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LIPM_BACAN
ID   LIPM_BACAN              Reviewed;         278 AA.
AC   Q81M24; E9R366; E9R367; Q6HTH7; Q6KMR8;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Octanoyltransferase LipM {ECO:0000255|HAMAP-Rule:MF_02118};
DE            EC=2.3.1.181 {ECO:0000255|HAMAP-Rule:MF_02118};
DE   AltName: Full=Octanoyl-[acyl-carrier-protein]:[GcvH] N-octanoyltransferase {ECO:0000255|HAMAP-Rule:MF_02118};
GN   Name=lipM {ECO:0000255|HAMAP-Rule:MF_02118};
GN   OrderedLocusNames=BA_4431, GBAA_4431, BAS4111;
OS   Bacillus anthracis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1392;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ames / isolate Porton;
RX   PubMed=12721629; DOI=10.1038/nature01586;
RA   Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA   Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA   Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA   Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA   DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA   Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA   Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA   Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA   White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA   Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT   "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT   related bacteria.";
RL   Nature 423:81-86(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ames ancestor;
RX   PubMed=18952800; DOI=10.1128/jb.01347-08;
RA   Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA   Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT   "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL   J. Bacteriol. 191:445-446(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sterne;
RA   Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA   Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA   Richardson P., Rubin E., Tice H.;
RT   "Complete genome sequence of Bacillus anthracis Sterne.";
RL   Submitted (JAN-2004) 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:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_02118}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|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:0000255|HAMAP-Rule:MF_02118}.
CC   -!- SIMILARITY: Belongs to the octanoyltransferase LipM family.
CC       {ECO:0000255|HAMAP-Rule:MF_02118}.
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DR   EMBL; AE016879; AAP28145.1; -; Genomic_DNA.
DR   EMBL; AE017334; AAT33548.1; -; Genomic_DNA.
DR   EMBL; AE017225; AAT56412.1; -; Genomic_DNA.
DR   RefSeq; NP_846659.1; NC_003997.3.
DR   RefSeq; WP_000514074.1; NZ_WXXJ01000027.1.
DR   RefSeq; YP_030361.1; NC_005945.1.
DR   AlphaFoldDB; Q81M24; -.
DR   SMR; Q81M24; -.
DR   STRING; 260799.BAS4111; -.
DR   DNASU; 1087804; -.
DR   EnsemblBacteria; AAP28145; AAP28145; BA_4431.
DR   EnsemblBacteria; AAT33548; AAT33548; GBAA_4431.
DR   GeneID; 45024091; -.
DR   KEGG; ban:BA_4431; -.
DR   KEGG; bar:GBAA_4431; -.
DR   KEGG; bat:BAS4111; -.
DR   PATRIC; fig|198094.11.peg.4400; -.
DR   eggNOG; COG0095; Bacteria.
DR   HOGENOM; CLU_022986_5_0_9; -.
DR   OMA; YAYLDDW; -.
DR   Proteomes; UP000000427; Chromosome.
DR   Proteomes; UP000000594; 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:0009249; P:protein lipoylation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.930.10; -; 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   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..278
FT                   /note="Octanoyltransferase LipM"
FT                   /id="PRO_0000410849"
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:0000255|HAMAP-Rule:MF_02118"
FT   SITE            165
FT                   /note="Lowers pKa of active site Cys"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02118"
SQ   SEQUENCE   278 AA;  32103 MW;  20F2643618464D75 CRC64;
     MGKEKWCYIN SGQCSPAFNM ALDECLLNWQ SEKKMPPTIR FYEWEVPTLT VGYFQRVEKD
     INMDVVNEKK YGFVRRQTGG RGVLHDKELT YSVIVSEDHP NMPKTVTEAY RVISQGLLDG
     FKALGLEAYY AVPKTEADRE NLKNPRSGVC FDAPSWYEIV VEGRKIAGSA QTRQKGVILQ
     HGSIPLEIDL DELYDLFLFP NERVKERMKS MFASKAVAIN ELTDRTFTIE QLIKAFEVGF
     EKGLDVELVP YELTEEQLHE VQTLAKEKYE SKEWNYKK
 
 
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