ID ATPA_ECOLI Reviewed; 513 AA.
AC P0ABB0; P00822; Q2M852; Q47249;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 27-MAR-2024, entry version 152.
DE RecName: Full=ATP synthase subunit alpha {ECO:0000255|HAMAP-Rule:MF_01346};
DE EC=7.1.2.2 {ECO:0000255|HAMAP-Rule:MF_01346};
DE AltName: Full=ATP synthase F1 sector subunit alpha {ECO:0000255|HAMAP-Rule:MF_01346};
DE AltName: Full=F-ATPase subunit alpha {ECO:0000255|HAMAP-Rule:MF_01346};
GN Name=atpA {ECO:0000255|HAMAP-Rule:MF_01346}; Synonyms=papA, uncA;
GN OrderedLocusNames=b3734, JW3712;
OS Escherichia coli (strain K12).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6395859; DOI=10.1042/bj2240799;
RA Walker J.E., Gay N.J., Saraste M., Eberle A.N.;
RT "DNA sequence around the Escherichia coli unc operon. Completion of the
RT sequence of a 17 kilobase segment containing asnA, oriC, unc, glmS and
RT phoS.";
RL Biochem. J. 224:799-815(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6272228; DOI=10.1093/nar/9.9.2187;
RA Gay N.J., Walker J.E.;
RT "The atp operon: nucleotide sequence of the region encoding the alpha-
RT subunit of Escherichia coli ATP-synthase.";
RL Nucleic Acids Res. 9:2187-2194(1981).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6277310; DOI=10.1016/0006-291x(81)90494-0;
RA Kanazawa H., Kayano T., Mabuchi K., Futai M.;
RT "Nucleotide sequence of the genes coding for alpha, beta and gamma subunits
RT of the proton-translocating ATPase of Escherichia coli.";
RL Biochem. Biophys. Res. Commun. 103:604-612(1981).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6301339; DOI=10.1111/j.1749-6632.1982.tb25731.x;
RA Kanazawa H., Futai M.;
RT "Structure and function of H+-ATPase: what we have learned from Escherichia
RT coli H+-ATPase.";
RL Ann. N. Y. Acad. Sci. 402:45-64(1982).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7686882; DOI=10.1006/geno.1993.1230;
RA Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.;
RT "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome:
RT organizational symmetry around the origin of replication.";
RL Genomics 16:551-561(1993).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-50.
RX PubMed=6278247; DOI=10.1007/bf00271191;
RA Nielsen J., Hansen F.G., Hoppe J., Friedl P., von Meyenburg K.;
RT "The nucleotide sequence of the atp genes coding for the F0 subunits a, b,
RT c and the F1 subunit delta of the membrane bound ATP synthase of
RT Escherichia coli.";
RL Mol. Gen. Genet. 184:33-39(1981).
RN [9]
RP SEQUENCE REVISION TO 239-244.
RX PubMed=2868922; DOI=10.1016/0014-5793(86)80310-6;
RA Slan-Lotter H., Clarke D.M., Bragg P.D.;
RT "Isolation of a fourth cysteinyl-containing peptide of the alpha-subunit of
RT the F1 ATPase from Escherichia coli necessitates revision of the DNA
RT sequence.";
RL FEBS Lett. 197:121-124(1986).
RN [10]
RP PROTEIN SEQUENCE OF 1-8.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Pasquali C., Sanchez J.-C., Ravier F., Golaz O., Hughes G.J., Frutiger S.,
RA Paquet N., Wilkins M., Appel R.D., Bairoch A., Hochstrasser D.F.;
RL Submitted (SEP-1994) to UniProtKB.
RN [11]
RP PROTEIN SEQUENCE OF 1-12.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [12]
RP MUTAGENESIS OF LYS-175.
RX PubMed=2903146; DOI=10.1016/s0021-9258(18)37542-2;
RA Rao R., Pagan J., Senior A.E.;
RT "Directed mutagenesis of the strongly conserved lysine 175 in the proposed
RT nucleotide-binding domain of alpha-subunit from Escherichia coli F1-
RT ATPase.";
RL J. Biol. Chem. 263:15957-15963(1988).
RN [13]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [14]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=BL21-DE3;
RX PubMed=16079137; DOI=10.1074/jbc.m506479200;
RA Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L.,
RA von Heijne G., Daley D.O.;
RT "Protein complexes of the Escherichia coli cell envelope.";
RL J. Biol. Chem. 280:34409-34419(2005).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (4.4 ANGSTROMS) OF AN ALPHA(3)/BETA (3)/GAMMA/EPSILON
RP COMPLEX.
RX PubMed=10570135; DOI=10.1073/pnas.96.24.13697;
RA Hausrath A.C., Grueber G., Matthews B.W., Capaldi R.A.;
RT "Structural features of the gamma subunit of the Escherichia coli F(1)
RT ATPase revealed by a 4.4-A resolution map obtained by X-ray
RT crystallography.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:13697-13702(1999).
CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC across the membrane. The alpha chain is a regulatory subunit.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate;
CC Xref=Rhea:RHEA:57720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.2;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01346};
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC - and CF(0) - the membrane proton channel. CF(1) has five subunits:
CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main
CC subunits: a(1), b(2) and c(9-12). The alpha and beta chains form an
CC alternating ring which encloses part of the gamma chain. CF(1) is
CC attached to CF(0) by a central stalk formed by the gamma and epsilon
CC chains, while a peripheral stalk is formed by the delta and b chains.
CC {ECO:0000255|HAMAP-Rule:MF_01346}.
