ID   VRAA_STAA1              Reviewed;         458 AA.
AC   Q9KWK5; A7WZ14;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 3.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Putative long chain fatty acid-CoA ligase VraA;
DE            EC=6.2.1.-;
DE   AltName: Full=Acyl-CoA synthetase;
GN   Name=vraA; OrderedLocusNames=SAHV_0573;
OS   Staphylococcus aureus (strain Mu3 / ATCC 700698).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=418127;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VANCOMYCIN RESISTANCE.
RX   PubMed=10708580; DOI=10.1006/bbrc.2000.2277;
RA   Kuroda M., Kuwahara-Arai K., Hiramatsu K.;
RT   "Identification of the up- and down-regulated genes in vancomycin-resistant
RT   Staphylococcus aureus strains Mu3 and Mu50 by cDNA differential
RT   hybridization method.";
RL   Biochem. Biophys. Res. Commun. 269:485-490(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mu3 / ATCC 700698;
RX   PubMed=17954695; DOI=10.1128/aac.00534-07;
RA   Neoh H.-M., Cui L., Yuzawa H., Takeuchi F., Matsuo M., Hiramatsu K.;
RT   "Mutated response regulator graR is responsible for phenotypic conversion
RT   of Staphylococcus aureus from heterogeneous vancomycin-intermediate
RT   resistance to vancomycin-intermediate resistance.";
RL   Antimicrob. Agents Chemother. 52:45-53(2008).
CC   -!- MISCELLANEOUS: May contribute to vancomycin resistance.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; AB035449; BAB03327.2; -; Genomic_DNA.
DR   EMBL; AP009324; BAF77456.1; -; Genomic_DNA.
DR   RefSeq; WP_001100835.1; NC_009782.1.
DR   AlphaFoldDB; Q9KWK5; -.
DR   SMR; Q9KWK5; -.
DR   KEGG; saw:SAHV_0573; -.
DR   HOGENOM; CLU_000022_59_0_9; -.
DR   OMA; WFESVCK; -.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; -; 1.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR042099; ANL_N_sf.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   3: Inferred from homology;
KW   Fatty acid metabolism; Ligase; Lipid metabolism.
FT   CHAIN           1..458
FT                   /note="Putative long chain fatty acid-CoA ligase VraA"
FT                   /id="PRO_0000193190"
FT   CONFLICT        159
FT                   /note="E -> Q (in Ref. 1; BAB03327)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   458 AA;  52024 MW;  0843B823F1F5267B CRC64;
     MNVILEQLKT HTQNKPNDIA LHIDDETITY SQLNARITSA VESLQKYSLN PVVAINMKSP
     VQSIICYLAL HRLHKVPMMM EGKWQSTIHR QLIEKYGIKD VIGDTGLMQN IDSPMFIDST
     QLQHYPNLLH IGFTSGTTGL PKAYYRDEDS WLASFEVNEM LMLKNENAIA APGPLSHSLT
     LYALLFALSS GRTFIGQTTF HPEKLLNQCH KISSYKVAMF LVPTMIKSLL LVYNNEHTIQ
     SFFSSGDKLH SSIFKKIKNQ ANDINLIEFF GTSETSFISY NLNQQAPVES VGVLFPNVEL
     KTTNHDHNGI GTICIKSNMM FSGYVSEQCI NNDEWFVTND NGYVKEQYLY LTGRQQDMLI
     IGGQNIYPAH VERLLTQSSS IDEAIIIGIP NERFGQIGVL LYSGDVTLTH KNVKQFLKKK
     VKRYEIPSMI HHVEKMYYTA SGKIAREKMM SMYLRGEL