ACSA_SALTY
ID ACSA_SALTY Reviewed; 652 AA.
AC Q8ZKF6;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Acetyl-coenzyme A synthetase {ECO:0000255|HAMAP-Rule:MF_01123};
DE Short=AcCoA synthetase {ECO:0000255|HAMAP-Rule:MF_01123};
DE Short=Acs {ECO:0000255|HAMAP-Rule:MF_01123};
DE EC=6.2.1.1 {ECO:0000255|HAMAP-Rule:MF_01123};
DE AltName: Full=Acetate--CoA ligase {ECO:0000255|HAMAP-Rule:MF_01123};
DE AltName: Full=Acyl-activating enzyme {ECO:0000255|HAMAP-Rule:MF_01123};
GN Name=acs {ECO:0000255|HAMAP-Rule:MF_01123}; OrderedLocusNames=STM4275;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP ACETYLATION AT LYS-609, AND DEACETYLATION BY SIR2 HOMOLOG.
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=12493915; DOI=10.1126/science.1077650;
RA Starai V.J., Celic I., Cole R.N., Boeke J.D., Escalante-Semerena J.C.;
RT "Sir2-dependent activation of acetyl-CoA synthetase by deacetylation of
RT active lysine.";
RL Science 298:2390-2392(2002).
RN [3]
RP ACETYLATION AT LYS-609.
RC STRAIN=LT2;
RX PubMed=15236963; DOI=10.1016/j.jmb.2004.05.010;
RA Starai V.J., Escalante-Semerena J.C.;
RT "Identification of the protein acetyltransferase (Pat) enzyme that
RT acetylates acetyl-CoA synthetase in Salmonella enterica.";
RL J. Mol. Biol. 340:1005-1012(2004).
RN [4]
RP FUNCTION.
RC STRAIN=LT2;
RX PubMed=16272400; DOI=10.1099/mic.0.28156-0;
RA Starai V.J., Garrity J., Escalante-Semerena J.C.;
RT "Acetate excretion during growth of Salmonella enterica on ethanolamine
RT requires phosphotransacetylase (EutD) activity, and acetate recapture
RT requires acetyl-CoA synthetase (Acs) and phosphotransacetylase (Pta)
RT activities.";
RL Microbiology 151:3793-3801(2005).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH ATP ANALOG AND
RP COENZYME A, AND SUBUNIT.
RX PubMed=12627952; DOI=10.1021/bi0271603;
RA Gulick A.M., Starai V.J., Horswill A.R., Homick K.M.,
RA Escalante-Semerena J.C.;
RT "The 1.75 A crystal structure of acetyl-CoA synthetase bound to adenosine-
RT 5'-propylphosphate and coenzyme A.";
RL Biochemistry 42:2866-2873(2003).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.42 ANGSTROMS) OF WILD-TYPE AND MUTANTS IN COMPLEX
RP WITH THE ATP ANALOG AMP; COENZYME A AND MAGNESIUM IONS, FUNCTION,
RP MUTAGENESIS OF ARG-194; ALA-357; ASP-517; GLY-524; ARG-526; ARG-584 AND
RP LYS-609, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=17497934; DOI=10.1021/bi6026506;
RA Reger A.S., Carney J.M., Gulick A.M.;
RT "Biochemical and crystallographic analysis of substrate binding and
RT conformational changes in acetyl-CoA synthetase.";
RL Biochemistry 46:6536-6546(2007).
CC -!- FUNCTION: Catalyzes the conversion of acetate into acetyl-CoA (AcCoA),
CC an essential intermediate at the junction of anabolic and catabolic
CC pathways. Acs undergoes a two-step reaction. In the first half
CC reaction, Acs 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. Required for acetate recapture but not for acetate
CC excretion when this organism is grown on ethanolamine
CC (PubMed:16272400). {ECO:0000255|HAMAP-Rule:MF_01123,
CC ECO:0000269|PubMed:16272400, ECO:0000269|PubMed:17497934}.
CC -!- FUNCTION: Enables the cell to use acetate during aerobic growth to
CC generate energy via the TCA cycle, and biosynthetic compounds via the
CC glyoxylate shunt. Acetylates CheY, the response regulator involved in
CC flagellar movement and chemotaxis. {ECO:0000255|HAMAP-Rule:MF_01123}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01123};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=77.1 uM for ATP (at pH 7.5 and at 37 degrees Celsius)
CC {ECO:0000269|PubMed:17497934};
CC KM=50 uM for CoA (at pH 7.5 and at 37 degrees Celsius)
CC {ECO:0000269|PubMed:17497934};
CC KM=6047 uM for acetate (at pH 7.5 and at 37 degrees Celsius)
CC {ECO:0000269|PubMed:17497934};
CC KM=9413 uM for propionate (at pH 7.5 and at 37 degrees Celsius)
CC {ECO:0000269|PubMed:17497934};
CC KM=9450 uM for glycine (at pH 7.5 and at 37 degrees Celsius)
CC {ECO:0000269|PubMed:17497934};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12627952,
CC ECO:0000269|PubMed:17497934}.
