ID ACSA_BACSU Reviewed; 572 AA. AC P39062; A0A6M4JL50; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 02-SEP-2026, entry version 141. DE RecName: Full=Acetyl-coenzyme A synthetase; DE Short=AcCoA synthetase; DE Short=Acs; DE EC=6.2.1.1 {ECO:0000269|PubMed:39019872, ECO:0000269|PubMed:40089509}; DE AltName: Full=Acetate--CoA ligase; DE AltName: Full=Acyl-activating enzyme; GN Name=acsA; OrderedLocusNames=BSU29680; OS Bacillus subtilis (strain 168). OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae; OC 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] {ECO:0000312|EMBL:QJP89687.1} RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=168 {ECO:0000312|EMBL:QJP89687.1}; RA Dragos A., Kovacs A.T.; RT "Phage recombination drives evolution of spore-forming Bacilli."; RL Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases. RN [5] RP FUNCTION, ACTIVITY REGULATION, AND ACETYLATION AT LYS-549. RX PubMed=16855235; DOI=10.1128/jb.00215-06; RA Gardner J.G., Grundy F.J., Henkin T.M., Escalante-Semerena J.C.; RT "Control of acetyl-coenzyme A synthetase (AcsA) activity by RT acetylation/deacetylation without NAD(+) involvement in Bacillus RT subtilis."; RL J. Bacteriol. 188:5460-5468(2006). RN [6] RP FUNCTION, ACTIVITY REGULATION, ACETYLATION BY ACUA, AND DISRUPTION RP PHENOTYPE. RX PubMed=19136592; DOI=10.1128/jb.01674-08; RA Gardner J.G., Escalante-Semerena J.C.; RT "In Bacillus subtilis, the sirtuin protein deacetylase, encoded by the srtN RT gene (formerly yhdZ), and functions encoded by the acuABC genes control the RT activity of acetyl coenzyme A synthetase."; RL J. Bacteriol. 191:1749-1755(2009). RN [7] 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). RN [8] RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBUNIT, INTERACTION RP WITH ACUA, ACETYLATION AT LYS-549, AND MUTAGENESIS OF GLU-473; VAL-477 AND RP LYS-549. RX PubMed=39019872; DOI=10.1038/s41467-024-49952-0; RA Qin C., Graf L.G., Striska K., Janetzky M., Geist N., Specht R., RA Schulze S., Palm G.J., Girbardt B., Doerre B., Berndt L., Kemnitz S., RA Doerr M., Bornscheuer U.T., Delcea M., Lammers M.; RT "Acetyl-CoA synthetase activity is enzymatically regulated by lysine RT acetylation using acetyl-CoA or acetyl-phosphate as donor molecule."; RL Nat. Commun. 15:6002-6002(2024). RN [9] {ECO:0007744|PDB:9G79, ECO:0007744|PDB:9G7F} RP STRUCTURE BY ELECTRON MICROSCOPY (2.9 ANGSTROMS) IN APO FORM AND IN COMPLEX RP WITH ACUA, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBUNIT, RP INTERACTION WITH ACUA, ACETYLATION AT LYS-549, AND MUTAGENESIS OF ARG-546; RP SER-547 AND LYS-549. RX PubMed=40089509; DOI=10.1038/s41467-025-57842-2; RA Zheng L., Du Y., Steinchen W., Girbig M., Abendroth F., Jalomo-Khayrova E., RA Bedrunka P., Bekeredjian-Ding I., Mais C.N., Hochberg G.K.A., Freitag J., RA Bange G.; RT "Regulation of acetyl-CoA biosynthesis via an intertwined acetyl-CoA RT synthetase/acetyltransferase complex."; RL Nat. Commun. 16:2557-2557(2025). CC -!