LIPLL_LISMO
ID LIPLL_LISMO Reviewed; 278 AA.
AC Q8Y489;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Lipoyl-[GcvH]:protein N-lipoyltransferase {ECO:0000255|HAMAP-Rule:MF_02119};
DE EC=2.3.1.200 {ECO:0000255|HAMAP-Rule:MF_02119};
DE AltName: Full=Lipoyl amidotransferase;
DE AltName: Full=Lipoyl-[GcvH]:E2 amidotransferase {ECO:0000255|HAMAP-Rule:MF_02119};
GN Name=lipL {ECO:0000255|HAMAP-Rule:MF_02119}; OrderedLocusNames=lmo2566;
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
RN [2]
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=20937762; DOI=10.1128/iai.00330-10;
RA Dowd G.C., Joyce S.A., Hill C., Gahan C.G.;
RT "Investigation of the mechanisms by which Listeria monocytogenes grows in
RT porcine gallbladder bile.";
RL Infect. Immun. 79:369-379(2011).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND PATHWAY.
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=21768091; DOI=10.1074/jbc.m111.273607;
RA Christensen Q.H., Hagar J.A., O'Riordan M.X., Cronan J.E.;
RT "A complex lipoate utilization pathway in Listeria monocytogenes.";
RL J. Biol. Chem. 286:31447-31456(2011).
CC -!- FUNCTION: Catalyzes the amidotransfer (transamidation) of the lipoyl
CC moiety from lipoyl-GcvH to the lipoyl domain of the E2 subunit of
CC lipoate-dependent enzymes. Takes part in a pathway for scavenging of
CC lipoic acid derived from eukaryotic host cells. Cannot use lipoyl-
CC tripeptide (DK(L)A), lipoamide (LD), or free lipoate as substrate.
CC {ECO:0000255|HAMAP-Rule:MF_02119, ECO:0000269|PubMed:21768091}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-N(6)-lipoyl-L-lysyl-[glycine-cleavage complex H protein] +
CC L-lysyl-[lipoyl-carrier protein] = (R)-N(6)-lipoyl-L-lysyl-[lipoyl-
CC carrier protein] + L-lysyl-[glycine-cleavage complex H protein];
CC Xref=Rhea:RHEA:16413, Rhea:RHEA-COMP:10494, Rhea:RHEA-COMP:10500,
CC Rhea:RHEA-COMP:10501, Rhea:RHEA-COMP:10502, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:83099; EC=2.3.1.200; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_02119, ECO:0000269|PubMed:21768091};
CC -!- PATHWAY: Protein modification; protein lipoylation via exogenous
CC pathway. {ECO:0000255|HAMAP-Rule:MF_02119,
CC ECO:0000269|PubMed:21768091}.
CC -!- DISRUPTION PHENOTYPE: Strains lacking this gene are attenuated in their
CC ability to grow in bile, but display no growth defect under normal
CC physiological conditions. The reduced tolerance of the mutant strain to
CC acidic bile salts is likely due to a decreased branched fatty acid
CC content of the membrane phospholipids, which results when
CC L.monocytogenes is deficient in lipoic acid.
CC {ECO:0000269|PubMed:20937762}.
CC -!- MISCELLANEOUS: L.monocytogenes is a natural lipoic acid auxotroph and
CC relies upon exogenous sources of lipoic acid for growth
CC (PubMed:21768091). Thus, this enzyme has not the same activity as its
CC ortholog in B.subtilis which is involved in the lipoate biosynthesis
CC pathway. {ECO:0000305|PubMed:21768091}.
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; AL591983; CAD00644.1; -; Genomic_DNA.
DR PIR; AF1395; AF1395.
DR RefSeq; NP_466089.1; NC_003210.1.
DR RefSeq; WP_009924631.1; NZ_CP023861.1.
DR AlphaFoldDB; Q8Y489; -.
DR SMR; Q8Y489; -.
DR STRING; 169963.lmo2566; -.
DR PaxDb; Q8Y489; -.
DR EnsemblBacteria; CAD00644; CAD00644; CAD00644.
DR GeneID; 984810; -.
DR KEGG; lmo:lmo2566; -.
DR PATRIC; fig|169963.11.peg.2629; -.
DR eggNOG; COG0095; Bacteria.
DR HOGENOM; CLU_067270_0_0_9; -.
DR OMA; VQIYLCI; -.
DR PhylomeDB; Q8Y489; -.
DR BioCyc; LMON169963:LMO2566-MON; -.
DR BioCyc; MetaCyc:MON-17112; -.
DR UniPathway; UPA00537; -.
DR Proteomes; UP000000817; Chromosome.
DR GO; GO:0017118; F:lipoyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016415; F:octanoyltransferase activity; IEA:InterPro.
DR GO; GO:0009107; P:lipoate biosynthetic process; IEA:InterPro.
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 1: Evidence at protein level;
KW Acyltransferase; Reference proteome; Transferase.
FT CHAIN 1..278
FT /note="Lipoyl-[GcvH]:protein N-lipoyltransferase"
FT /id="PRO_0000424231"
FT DOMAIN 44..250
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01067"
FT ACT_SITE 149
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02119"
FT SITE 161
FT /note="Lowers pKa of active site Cys"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02119"
SQ SEQUENCE 278 AA; 30945 MW; FA2037EFF272C97E CRC64;
MNIENTLLKQ DVWRFIDNTT INPAFDAIQS FATDDTLCRS VGARMAPSTV RGWVHEKTVS
LGIQDSKLPD IDKGIAFLQK QGYRVVVRNS GGLAVVLDSG VLNLSMVLPD AERGIAIERG
YETMFTLIKD MFVDCNEVIE AKEIEDSYCP GSYDLSIQGK KFAGISQRRM AKGVAVQIYL
AIDGDQTTRS ELIRDFYTIS GKAKQTKYTF PDVNPNVMGS LSDLMKNDIS LNGTLVRLFN
SLRHYAGDLV SGTLTSEELD LFPAYYERLI ARNDKVLT