CC -!- PTM: Acetylated. Deacetylation by the SIR2-homolog deacetylase
CC activates the enzyme. {ECO:0000255|HAMAP-Rule:MF_01123,
CC ECO:0000269|PubMed:12493915, ECO:0000269|PubMed:15236963}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000255|HAMAP-Rule:MF_01123}.
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; AE006468; AAL23099.1; -; Genomic_DNA.
DR RefSeq; NP_463140.1; NC_003197.2.
DR RefSeq; WP_000083882.1; NC_003197.2.
DR PDB; 1PG3; X-ray; 2.30 A; A/B=1-652.
DR PDB; 1PG4; X-ray; 1.75 A; A/B=1-652.
DR PDB; 2P20; X-ray; 2.22 A; A/B=1-652.
DR PDB; 2P2B; X-ray; 2.20 A; A/B=1-652.
DR PDB; 2P2F; X-ray; 2.58 A; A/B=1-652.
DR PDB; 2P2J; X-ray; 2.30 A; A/B=1-652.
DR PDB; 2P2M; X-ray; 2.11 A; A/B=1-652.
DR PDB; 2P2Q; X-ray; 2.42 A; A/B=1-652.
DR PDB; 5JRH; X-ray; 1.64 A; A/B=1-652.
DR PDBsum; 1PG3; -.
DR PDBsum; 1PG4; -.
DR PDBsum; 2P20; -.
DR PDBsum; 2P2B; -.
DR PDBsum; 2P2F; -.
DR PDBsum; 2P2J; -.
DR PDBsum; 2P2M; -.
DR PDBsum; 2P2Q; -.
DR PDBsum; 5JRH; -.
DR AlphaFoldDB; Q8ZKF6; -.
DR SMR; Q8ZKF6; -.
DR STRING; 99287.STM4275; -.
DR DrugBank; DB03230; Adenosine-5'-Propylphosphate.
DR DrugBank; DB01992; Coenzyme A.
DR iPTMnet; Q8ZKF6; -.
DR PaxDb; Q8ZKF6; -.
DR EnsemblBacteria; AAL23099; AAL23099; STM4275.
DR GeneID; 1255801; -.
DR KEGG; stm:STM4275; -.
DR PATRIC; fig|99287.12.peg.4496; -.
DR HOGENOM; CLU_000022_3_6_6; -.
DR OMA; DHWWHDL; -.
DR PhylomeDB; Q8ZKF6; -.
DR BioCyc; SENT99287:STM4275-MON; -.
DR SABIO-RK; Q8ZKF6; -.
DR EvolutionaryTrace; Q8ZKF6; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0003987; F:acetate-CoA ligase activity; IDA:CACAO.
DR GO; GO:0016208; F:AMP binding; IEA:InterPro.
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 GO; GO:0019427; P:acetyl-CoA biosynthetic process from acetate; IEA:UniProtKB-UniRule.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR HAMAP; MF_01123; Ac_CoA_synth; 1.
DR InterPro; IPR011904; Ac_CoA_lig.
DR InterPro; IPR032387; ACAS_N.
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; PF16177; ACAS_N; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR TIGRFAMs; TIGR02188; Ac_CoA_lig_AcsA; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Ligase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..652
FT /note="Acetyl-coenzyme A synthetase"
FT /id="PRO_0000208386"
FT BINDING 191..194
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT BINDING 311
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123,
FT ECO:0000269|PubMed:12627952, ECO:0000269|PubMed:17497934"
FT BINDING 335
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123,
FT ECO:0000269|PubMed:12627952, ECO:0000269|PubMed:17497934"
FT BINDING 387..389
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 411..416
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 500
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 515
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 523
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123,
FT ECO:0000269|PubMed:12627952, ECO:0000269|PubMed:17497934"
FT BINDING 526
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 537
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 539
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 542
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 584
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123,
FT ECO:0000269|PubMed:12627952, ECO:0000269|PubMed:17497934"
FT SITE 517
FT /note="Hinge residue important for conformational
FT flexibility"
FT MOD_RES 609
FT /note="N6-acetyllysine; by Pat"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01123,
FT ECO:0000269|PubMed:12493915, ECO:0000269|PubMed:15236963"
FT MUTAGEN 194
FT /note="R->A: Results in a 2-fold reduction in the catalytic
FT efficiency for both ATP and CoA. 2-fold increase in the
FT affinity for ATP and 3-fold reduction for CoA."