- FUNCTION: Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), CC an essential intermediate at the junction of anabolic and catabolic CC pathways (PubMed:39019872, PubMed:40089509). AcsA undergoes a two-step CC reaction. In the first half reaction, AcsA combines acetate with ATP to CC form acetyl-adenylate (AcAMP) intermediate (PubMed:39019872, CC PubMed:40089509). In the second half reaction, it can then transfer the CC acetyl group from AcAMP to the sulfhydryl group of CoA, forming the CC product AcCoA (PubMed:39019872, PubMed:40089509). Has a role in growth CC and sporulation on acetate (PubMed:7934817). When complexed to AcuA, CC possesses intrinsic phosphotransacetylase activity, catalyzing the CC transfer of an acetyl group first from acetylphosphate to CoA and then CC to Lys-549 of AcsA (PubMed:39019872). Required for efficient growth CC under low-acetate conditions (PubMed:19136592). Compensates for AcsA in CC S.typhimurium under acetate conditions (PubMed:16855235). CC {ECO:0000269|PubMed:16855235, ECO:0000269|PubMed:19136592, CC ECO:0000269|PubMed:39019872, ECO:0000269|PubMed:40089509, CC 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 Evidence={ECO:0000269|PubMed:39019872, ECO:0000269|PubMed:40089509}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P27550}; CC -!- ACTIVITY REGULATION: Acetylation at Lys-549 by AcuA leads to inhibition CC of catalytic activity (PubMed:16855235, PubMed:39019872, CC PubMed:40089509). Activated by histone-deacetylase type AcuC, probably CC in conjunction with NAD-dependent protein deacetylase SrtN CC (PubMed:16855235, PubMed:19136592, PubMed:39019872). CC {ECO:0000269|PubMed:16855235, ECO:0000269|PubMed:19136592, CC ECO:0000269|PubMed:39019872, ECO:0000269|PubMed:40089509}. CC -!- SUBUNIT: Homodimer (PubMed:39019872, PubMed:40089509). Forms a CC heterotetrameric complex with AcuA consisting of two AcuA-AcsA CC heterodimers (PubMed:39019872, PubMed:40089509). Interacts (via C- CC terminus) with AcuA (via acetyltransferase domain); the interaction is CC direct and the C-terminus of AcuA occupies the CoA-binding site in the CC N-terminal domain of AcsA (PubMed:40089509). The AcuA-AcsA complex CC dissociates upon acetyl-CoA-dependent acetylation of AcsA and when CC acetate levels are high (PubMed:39019872, PubMed:40089509). Interacts CC with FloT (PubMed:23651456). {ECO:0000269|PubMed:23651456, CC ECO:0000269|PubMed:39019872, ECO:0000269|PubMed:40089509}. 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 by acetyltransferase AcuA (PubMed:16855235, CC PubMed:19136592, PubMed:39019872, PubMed:40089509). Deacetylation by CC histone-deacetylase type AcuC activates AcsA (PubMed:16855235, CC PubMed:39019872). SIR2-homolog deacetylase also deacetylates AcsA CC (PubMed:19136592). {ECO:0000269|PubMed:16855235, CC ECO:0000269|PubMed:19136592, ECO:0000269|PubMed:39019872, CC ECO:0000269|PubMed:40089509}. CC -!- DISRUPTION PHENOTYPE: Loses the ability to utilize acetate as a carbon CC source for growth or sporulation. {ECO:0000269|PubMed:19136592, CC ECO:0000269|PubMed:7934817}. 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; L17309; AAA68287.1; -; Genomic_DNA. DR EMBL; AF008220; AAC00302.1; -; Genomic_DNA. DR EMBL; AL009126; CAB14946.1; -; Genomic_DNA. DR EMBL; CP052842; QJP89687.1; -; Genomic_DNA. DR PIR; S39646; S39646. DR RefSeq; NP_390846.1; NC_000964.3. DR RefSeq; WP_004399030.1; NC_000964.3. DR PDB; 9G79; EM; 2.89 A; A/B=1-572. DR PDB; 9G7F; EM; 2.93 A; A/B=1-572. DR AlphaFoldDB; P39062; -. DR EMDB; EMD-51116; -. DR EMDB; EMD-51121; -. DR SMR; P39062; -. DR STRING; 224308.BSU29680; -. DR PaxDb; 224308-BSU29680; -. 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 OrthoDB; 9778383at2; -. DR PhylomeDB; P39062; -. DR BioCyc; BSUB:BSU29680-MONOMER; -. DR SABIO-RK; P39062; -. DR Proteomes; UP000001570; Chromosome. DR AbasyAtlas; P39062; -. 