ID A0A0H4KM49_9BACI Unreviewed; 280 AA.
AC A0A0H4KM49;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Octanoyltransferase LipM {ECO:0000256|HAMAP-Rule:MF_02118};
DE EC=2.3.1.181 {ECO:0000256|HAMAP-Rule:MF_02118};
DE AltName: Full=Octanoyl-[acyl-carrier-protein]:[GcvH] N-octanoyltransferase {ECO:0000256|HAMAP-Rule:MF_02118};
GN Name=lipM {ECO:0000256|HAMAP-Rule:MF_02118};
GN ORFNames=BEH_19650 {ECO:0000313|EMBL:AKO95167.1};
OS Priestia filamentosa.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Priestia.
OX NCBI_TaxID=1402861 {ECO:0000313|EMBL:AKO95167.1, ECO:0000313|Proteomes:UP000036202};
RN [1] {ECO:0000313|EMBL:AKO95167.1, ECO:0000313|Proteomes:UP000036202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hbe603 {ECO:0000313|EMBL:AKO95167.1,
RC ECO:0000313|Proteomes:UP000036202};
RX PubMed=26248285;
RA Jia N., Du J., Ding M.Z., Gao F., Yuan Y.J.;
RT "Genome Sequence of Bacillus endophyticus and Analysis of Its Companion
RT Mechanism in the Ketogulonigenium vulgare-Bacillus Strain Consortium.";
RL PLoS ONE 10:E0135104-E0135104(2015).
RN [2] {ECO:0000313|Proteomes:UP000036202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hbe603 {ECO:0000313|Proteomes:UP000036202};
RA Jia N., Du J., Ding M.-Z., Gao F., Yuan Y.-J.;
RT "Genome Sequence of Bacillus endophyticus and Analysis of its Companion
RT Mechanism in the Ketogulonigenium vulgare-Bacillus strain Consortium.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the transfer of endogenously produced octanoic acid
CC from octanoyl-acyl-carrier-protein onto the lipoyl domain of GcvH, an
CC intermediate carrier during protein lipoylation. {ECO:0000256|HAMAP-
CC Rule:MF_02118}.
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:0000256|HAMAP-Rule:MF_02118};
CC -!- PATHWAY: Protein modification; protein lipoylation via endogenous
CC pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-
CC protein]. {ECO:0000256|HAMAP-Rule:MF_02118}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_02118}.
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 The reaction proceeds via an octanoyl-thioester enzyme intermediate.
CC {ECO:0000256|HAMAP-Rule:MF_02118}.
CC -!- SIMILARITY: Belongs to the octanoyltransferase LipM family.
CC {ECO:0000256|HAMAP-Rule:MF_02118}.
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DR EMBL; CP011974; AKO95167.1; -; Genomic_DNA.
DR RefSeq; WP_046217980.1; NZ_NQYF01000001.1.
DR AlphaFoldDB; A0A0H4KM49; -.
DR KEGG; beo:BEH_19650; -.
DR PATRIC; fig|135735.6.peg.4167; -.
DR OrthoDB; 9774653at2; -.
DR Proteomes; UP000036202; Chromosome.
DR GO; GO:0033819; F:lipoyl(octanoyl) transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009107; P:lipoate biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR CDD; cd16443; LplA; 1.
DR HAMAP; MF_02118; LipM; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004143; BPL_LPL_catalytic.
DR InterPro; IPR024898; LipM.
DR PANTHER; PTHR43679:SF2; OCTANOYLTRANSFERASE LIPM; 1.
DR PANTHER; PTHR43679; OCTANOYLTRANSFERASE LIPM-RELATED; 1.
DR Pfam; PF03099; BPL_LplA_LipB; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|HAMAP-Rule:MF_02118};
KW Reference proteome {ECO:0000313|Proteomes:UP000036202};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_02118, ECO:0000313|EMBL:AKO95167.1}.
FT DOMAIN 35..250
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
FT ACT_SITE 152
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02118"
FT SITE 167
FT /note="Lowers pKa of active site Cys"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02118"
SQ SEQUENCE 280 AA; 32440 MW; DA5A80C6AA63CF44 CRC64;
MRKMTEVWRF INWSKHSPYY NMALDEALLD WHSEGKIPPT IRFYGWDPAT LSIGYFQKAE
KEVNFEEVRK RGLGFVRRPT GGRGVLHDDE LTYSVIVSEQ HKSMPHTVTE AYRVISEGLL
EGFRALGLDA YFAIPRTEEE KEGLKNPRSS VCFDAPSWYE LVVEGRKVAG SAQTRQKGVI
LQHGSILLSI DEEALFSMFH YPSERVKERM RKSFRNKAVA VNDVAGRIVS IEEANEAFKR
GFEKGLNIKL EEYILSEEEE AYVKKLALDK YAKDEWNYRR
//