FT /evidence="ECO:0000269|PubMed:17497934"
FT MUTAGEN 194
FT /note="R->E: Results in a 2-fold reduction in the catalytic
FT efficiency for both ATP and CoA. 2-fold increase in the
FT affinity for ATP and 2-fold reduction for CoA."
FT /evidence="ECO:0000269|PubMed:17497934"
FT MUTAGEN 357
FT /note="A->V: Results in a 2-fold reduction in the catalytic
FT efficiency for both ATP and CoA. 3-fold increase in the
FT affinity for ATP and 3-fold reduction for CoA."
FT /evidence="ECO:0000269|PubMed:17497934"
FT MUTAGEN 517
FT /note="D->G: Results in a 2-fold reduction in the catalytic
FT efficiency for both ATP and CoA. 2-fold increase in the
FT affinity for ATP and 10-fold reduction for CoA."
FT /evidence="ECO:0000269|PubMed:17497934"
FT MUTAGEN 517
FT /note="D->P: Results in a 2-fold reduction in the catalytic
FT efficiency for both ATP and CoA. 3-fold reduction in the
FT affinity for ATP and 4.5-fold reduction for CoA."
FT /evidence="ECO:0000269|PubMed:17497934"
FT MUTAGEN 524
FT /note="G->L: No acetyl-coenzyme A synthetase activity."
FT /evidence="ECO:0000269|PubMed:17497934"
FT MUTAGEN 524
FT /note="G->S: Results in a 2-fold reduction in the catalytic
FT efficiency for both ATP and CoA. Almost the same affinity
FT as the wild-type for ATP, but 9-fold reduction in the
FT affinity for CoA."
FT /evidence="ECO:0000269|PubMed:17497934"
FT MUTAGEN 526
FT /note="R->A: Results in a 2-fold reduction in the catalytic
FT efficiency for both ATP and CoA. 3-fold increase in the
FT affinity for ATP and 4-fold reduction for CoA."
FT /evidence="ECO:0000269|PubMed:17497934"
FT MUTAGEN 584
FT /note="R->A: Results in a 2-fold reduction in the catalytic
FT efficiency for both ATP and CoA. 2-fold increase in the
FT affinity for ATP and 7-fold reduction for CoA."
FT /evidence="ECO:0000269|PubMed:17497934"
FT MUTAGEN 584
FT /note="R->E: Results in a 2-fold reduction in the catalytic
FT efficiency for both ATP and CoA. 3-fold increase in the
FT affinity for ATP and 8-fold reduction for CoA."
FT /evidence="ECO:0000269|PubMed:17497934"
FT MUTAGEN 609
FT /note="K->A: No acetyl-coenzyme A synthetase activity."
FT /evidence="ECO:0000269|PubMed:17497934"
FT HELIX 11..16
FT /evidence="ECO:0007829|PDB:5JRH"
FT HELIX 21..33
FT /evidence="ECO:0007829|PDB:5JRH"
FT HELIX 35..42
FT /evidence="ECO:0007829|PDB:5JRH"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:5JRH"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:5JRH"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:5JRH"
FT HELIX 77..81
FT /evidence="ECO:0007829|PDB:5JRH"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:5JRH"
FT HELIX 86..89
FT /evidence="ECO:0007829|PDB:5JRH"
FT STRAND 92..98
FT /evidence="ECO:0007829|PDB:5JRH"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:5JRH"
FT HELIX 110..126
FT /evidence="ECO:0007829|PDB:5JRH"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:5JRH"
FT HELIX 143..155
FT /evidence="ECO:0007829|PDB:5JRH"
FT STRAND 158..161
FT /evidence="ECO:0007829|PDB:5JRH"
FT HELIX 168..178
FT /evidence="ECO:0007829|PDB:5JRH"
FT STRAND 181..187
FT /evidence="ECO:0007829|PDB:5JRH"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:5JRH"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:5JRH"
FT HELIX 198..206