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:acetyl-CoA synthetase activity; IDA:UniProtKB. DR GO; GO:0006085; P:acetyl-CoA biosynthetic process; IDA:UniProtKB. DR CDD; cd05969; MACS_like_4; 1. DR FunFam; 3.30.300.30:FF:000005; Acyl-coenzyme A synthetase ACSM5, mitochondrial; 1. DR Gene3D; 3.30.300.30; -; 1. DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1. DR InterPro; IPR045851; AMP-b_sf. DR InterPro; IPR025110; AMP-bd_C. DR InterPro; IPR020845; AMP-binding_CS. DR InterPro; IPR000873; AMP-dep_synth/lig_dom. DR InterPro; IPR042099; ANL_N_sf. DR NCBIfam; NF003313; PRK04319.1; 1. DR PANTHER; PTHR24095; ACETYL-COENZYME A SYNTHETASE; 1. DR PANTHER; PTHR24095:SF14; ACETYL-COENZYME A SYNTHETASE 1; 1. DR Pfam; PF00501; AMP-binding; 1. DR Pfam; PF13193; AMP-binding_C; 1. DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1. DR PROSITE; PS00455; AMP_BINDING; 1. DR PDBsum; 9G79; -. DR PDBsum; 9G7F; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; ATP-binding; Cell membrane; Ligase; Magnesium; KW Membrane; Metal-binding; Nucleotide-binding; Reference proteome. FT CHAIN 1..572 FT /note="Acetyl-coenzyme A synthetase" FT /id="PRO_0000208354" FT BINDING 255 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000250|UniProtKB:Q8ZKF6" FT BINDING 260 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000250|UniProtKB:Q8ZKF6" FT BINDING 333 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:Q8ZKF6" FT BINDING 354 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:Q8ZKF6" FT BINDING 355 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:Q8ZKF6" FT BINDING 359 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:Q8ZKF6" FT BINDING 440 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:Q8ZKF6" FT BINDING 455 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:Q8ZKF6" FT BINDING 463 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000250|UniProtKB:Q8ZKF6" FT BINDING 464 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000250|UniProtKB:Q8ZKF6" FT BINDING 466 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:Q8ZKF6" FT BINDING 477 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:Q8ZKF6" FT BINDING 479 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:Q8ZKF6" FT BINDING 482 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:Q8ZKF6" FT BINDING 524 FT /ligand="CoA" FT /ligand_id="ChEBI:CHEBI:57287" FT /evidence="ECO:0000250|UniProtKB:Q8ZKF6" FT MOD_RES 549 FT /note="N6-acetyllysine; by AcuA" FT /evidence="ECO:0000269|PubMed:16855235, FT ECO:0000269|PubMed:39019872, ECO:0000269|PubMed:40089509" FT MUTAGEN 473 FT /note="E->A: Impairs the acetylation activity of the FT AcuA-AcsA complex. Reduces the binding affinity of AcsA to FT AcuA." FT /evidence="ECO:0000269|PubMed:39019872" FT MUTAGEN 477 FT /note="V->A: Impairs the acetylation activity of the FT AcuA-AcsA complex. Reduces the binding affinity of AcsA to FT AcuA." FT /evidence="ECO:0000269|PubMed:39019872" FT MUTAGEN 546 FT /note="R->E: Does not affect complex formation with AcuA." FT /evidence="ECO:0000269|PubMed:40089509" FT MUTAGEN 547 FT /note="S->A: Does not affect complex formation with AcuA." FT /evidence="ECO:0000269|PubMed:40089509" FT MUTAGEN 549 FT /note="K->A: Reduces complex formation with AcuA." FT /evidence="ECO:0000269|PubMed:40089509" FT MUTAGEN 549 FT /note="K->Q: Partially