transfer of endogenously produced octanoic
CC acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of
CC lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate
CC although octanoyl-ACP is likely to be the physiological substrate
CC (By similarity).
CC -!- CATALYTIC ACTIVITY: Octanoyl-[acyl-carrier-protein] + protein =
CC protein N(6)-(octanoyl)lysine + [acyl-carrier-protein].
CC -!- PATHWAY: Protein modification; protein lipoylation via endogenous
CC pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-
CC protein]: step 1/2.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (Potential).
CC -!- MISCELLANEOUS: In the reaction, the free carboxyl group of
CC octanoic acid is attached via an amide linkage to the epsilon-
CC amino group of a specific lysine residue of lipoyl domains of
CC lipoate-dependent enzymes (By similarity).
CC -!- SIMILARITY: Belongs to the LipB family.
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DR EMBL; CP000923; ABY93309.1; -; Genomic_DNA.
DR RefSeq; YP_001663645.1; NC_010320.1.
DR ProteinModelPortal; B0K3J8; -.
DR STRING; 399726.Teth514_2037; -.
DR EnsemblBacteria; ABY93309; ABY93309; Teth514_2037.
DR GeneID; 5876195; -.
DR KEGG; tex:Teth514_2037; -.
DR PATRIC; 23893780; VBITheSp86957_2113.
DR eggNOG; COG0321; -.
DR HOGENOM; HOG000194322; -.
DR KO; K03801; -.
DR OMA; NFVRRLE; -.
DR ProtClustDB; CLSK901366; -.
DR UniPathway; UPA00538; UER00592.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0033819; F:lipoyl(octanoyl) transferase activity; IEA:EC.
DR GO; GO:0016415; F:octanoyltransferase activity; IEA:InterPro.
DR GO; GO:0006464; P:cellular protein modification process; IEA:InterPro.
DR GO; GO:0009107; P:lipoate biosynthetic process; IEA:InterPro.
DR HAMAP; MF_00013; LipB; 1; -.
DR InterPro; IPR004143; BPL_LipA_LipB.
DR InterPro; IPR000544; Octanoyltransferase.
DR InterPro; IPR020605; Octanoyltransferase_CS.
DR PANTHER; PTHR10993:SF0; PTHR10993:SF0; 1.
DR Pfam; PF03099; BPL_LplA_LipB; 1.
DR PIRSF; PIRSF016262; LPLase; 1.
DR TIGRFAMs; TIGR00214; lipB; 1.
DR PROSITE; PS01313; LIPB; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Complete proteome; Cytoplasm; Transferase.
FT CHAIN 1 228 Octanoyltransferase.
FT /FTId=PRO_1000089480.
FT REGION 76 83 Substrate binding (By similarity).
FT REGION 143 145 Substrate binding (By similarity).
FT REGION 156 158 Substrate binding (By similarity).
FT ACT_SITE 174 174 Acyl-thioester intermediate (By
FT similarity).
FT SITE 140 140 Lowers pKa of active site Cys (By
FT similarity).
SQ SEQUENCE 228 AA; 25684 MW; DCFC5F634F7C7C97 CRC64;
MRKGEVLKLG IVPYMEGKEI QLKAFERVKK GETDGILILL QHPPVYTIGV SGGFDENILV
PLAELKKKAE LYKVERGGKI TFHGPGQIVA YPIFNLAKWQ KDVHLFVYKL EETIIKLLEE
YGIKAGRKPK YTGVWVGDEK ICAIGIAVRR WITWHGIAFN VNTDLSYFGL INACGITEFG
VTSMQKLGIN EDIEKVKEKM VDKFSEVFGI HFSEITLDRL AVIDNAKA
//