FT /evidence="ECO:0007829|PDB:5JRH"
FT STRAND 216..220
FT /evidence="ECO:0007829|PDB:5JRH"
FT TURN 231..233
FT /evidence="ECO:0007829|PDB:5JRH"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:5JRH"
FT HELIX 237..243
FT /evidence="ECO:0007829|PDB:5JRH"
FT STRAND 257..264
FT /evidence="ECO:0007829|PDB:5JRH"
FT STRAND 267..270
FT /evidence="ECO:0007829|PDB:5JRH"
FT STRAND 272..278
FT /evidence="ECO:0007829|PDB:5JRH"
FT HELIX 279..292
FT /evidence="ECO:0007829|PDB:5JRH"
FT STRAND 300..303
FT /evidence="ECO:0007829|PDB:5JRH"
FT HELIX 310..314
FT /evidence="ECO:0007829|PDB:5JRH"
FT TURN 315..317
FT /evidence="ECO:0007829|PDB:5JRH"
FT HELIX 318..322
FT /evidence="ECO:0007829|PDB:5JRH"
FT STRAND 326..330
FT /evidence="ECO:0007829|PDB:5JRH"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:5JRH"
FT HELIX 341..349
FT /evidence="ECO:0007829|PDB:5JRH"
FT STRAND 352..356
FT /evidence="ECO:0007829|PDB:5JRH"
FT HELIX 358..365
FT /evidence="ECO:0007829|PDB:5JRH"
FT HELIX 366..371
FT /evidence="ECO:0007829|PDB:5JRH"
FT TURN 372..374
FT /evidence="ECO:0007829|PDB:5JRH"
FT STRAND 382..388
FT /evidence="ECO:0007829|PDB:5JRH"
FT HELIX 392..401
FT /evidence="ECO:0007829|PDB:5JRH"
FT TURN 402..405
FT /evidence="ECO:0007829|PDB:5JRH"
FT STRAND 409..413
FT /evidence="ECO:0007829|PDB:5JRH"
FT HELIX 416..418
FT /evidence="ECO:0007829|PDB:5JRH"
FT TURN 427..429
FT /evidence="ECO:0007829|PDB:5JRH"
FT STRAND 438..440
FT /evidence="ECO:0007829|PDB:5JRH"
FT STRAND 446..449
FT /evidence="ECO:0007829|PDB:5JRH"
FT STRAND 458..466
FT /evidence="ECO:0007829|PDB:5JRH"
FT HELIX 481..489
FT /evidence="ECO:0007829|PDB:5JRH"
FT STRAND 490..492
FT /evidence="ECO:0007829|PDB:5JRH"
FT STRAND 495..504
FT /evidence="ECO:0007829|PDB:5JRH"
FT STRAND 510..522
FT /evidence="ECO:0007829|PDB:5JRH"
FT STRAND 525..528
FT /evidence="ECO:0007829|PDB:5JRH"
FT HELIX 529..537
FT /evidence="ECO:0007829|PDB:5JRH"
FT STRAND 542..552
FT /evidence="ECO:0007829|PDB:5JRH"
FT TURN 553..555
FT /evidence="ECO:0007829|PDB:5JRH"
FT STRAND 556..565
FT /evidence="ECO:0007829|PDB:5JRH"
FT HELIX 573..586
FT /evidence="ECO:0007829|PDB:5JRH"
FT HELIX 589..591
FT /evidence="ECO:0007829|PDB:5JRH"
FT STRAND 594..598
FT /evidence="ECO:0007829|PDB:5JRH"
FT STRAND 604..607
FT /evidence="ECO:0007829|PDB:2P2M"
FT HELIX 612..620
FT /evidence="ECO:0007829|PDB:5JRH"
FT HELIX 629..631
FT /evidence="ECO:0007829|PDB:1PG4"
FT STRAND 632..634
FT /evidence="ECO:0007829|PDB:2P2M"
FT HELIX 637..646
FT /evidence="ECO:0007829|PDB:5JRH"
SQ SEQUENCE 652 AA; 72153 MW; 347209D1D3D349D8 CRC64;
MSQTHKHAIP ANIADRCLIN PEQYETKYKQ SINDPDTFWG EQGKILDWIT PYQKVKNTSF
APGNVSIKWY EDGTLNLAAN CLDRHLQENG DRTAIIWEGD DTSQSKHISY RELHRDVCRF
ANTLLDLGIK KGDVVAIYMP MVPEAAVAML ACARIGAVHS VIFGGFSPEA VAGRIIDSSS
RLVITADEGV RAGRSIPLKK NVDDALKNPN VTSVEHVIVL KRTGSDIDWQ EGRDLWWRDL
IEKASPEHQP EAMNAEDPLF ILYTSGSTGK PKGVLHTTGG YLVYAATTFK YVFDYHPGDI
YWCTADVGWV TGHSYLLYGP LACGATTLMF EGVPNWPTPA RMCQVVDKHQ VNILYTAPTA
IRALMAEGDK AIEGTDRSSL RILGSVGEPI NPEAWEWYWK KIGKEKCPVV DTWWQTETGG
FMITPLPGAI ELKAGSATRP FFGVQPALVD NEGHPQEGAT EGNLVITDSW PGQARTLFGD
HERFEQTYFS TFKNMYFSGD GARRDEDGYY WITGRVDDVL NVSGHRLGTA EIESALVAHP
KIAEAAVVGI PHAIKGQAIY AYVTLNHGEE PSPELYAEVR NWVRKEIGPL ATPDVLHWTD
SLPKTRSGKI MRRILRKIAA GDTSNLGDTS TLADPGVVEK LLEEKQAIAM PS
