ACSA_BACSU
ID ACSA_BACSU Reviewed; 572 AA.
AC P39062;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Acetyl-coenzyme A synthetase;
DE Short=AcCoA synthetase;
DE Short=Acs;
DE EC=6.2.1.1;
DE AltName: Full=Acetate--CoA ligase;
DE AltName: Full=Acyl-activating enzyme;
GN Name=acsA; OrderedLocusNames=BSU29680;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN SPORULATION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=168;
RX PubMed=7934817; DOI=10.1111/j.1365-2958.1993.tb01952.x;
RA Grundy F.J., Waters D.A., Takova T.Y., Henkin T.M.;
RT "Identification of genes involved in utilization of acetate and acetoin in
RT Bacillus subtilis.";
RL Mol. Microbiol. 10:259-271(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9387221; DOI=10.1099/00221287-143-11-3431;
RA Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT "Sequencing and functional annotation of the Bacillus subtilis genes in the
RT 200 kb rrnB-dnaB region.";
RL Microbiology 143:3431-3441(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP INTERACTION WITH FLOT, AND SUBCELLULAR LOCATION.
RC STRAIN=168;
RX PubMed=23651456; DOI=10.1111/mmi.12252;
RA Bach J.N., Bramkamp M.;
RT "Flotillins functionally organize the bacterial membrane.";
RL Mol. Microbiol. 88:1205-1217(2013).
CC -!- FUNCTION: Catalyzes the conversion of acetate into acetyl-CoA (AcCoA),
CC an essential intermediate at the junction of anabolic and catabolic
CC pathways. AcsA undergoes a two-step reaction. In the first half
CC reaction, AcsA combines acetate with ATP to form acetyl-adenylate
CC (AcAMP) intermediate. In the second half reaction, it can then transfer
CC the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the
CC product AcCoA (By similarity). Has a role in growth and sporulation on
CC acetate. {ECO:0000250, ECO:0000269|PubMed:7934817}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate;
CC Xref=Rhea:RHEA:23176, ChEBI:CHEBI:30089, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:456215; EC=6.2.1.1;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBUNIT: Interacts with FloT. {ECO:0000269|PubMed:23651456}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23651456}.
CC Membrane raft {ECO:0000269|PubMed:23651456}. Note=Present in detergent-
CC resistant membrane (DRM) fractions that may be equivalent to eukaryotic
CC membrane rafts; these rafts include proteins involved in signaling,
CC molecule trafficking and protein secretion.
CC {ECO:0000269|PubMed:23651456}.
CC -!- PTM: Acetylated. Deacetylation by the SIR2-homolog deacetylase
CC activates the enzyme (By similarity). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Disruption of this gene induces a loss of the
CC ability to utilize acetate as a carbon source for growth or
CC sporulation. {ECO:0000269|PubMed:7934817}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; L17309; AAA68287.1; -; Genomic_DNA.
DR EMBL; AF008220; AAC00302.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14946.1; -; Genomic_DNA.
DR PIR; S39646; S39646.
DR RefSeq; NP_390846.1; NC_000964.3.
DR RefSeq; WP_004399030.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P39062; -.
DR SMR; P39062; -.
DR STRING; 224308.BSU29680; -.
DR PaxDb; P39062; -.
DR PRIDE; P39062; -.
DR EnsemblBacteria; CAB14946; CAB14946; BSU_29680.
DR GeneID; 937324; -.
DR KEGG; bsu:BSU29680; -.
DR PATRIC; fig|224308.179.peg.3226; -.
DR eggNOG; COG0365; Bacteria.
DR InParanoid; P39062; -.
DR OMA; DHWWHDL; -.
DR PhylomeDB; P39062; -.
DR BioCyc; BSUB:BSU29680-MON; -.
DR SABIO-RK; P39062; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003987; F:acetate-CoA ligase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006085; P:acetyl-CoA biosynthetic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW Acetylation; ATP-binding; Cell membrane; Ligase; Magnesium; Membrane;
KW Metal-binding; Nucleotide-binding; Reference proteome.
FT CHAIN 1..572
FT /note="Acetyl-coenzyme A synthetase"
FT /id="PRO_0000208354"
FT BINDING 260
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 333..335
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 354..359
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 440
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 455
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 463
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 466
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 477
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 479
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 482
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 524
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT MOD_RES 549
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 572 AA; 64892 MW; 2E16BB907A253F97 CRC64;
MNLKALPAIE GDHNLKNYEE TYRHFDWAEA EKHFSWHETG KLNAAYEAID RHAESFRKNK
VALYYKDAKR DEKYTFKEMK EESNRAGNVL RRYGNVEKGD RVFIFMPRSP ELYFIMLGAI
KIGAIAGPLF EAFMEGAVKD RLENSEAKVV VTTPELLERI PVDKLPHLQH VFVVGGEAES
GTNIINYDEA AKQESTRLDI EWMDKKDGFL LHYTSGSTGT PKGVLHVHEA MIQQYQTGKW
VLDLKEEDIY WCTADPGWVT GTVYGIFAPW LNGATNVIVG GRFSPESWYG TIEQLGVNVW
YSAPTAFRML MGAGDEMAAK YDLTSLRHVL SVGEPLNPEV IRWGHKVFNK RIHDTWWMTE
TGSQLICNYP CMDIKPGSMG KPIPGVEAAI VDNQGNELPP YRMGNLAIKK GWPSMMHTIW
NNPEKYESYF MPGGWYVSGD SAYMDEEGYF WFQGRVDDVI MTSGERVGPF EVESKLVEHP
AIAEAGVIGK PDPVRGEIIK AFIALREGFE PSDKLKEEIR LFVKQGLAAH AAPREIEFKD
KLPKTRSGKI MRRVLKAWEL NLPAGDLSTM ED
