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Database: UniProt
Entry: A0A0T9XLI4_SALET
LinkDB: A0A0T9XLI4_SALET
Original site: A0A0T9XLI4_SALET 
ID   A0A0T9XLI4_SALET        Unreviewed;       338 AA.
AC   A0A0T9XLI4;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   23-MAY-2018, entry version 24.
DE   RecName: Full=Lipoate-protein ligase A {ECO:0000256|HAMAP-Rule:MF_01602};
DE            EC=6.3.1.20 {ECO:0000256|HAMAP-Rule:MF_01602};
DE   AltName: Full=Lipoate--protein ligase {ECO:0000256|HAMAP-Rule:MF_01602};
GN   Name=lplA {ECO:0000256|HAMAP-Rule:MF_01602,
GN   ECO:0000313|EMBL:CNU69488.1};
GN   ORFNames=ERS008198_02578 {ECO:0000313|EMBL:CNU35768.1},
GN   ERS008207_03270 {ECO:0000313|EMBL:CNU69488.1}, ERS008210_02119
GN   {ECO:0000313|EMBL:CPR49955.1}, ERS008215_02860
GN   {ECO:0000313|EMBL:CFW73804.1};
OS   Salmonella enterica subsp. enterica serovar Bovismorbificans.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=58097 {ECO:0000313|EMBL:CNU69488.1, ECO:0000313|Proteomes:UP000042394};
RN   [1] {ECO:0000313|Proteomes:UP000039385, ECO:0000313|Proteomes:UP000041314, ECO:0000313|Proteomes:UP000042394}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=51892776 {ECO:0000313|EMBL:CPR49955.1,
RC   ECO:0000313|Proteomes:UP000039385}, A1104
RC   {ECO:0000313|EMBL:CNU35768.1, ECO:0000313|Proteomes:UP000041314},
RC   A31126 {ECO:0000313|EMBL:CFW73804.1,
RC   ECO:0000313|Proteomes:UP000048853}, and D4891
RC   {ECO:0000313|EMBL:CNU69488.1, ECO:0000313|Proteomes:UP000042394};
RA   Murphy D.;
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes both the ATP-dependent activation of
CC       exogenously supplied lipoate to lipoyl-AMP and the transfer of the
CC       activated lipoyl onto the lipoyl domains of lipoate-dependent
CC       enzymes. {ECO:0000256|HAMAP-Rule:MF_01602,
CC       ECO:0000256|SAAS:SAAS00894010}.
CC   -!- CATALYTIC ACTIVITY: ATP + (R)-lipoate + a [lipoyl-carrier
CC       protein]-L-lysine = a [lipoyl-carrier protein]-N(6)-(lipoyl)lysine
CC       + AMP + diphosphate. {ECO:0000256|HAMAP-Rule:MF_01602,
CC       ECO:0000256|SAAS:SAAS00603726}.
CC   -!- PATHWAY: Protein modification; protein lipoylation via exogenous
CC       pathway; protein N(6)-(lipoyl)lysine from lipoate: step 2/2.
CC       {ECO:0000256|HAMAP-Rule:MF_01602, ECO:0000256|SAAS:SAAS00701662}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01602,
CC       ECO:0000256|SAAS:SAAS00894007}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01602,
CC       ECO:0000256|SAAS:SAAS00894009}.
CC   -!- MISCELLANEOUS: In the transfer reaction, the free carboxyl group
CC       of lipoic acid is attached via an amide linkage to the epsilon-
CC       amino group of a specific lysine residue of lipoyl domains of
CC       lipoate-dependent enzymes. {ECO:0000256|HAMAP-Rule:MF_01602}.
CC   -!- SIMILARITY: Belongs to the LplA family. {ECO:0000256|HAMAP-
CC       Rule:MF_01602, ECO:0000256|SAAS:SAAS00894016}.
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DR   EMBL; CGIA01000010; CFW73804.1; -; Genomic_DNA.
DR   EMBL; CQPA01000019; CNU35768.1; -; Genomic_DNA.
DR   EMBL; CQPD01000035; CNU69488.1; -; Genomic_DNA.
DR   EMBL; CSTI01000010; CPR49955.1; -; Genomic_DNA.
DR   RefSeq; WP_000209756.1; NZ_MZFY01000010.1.
DR   EnsemblBacteria; CFW73804; CFW73804; ERS008215_02860.
DR   EnsemblBacteria; CNU35768; CNU35768; ERS008198_02578.
DR   EnsemblBacteria; CNU69488; CNU69488; ERS008207_03270.
DR   EnsemblBacteria; CPR49955; CPR49955; ERS008210_02119.
DR   UniPathway; UPA00537; UER00595.
DR   Proteomes; UP000039385; Unassembled WGS sequence.
DR   Proteomes; UP000041314; Unassembled WGS sequence.
DR   Proteomes; UP000042394; Unassembled WGS sequence.
DR   Proteomes; UP000048853; Unassembled WGS sequence.
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   HAMAP; MF_01602; LplA; 1.
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   PANTHER; PTHR12561:SF5; PTHR12561:SF5; 1.
DR   Pfam; PF03099; BPL_LplA_LipB; 1.
DR   Pfam; PF10437; Lip_prot_lig_C; 1.
DR   TIGRFAMs; TIGR00545; lipoyltrans; 1.
DR   PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01602,
KW   ECO:0000256|SAAS:SAAS00428641};
KW   Complete proteome {ECO:0000313|Proteomes:UP000039385,
KW   ECO:0000313|Proteomes:UP000041314, ECO:0000313|Proteomes:UP000042394,
KW   ECO:0000313|Proteomes:UP000048853};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01602,
KW   ECO:0000256|SAAS:SAAS00894000};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_01602,
KW   ECO:0000256|SAAS:SAAS00603725, ECO:0000313|EMBL:CNU69488.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01602,
KW   ECO:0000256|SAAS:SAAS00026749};
KW   Nucleotidyltransferase {ECO:0000313|EMBL:CNU69488.1};
KW   Transferase {ECO:0000313|EMBL:CNU69488.1}.
FT   DOMAIN       29    216       BPL/LPL catalytic. {ECO:0000259|PROSITE:
FT                                PS51733}.
FT   NP_BIND      76     79       ATP. {ECO:0000256|HAMAP-Rule:MF_01602}.
FT   BINDING      71     71       ATP. {ECO:0000256|HAMAP-Rule:MF_01602}.
FT   BINDING     134    134       ATP. {ECO:0000256|HAMAP-Rule:MF_01602}.
FT   BINDING     134    134       Lipoate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01602}.
SQ   SEQUENCE   338 AA;  37935 MW;  3C1FB7628029847C CRC64;
     MTTLRLLISD SYDPWFNLAV EECIFRQMPA TQRVLFLWRN ADTVVIGRAQ NPWKECNTRR
     MEEDNVRLAR RSSGGGAVFH DLGNTCFTFM AGKPEYDKTI STHIVLAALN SLGVMADASG
     RNDLVVKTPD GDRKVSGSAY RETKDRGFHH GTLLLNADLS RLANYLNPDK KKLAAKGITS
     VRSRVANLTE LLPGITHEQV CQAVTEAFFA HYGERVDAEV ISPDKTPDLP NFAETFARQS
     SWEWNFGQAP AFSHLLDERF TWGGVELHFD VEKGVITRAQ AFTDSLNPAP LEALAERLQG
     CLYRADKLQE TCEALLVDFP EQEKELRELS AWIAEAVR
//
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