dissociates the AcuA-AcsA complex." FT /evidence="ECO:0000269|PubMed:39019872" FT MUTAGEN 549 FT /note="K->R: Abolishes acetylation at this residue by FT AcuA." FT /evidence="ECO:0000269|PubMed:39019872" FT HELIX 18..24 FT /evidence="ECO:0007829|PDB:9G79" FT HELIX 27..30 FT /evidence="ECO:0007829|PDB:9G79" FT HELIX 31..33 FT /evidence="ECO:0007829|PDB:9G79" FT HELIX 36..39 FT /evidence="ECO:0007829|PDB:9G79" FT HELIX 46..50 FT /evidence="ECO:0007829|PDB:9G79" FT HELIX 51..54 FT /evidence="ECO:0007829|PDB:9G7F" FT TURN 56..59 FT /evidence="ECO:0007829|PDB:9G79" FT STRAND 60..66 FT /evidence="ECO:0007829|PDB:9G79" FT STRAND 71..75 FT /evidence="ECO:0007829|PDB:9G79" FT HELIX 76..89 FT /evidence="ECO:0007829|PDB:9G79" FT HELIX 90..94 FT /evidence="ECO:0007829|PDB:9G79" FT STRAND 101..106 FT /evidence="ECO:0007829|PDB:9G79" FT HELIX 110..121 FT /evidence="ECO:0007829|PDB:9G79" FT STRAND 125..128 FT /evidence="ECO:0007829|PDB:9G79" FT HELIX 135..145 FT /evidence="ECO:0007829|PDB:9G79" FT STRAND 148..152 FT /evidence="ECO:0007829|PDB:9G79" FT TURN 154..156 FT /evidence="ECO:0007829|PDB:9G79" FT HELIX 157..159 FT /evidence="ECO:0007829|PDB:9G79" FT HELIX 162..164 FT /evidence="ECO:0007829|PDB:9G79" FT STRAND 170..173 FT /evidence="ECO:0007829|PDB:9G79" FT STRAND 182..186 FT /evidence="ECO:0007829|PDB:9G79" FT HELIX 187..192 FT /evidence="ECO:0007829|PDB:9G79" FT HELIX 200..202 FT /evidence="ECO:0007829|PDB:9G7F" FT STRAND 207..214 FT /evidence="ECO:0007829|PDB:9G79" FT STRAND 222..227 FT /evidence="ECO:0007829|PDB:9G79" FT HELIX 230..240 FT /evidence="ECO:0007829|PDB:9G79" FT STRAND 249..252 FT /evidence="ECO:0007829|PDB:9G79" FT HELIX 259..262 FT /evidence="ECO:0007829|PDB:9G79" FT HELIX 263..267 FT /evidence="ECO:0007829|PDB:9G79" FT HELIX 268..271 FT /evidence="ECO:0007829|PDB:9G79" FT STRAND 275..279 FT /evidence="ECO:0007829|PDB:9G79" FT HELIX 285..295 FT /evidence="ECO:0007829|PDB:9G79" FT STRAND 299..302 FT /evidence="ECO:0007829|PDB:9G79" FT HELIX 304..312 FT /evidence="ECO:0007829|PDB:9G79" FT HELIX 315..319 FT /evidence="ECO:0007829|PDB:9G79" FT STRAND 328..331 FT /evidence="ECO:0007829|PDB:9G79" FT HELIX 335..337 FT /evidence="ECO:0007829|PDB:9G79" FT HELIX 338..347 FT /evidence="ECO:0007829|PDB:9G79" FT STRAND 352..356 FT /evidence="ECO:0007829|PDB:9G79" FT TURN 359..361 FT /evidence="ECO:0007829|PDB:9G79" FT STRAND 378..382 FT /evidence="ECO:0007829|PDB:9G79" FT STRAND 388..391 FT /evidence="ECO:0007829|PDB:9G79" FT STRAND 400..402 FT /evidence="ECO:0007829|PDB:9G7F" FT STRAND 404..410 FT /evidence="ECO:0007829|PDB:9G79" FT STRAND 416..419 FT /evidence="ECO:0007829|PDB:9G79" FT HELIX 423..427 FT /evidence="ECO:0007829|PDB:9G79" FT TURN 432..434 FT /evidence="ECO:0007829|PDB:9G79" FT STRAND 435..444 FT /evidence="ECO:0007829|PDB:9G79" FT STRAND 446..448 FT /evidence="ECO:0007829|PDB:9G7F" FT STRAND 450..452 FT /evidence="ECO:0007829|PDB:9G79" FT HELIX 469..477 FT /evidence="ECO:0007829|PDB:9G7F" FT STRAND 479..492 FT /evidence="ECO:0007829|PDB:9G7F" FT TURN 493..495 FT /evidence="ECO:0007829|PDB:9G7F" FT STRAND 496..505 FT /evidence="ECO:0007829|PDB:9G7F" FT HELIX 513..526 FT /evidence="ECO:0007829|PDB:9G7F" FT STRAND 534..538 FT /evidence="ECO:0007829|PDB:9G7F" FT STRAND 546..548 FT /evidence="ECO:0007829|PDB:9G7F" FT HELIX 553..558 FT /evidence="ECO:0007829|PDB:9G7F" 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 //