(data stored in SCRATCH zone)

SWISSPROT: LIPM_BACSU

ID   LIPM_BACSU              Reviewed;         278 AA.
AC   P54511; O32018;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2002, sequence version 2.
DT   11-DEC-2019, entry version 108.
DE   RecName: Full=Octanoyltransferase LipM;
DE            EC=2.3.1.181;
DE   AltName: Full=Octanoyl-[acyl-carrier-protein]:[GcvH] N-octanoyltransferase;
GN   Name=lipM; Synonyms=yqhM; OrderedLocusNames=BSU24530;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / JH642;
RX   PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA   Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA   Kobayashi Y.;
RT   "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT   Bacillus subtilis genome containing the skin element and many sporulation
RT   genes.";
RL   Microbiology 142:3103-3111(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   IDENTIFICATION, GENE NAME, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP   SPECIFICITY, PATHWAY, REACTION MECHANISM, ACTIVE SITE, SUBUNIT, AND
RP   MUTAGENESIS OF CYS-150 AND LYS-165.
RC   STRAIN=168;
RX   PubMed=20882995; DOI=10.1021/bi101215f;
RA   Christensen Q.H., Cronan J.E.;
RT   "Lipoic acid synthesis: a new family of octanoyltransferases generally
RT   annotated as lipoate protein ligases.";
RL   Biochemistry 49:10024-10036(2010).
RN   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=168 / JH642;
RX   PubMed=21338420; DOI=10.1111/j.1365-2958.2011.07597.x;
RA   Martin N., Christensen Q.H., Mansilla M.C., Cronan J.E., de Mendoza D.;
RT   "A novel two-gene requirement for the octanoyltransfer reaction of Bacillus
RT   subtilis lipoic acid biosynthesis.";
RL   Mol. Microbiol. 80:335-349(2011).
RN   [5]
RP   FUNCTION, AND SPECIFICITY FOR GCVH.
RC   STRAIN=168 / JH642;
RX   PubMed=21338421; DOI=10.1111/j.1365-2958.2011.07598.x;
RA   Christensen Q.H., Martin N., Mansilla M.C., de Mendoza D., Cronan J.E.;
RT   "A novel amidotransferase required for lipoic acid cofactor assembly in
RT   Bacillus subtilis.";
RL   Mol. Microbiol. 80:350-363(2011).
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. Is also able to
CC       catalyze the reverse reaction. Octanoyl-CoA can also act as a substrate
CC       although very poorly. Does not display lipoate protein ligase activity,
CC       despite its sequence similarity to LplA. {ECO:0000269|PubMed:20882995,
CC       ECO:0000269|PubMed:21338420, ECO:0000269|PubMed:21338421}.
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:0000269|PubMed:20882995};
CC   -!- PATHWAY: Protein modification; protein lipoylation via endogenous
CC       pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-
CC       protein]. {ECO:0000269|PubMed:20882995}.
CC   -!- SUBUNIT: Monomer. {ECO:0000305|PubMed:20882995}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene are auxotrophic for
CC       lipoic acid when grown in minimal medium but grow as well as the wild-
CC       type strain in the presence of lipoic acid. The requirement for lipoic
CC       acid can be bypassed by addition of both acetate and branched-chain
CC       fatty acid (BCFA) precursors. The mutant cells are devoid of lipoylated
CC       proteins. {ECO:0000269|PubMed:21338420}.
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   -!- SIMILARITY: Belongs to the octanoyltransferase LipM family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA12550.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; D84432; BAA12550.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AL009126; CAB14384.1; -; Genomic_DNA.
DR   PIR; D69959; D69959.
DR   RefSeq; NP_390333.1; NC_000964.3.
DR   RefSeq; WP_004398586.1; NZ_JNCM01000036.1.
DR   STRING; 224308.BSU24530; -.
DR   PaxDb; P54511; -.
DR   PRIDE; P54511; -.
DR   DNASU; 938551; -.
DR   EnsemblBacteria; CAB14384; CAB14384; BSU24530.
DR   GeneID; 938551; -.
DR   KEGG; bsu:BSU24530; -.
DR   PATRIC; fig|224308.179.peg.2671; -.
DR   eggNOG; ENOG4107S5Z; Bacteria.
DR   eggNOG; COG0095; LUCA.
DR   HOGENOM; HOG000245032; -.
DR   InParanoid; P54511; -.
DR   KO; K23734; -.
DR   OMA; YAYLDDW; -.
DR   PhylomeDB; P54511; -.
DR   BioCyc; BSUB:BSU24530-MONOMER; -.
DR   BioCyc; MetaCyc:BSU24530-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0033819; F:lipoyl(octanoyl) transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102555; F:octanoyl transferase activity (acting on glycine-cleavage complex H protein); IEA:UniProtKB-EC.
DR   GO; GO:0016415; F:octanoyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0006464; P:cellular protein modification process; IDA:UniProtKB.
DR   GO; GO:0009107; P:lipoate biosynthetic process; IMP:UniProtKB.
DR   GO; GO:0009249; P:protein lipoylation; IMP:UniProtKB.
DR   HAMAP; MF_02118; LipM; 1.
DR   InterPro; IPR004143; BPL_LPL_catalytic.
DR   InterPro; IPR024898; LipM.
DR   Pfam; PF03099; BPL_LplA_LipB; 1.
DR   PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P54511.
DR   SWISS-2DPAGE; P54511.
KW   Acyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..278
FT                   /note="Octanoyltransferase LipM"
FT                   /id="PRO_0000049820"
FT   DOMAIN          33..248
FT                   /note="BPL/LPL catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01067"
FT   ACT_SITE        150
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000269|PubMed:20882995"
FT   SITE            165
FT                   /note="Lowers pKa of active site Cys"
FT                   /evidence="ECO:0000305"
FT   MUTAGEN         150
FT                   /note="C->A,S: Loss of catalytic activity. Inability to
FT                   form the acyl-enzyme intermediate."
FT                   /evidence="ECO:0000269|PubMed:20882995"
FT   MUTAGEN         165
FT                   /note="K->A: Reduced catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:20882995"
FT   MUTAGEN         165
FT                   /note="K->R: No effect on catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:20882995"
SQ   SEQUENCE   278 AA;  32241 MW;  51FAFEF48C3CED05 CRC64;
     MQKETWRFID SGNASPAFNM ALDEALLYWH SEKKIPPVIR FYGWNPATLS VGYFQNIKKE
     INFEAVHKYN LGFVRRPTGG RGVLHDQELT YSVIVSEEHP EMPATVTEAY RVISEGILQG
     FRNLGLDAYF AIPRTEKEKE SLKNPRSSVC FDAPSWYELV VEGRKVAGSA QTRQKGVILQ
     HGSILLDLDE DKLFDLFLYP SERVRERMQR NFKNKAVAIN ELIEKRVTMD EARKAFKEGF
     ETGLNIHLEP YELSQEELDF VHHLAETKYA SDEWNYKR
//

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