LPLA_KLEP7
ID LPLA_KLEP7 Reviewed; 338 AA.
AC A6TI00;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Lipoate-protein ligase A {ECO:0000255|HAMAP-Rule:MF_01602};
DE EC=6.3.1.20 {ECO:0000255|HAMAP-Rule:MF_01602};
DE AltName: Full=Lipoate--protein ligase {ECO:0000255|HAMAP-Rule:MF_01602};
GN Name=lplA {ECO:0000255|HAMAP-Rule:MF_01602};
GN OrderedLocusNames=KPN78578_47600; ORFNames=KPN_04841;
OS Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=272620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700721 / MGH 78578;
RG The Klebsiella pneumonia Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes both the ATP-dependent activation of exogenously
CC supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl
CC onto the lipoyl domains of lipoate-dependent enzymes.
CC {ECO:0000255|HAMAP-Rule:MF_01602}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-lipoate + ATP + L-lysyl-[lipoyl-carrier protein] = (R)-
CC N(6)-lipoyl-L-lysyl-[lipoyl-carrier protein] + AMP + diphosphate +
CC H(+); Xref=Rhea:RHEA:49288, Rhea:RHEA-COMP:10500, Rhea:RHEA-
CC COMP:10502, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:83088, ChEBI:CHEBI:83099,
CC ChEBI:CHEBI:456215; EC=6.3.1.20; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01602};
CC -!- PATHWAY: Protein modification; protein lipoylation via exogenous
CC pathway; protein N(6)-(lipoyl)lysine from lipoate: step 1/2.
CC {ECO:0000255|HAMAP-Rule:MF_01602}.
CC -!- PATHWAY: Protein modification; protein lipoylation via exogenous
CC pathway; protein N(6)-(lipoyl)lysine from lipoate: step 2/2.
CC {ECO:0000255|HAMAP-Rule:MF_01602}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01602}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01602}.
CC -!- MISCELLANEOUS: In the transfer reaction, the free carboxyl group of
CC lipoic acid is attached via an amide linkage to the epsilon-amino group
CC of a specific lysine residue of lipoyl domains of lipoate-dependent
CC enzymes. {ECO:0000255|HAMAP-Rule:MF_01602}.
CC -!- SIMILARITY: Belongs to the LplA family. {ECO:0000255|HAMAP-
CC Rule:MF_01602}.
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DR EMBL; CP000647; ABR80184.1; -; Genomic_DNA.
DR RefSeq; WP_002887791.1; NC_009648.1.
DR AlphaFoldDB; A6TI00; -.
DR SMR; A6TI00; -.
DR STRING; 272620.KPN_04841; -.
DR EnsemblBacteria; ABR80184; ABR80184; KPN_04841.
DR KEGG; kpn:KPN_04841; -.
DR HOGENOM; CLU_022986_0_1_6; -.
DR OMA; RTCPEDD; -.
DR UniPathway; UPA00537; UER00594.
DR UniPathway; UPA00537; UER00595.
DR Proteomes; UP000000265; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016979; F:lipoate-protein ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009249; P:protein lipoylation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.930.10; -; 1.
DR HAMAP; MF_01602; LplA; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004143; BPL_LPL_catalytic.
DR InterPro; IPR023741; Lipoate_ligase_A.
DR InterPro; IPR019491; Lipoate_protein_ligase_C.
DR InterPro; IPR004562; LipoylTrfase_LipoateP_Ligase.
DR PANTHER; PTHR12561; PTHR12561; 1.
DR Pfam; PF03099; BPL_LplA_LipB; 1.
DR Pfam; PF10437; Lip_prot_lig_C; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00545; lipoyltrans; 1.
DR PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Ligase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..338
FT /note="Lipoate-protein ligase A"
FT /id="PRO_1000069384"
FT DOMAIN 29..216
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01067"
FT BINDING 71
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01602"
FT BINDING 76..79
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01602"
FT BINDING 134
FT /ligand="(R)-lipoate"
FT /ligand_id="ChEBI:CHEBI:83088"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01602"
FT BINDING 134
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01602"
SQ SEQUENCE 338 AA; 37727 MW; 8040CFF37720BC10 CRC64;
MSTLRLLLSD SYDPWFNLAV EECIFRQMPA TQRVLFLWRN ADTVVIGRAQ NPWKECNTRR
MEEDHVRLAR RSSGGGAVFH DLGNTCFTFM AGKPEYDKTV STAIVLAALN SLGVTAEASG
RNDLVVKTDS GDRKVSGSAY RETMDRGFHH GTLLLNADLS RLANYLNPDQ KKLQAKGITS
VRGRVANLVE LLPGITHQQV CEAIQEAFFS HYGERVDAEV ISPDNTPDLP NFAETFARQS
SWEWNFGQAP AFSHLLDERF RWGGVELHFD VEKGHITRAQ AFTDSLNPAP LEALAARLVG
CQYRAEVLQQ QCEALVGDFP EQEAELKELS AWIAGAVR
