VRAA_STAEQ
ID VRAA_STAEQ Reviewed; 453 AA.
AC Q5HRH4;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 75.
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=SERP0219;
OS Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176279;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35984 / RP62A;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000029; AAW53591.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5HRH4; -.
DR SMR; Q5HRH4; -.
DR STRING; 176279.SERP0219; -.
DR EnsemblBacteria; AAW53591; AAW53591; SERP0219.
DR KEGG; ser:SERP0219; -.
DR eggNOG; COG0318; Bacteria.
DR HOGENOM; CLU_000022_59_0_9; -.
DR OMA; WFESVCK; -.
DR Proteomes; UP000000531; Chromosome.
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; 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 PROSITE; PS00455; AMP_BINDING; 1.
PE 3: Inferred from homology;
KW Fatty acid metabolism; Ligase; Lipid metabolism; Reference proteome.
FT CHAIN 1..453
FT /note="Putative long chain fatty acid-CoA ligase VraA"
FT /id="PRO_0000193198"
SQ SEQUENCE 453 AA; 51758 MW; 73199CA2D09B11FD CRC64;
MKKIMEYLQH YINQYPHRLA LVFEDRHLTY GELSKEIYQA SMRYKEVKLN EKVGLMDDHP
VNNIINYFAV HQRGGIPCIF NHQWSNERIH QLVKSYDIQW LIKDNHLTLN HDDSIYNDEV
IPRNVIHIGF TSGTTGLPKA FYRNEHSWIV SFKENEKLLQ HCEETIVAPG PLSHSLSLYA
CIYALSTGKT FIGQKNFNPL SLMRLINQLN KATAIFVVPT MVQQLISTQR HCSSIKSILS
SGAKLTLQQF QQISTLYPQA NLIEFFGTSE ASFISYNFNQ SSPAHSVGKL FPHVETRLLN
QDDDAVGLLA VRSEMVFSGY VGQSNQEGSW IKTGDFAYIK NQHLFLVGRE SDRIIVGGIN
VYPTAIESLI MDIEGIDEAL VIGIPHAKFG EIAILLYSGK VQLNYRQIKS FLMKQLSRQE
VPSKLKKIDH MIYTESGKIA RKEMKNKFIN GEL