ID   LIPL_BREBN              Reviewed;         280 AA.
AC   C0ZF00;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Octanoyl-[GcvH]:protein N-octanoyltransferase {ECO:0000255|HAMAP-Rule:MF_02119};
DE            EC=2.3.1.204 {ECO:0000255|HAMAP-Rule:MF_02119};
DE   AltName: Full=Octanoyl-[GcvH]:E2 amidotransferase {ECO:0000255|HAMAP-Rule:MF_02119};
GN   Name=lipL {ECO:0000255|HAMAP-Rule:MF_02119}; OrderedLocusNames=BBR47_33820;
OS   Brevibacillus brevis (strain 47 / JCM 6285 / NBRC 100599).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX   NCBI_TaxID=358681;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=47 / JCM 6285 / NBRC 100599;
RA   Hosoyama A., Yamada R., Hongo Y., Terui Y., Ankai A., Masuyama W.,
RA   Sekiguchi M., Takeda T., Asano K., Ohji S., Ichikawa N., Narita S.,
RA   Aoki N., Miura H., Matsushita S., Sekigawa T., Yamagata H., Yoshikawa H.,
RA   Udaka S., Tanikawa S., Fujita N.;
RT   "Brevibacillus brevis strain 47, complete genome.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the amidotransfer (transamidation) of the octanoyl
CC       moiety from octanoyl-GcvH to the lipoyl domain of the E2 subunit of
CC       lipoate-dependent enzymes. {ECO:0000255|HAMAP-Rule:MF_02119}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[lipoyl-carrier protein] + N(6)-octanoyl-L-lysyl-
CC         [glycine-cleavage complex H protein] = L-lysyl-[glycine-cleavage
CC         complex H protein] + N(6)-octanoyl-L-lysyl-[lipoyl-carrier protein];
CC         Xref=Rhea:RHEA:20213, Rhea:RHEA-COMP:10500, Rhea:RHEA-COMP:10501,
CC         Rhea:RHEA-COMP:10503, Rhea:RHEA-COMP:10504, ChEBI:CHEBI:29969,
CC         ChEBI:CHEBI:78809; EC=2.3.1.204; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_02119};
CC   -!- PATHWAY: Protein modification; protein lipoylation via endogenous
CC       pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-
CC       protein]. {ECO:0000255|HAMAP-Rule:MF_02119}.
CC   -!- MISCELLANEOUS: The reaction proceeds via a thioester-linked acyl-enzyme
CC       intermediate. {ECO:0000255|HAMAP-Rule:MF_02119}.
CC   -!- SIMILARITY: Belongs to the octanoyltransferase LipL family.
CC       {ECO:0000255|HAMAP-Rule:MF_02119}.
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DR   EMBL; AP008955; BAH44359.1; -; Genomic_DNA.
DR   RefSeq; WP_015891666.1; NC_012491.1.
DR   AlphaFoldDB; C0ZF00; -.
DR   SMR; C0ZF00; -.
DR   STRING; 358681.BBR47_33820; -.
DR   EnsemblBacteria; BAH44359; BAH44359; BBR47_33820.
DR   KEGG; bbe:BBR47_33820; -.
DR   eggNOG; COG0095; Bacteria.
DR   HOGENOM; CLU_067270_0_0_9; -.
DR   OMA; VQIYLCI; -.
DR   OrthoDB; 871298at2; -.
DR   Proteomes; UP000001877; Chromosome.
DR   GO; GO:0016415; F:octanoyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009107; P:lipoate biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009249; P:protein lipoylation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.930.10; -; 1.
DR   HAMAP; MF_02119; LipL; 1.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR004143; BPL_LPL_catalytic.
DR   InterPro; IPR024897; LipL.
DR   Pfam; PF03099; BPL_LplA_LipB; 1.
DR   SUPFAM; SSF55681; SSF55681; 1.
DR   PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..280
FT                   /note="Octanoyl-[GcvH]:protein N-octanoyltransferase"
FT                   /id="PRO_0000410838"
FT   DOMAIN          38..240
FT                   /note="BPL/LPL catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01067"
FT   ACT_SITE        140
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02119"
FT   SITE            152
FT                   /note="Lowers pKa of active site Cys"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02119"
SQ   SEQUENCE   280 AA;  31189 MW;  6163A4FDD9365733 CRC64;
     MSFSVNQPFR WMDSGTYQDS PLEPLIRDEA LAASMQSESA APVIHLWVYD QALYLGRRDA
     KLPHLQQALH QFGQDGFGCV LRSSGGACVP LDAGVLNMAC LLPNTSISID SFFSFVAQLL
     DVGLRDYGKL EFGEVTGSYC AGEYDFSIHG KKIGGMAQRR TRHGSILQLC INVDDRPRGE
     WMEHFYRLAG LDEMQSHKPI PSIDASTVGS IASLTGKLAT MDDVKARLLE TIRSEWAVSP
     TPFYVQNELV TESRHHLSQR LHLFSYTAKE LAAPDWHLPE