CC -!- INTERACTION:
CC P0ABB0; P0A6E6: atpC; NbExp=3; IntAct=EBI-368707, EBI-544362;
CC P0ABB0; P0ABB4: atpD; NbExp=13; IntAct=EBI-368707, EBI-368783;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01346, ECO:0000269|PubMed:16079137}; Peripheral membrane
CC protein {ECO:0000255|HAMAP-Rule:MF_01346, ECO:0000269|PubMed:16079137}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000255|HAMAP-Rule:MF_01346}.
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DR EMBL; X01631; CAA25780.1; ALT_SEQ; Genomic_DNA.
DR EMBL; J01594; AAA24735.1; ALT_SEQ; Genomic_DNA.
DR EMBL; V00265; CAA23519.1; ALT_SEQ; Genomic_DNA.
DR EMBL; V00312; CAA23596.1; ALT_SEQ; Genomic_DNA.
DR EMBL; M12212; AAA20045.1; -; Unassigned_DNA.
DR EMBL; M25464; AAA83873.1; -; Genomic_DNA.
DR EMBL; L10328; AAA62086.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76757.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77554.1; -; Genomic_DNA.
DR EMBL; V00266; CAA23525.1; -; Genomic_DNA.
DR PIR; G65176; PWECA.
DR RefSeq; NP_418190.1; NC_000913.3.
DR RefSeq; WP_001176745.1; NZ_STEB01000015.1.
DR PDB; 1D8S; X-ray; 4.40 A; A/B/C=1-513.
DR PDB; 3OAA; X-ray; 3.26 A; A/B/C/I/J/K/Q/R/S/Y/Z/a=1-513.
DR PDB; 5T4O; EM; 6.90 A; A/B/C=1-513.
DR PDB; 5T4P; EM; 7.77 A; A/B/C=1-513.
DR PDB; 5T4Q; EM; 8.53 A; A/B/C=1-513.
DR PDB; 6OQR; EM; 3.10 A; A/B/C=1-513.
DR PDB; 6OQS; EM; 3.30 A; A/B/C=1-513.
DR PDB; 6OQT; EM; 3.10 A; A/B/C=1-513.
DR PDB; 6OQU; EM; 3.20 A; A/B/C=1-513.
DR PDB; 6OQV; EM; 3.30 A; A/B/C=1-513.
DR PDB; 6OQW; EM; 3.10 A; A/B/C=1-513.
DR PDB; 6PQV; EM; 3.30 A; A/B/C=1-513.
DR PDB; 6WNQ; EM; 3.40 A; A/B/C=1-513.
DR PDB; 6WNR; EM; 3.30 A; A/B/C=1-513.
DR PDBsum; 1D8S; -.
DR PDBsum; 3OAA; -.
DR PDBsum; 5T4O; -.
DR PDBsum; 5T4P; -.
DR PDBsum; 5T4Q; -.
DR PDBsum; 6OQR; -.
DR PDBsum; 6OQS; -.
DR PDBsum; 6OQT; -.
DR PDBsum; 6OQU; -.
DR PDBsum; 6OQV; -.
DR PDBsum; 6OQW; -.
DR PDBsum; 6PQV; -.
DR PDBsum; 6WNQ; -.
DR PDBsum; 6WNR; -.
DR AlphaFoldDB; P0ABB0; -.
DR EMDB; EMD-20167; -.
DR EMDB; EMD-20168; -.
DR EMDB; EMD-20169; -.
DR EMDB; EMD-20170; -.
DR EMDB; EMD-20171; -.
DR EMDB; EMD-20172; -.
DR EMDB; EMD-20454; -.
DR EMDB; EMD-21854; -.
DR EMDB; EMD-21855; -.
DR EMDB; EMD-8357; -.
DR EMDB; EMD-8358; -.
DR EMDB; EMD-8359; -.
DR SMR; P0ABB0; -.
DR BioGRID; 852544; 9.
DR ComplexPortal; CPX-4022; ATP synthase complex.
DR DIP; DIP-31845N; -.
DR IntAct; P0ABB0; 29.
DR MINT; P0ABB0; -.
DR STRING; 511145.b3734; -.
DR TCDB; 3.A.2.1.1; the h+- or na+-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR SWISS-2DPAGE; P0ABB0; -.
DR jPOST; P0ABB0; -.
DR PaxDb; 511145-b3734; -.
DR EnsemblBacteria; AAC76757; AAC76757; b3734.
DR GeneID; 83578726; -.
DR GeneID; 948242; -.
DR KEGG; ecj:JW3712; -.
DR KEGG; eco:b3734; -.
DR PATRIC; fig|1411691.4.peg.2966; -.
DR EchoBASE; EB0096; -.
DR eggNOG; COG0056; Bacteria.
DR HOGENOM; CLU_010091_2_1_6; -.
DR InParanoid; P0ABB0; -.
DR OMA; INQRDNW; -.
DR OrthoDB; 9803053at2; -.
DR PhylomeDB; P0ABB0; -.
DR BioCyc; EcoCyc:ATPA-MONOMER; -.
DR BioCyc; MetaCyc:ATPA-MONOMER; -.
DR BRENDA; 7.1.2.2; 2026.
DR EvolutionaryTrace; P0ABB0; -.
DR PRO; PR:P0ABB0; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; NAS:ComplexPortal.
DR GO; GO:0045259; C:proton-transporting ATP synthase complex; IPI:ComplexPortal.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IMP:EcoliWiki.
DR GO; GO:0043531; F:ADP binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:UniProtKB-EC.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IMP:EcoliWiki.
DR GO; GO:0042777; P:proton motive force-driven plasma membrane ATP synthesis; IMP:ComplexPortal.
DR CDD; cd18113; ATP-synt_F1_alpha_C; 1.
DR CDD; cd18116; ATP-synt_F1_alpha_N; 1.
DR CDD; cd01132; F1-ATPase_alpha_CD; 1.
DR Gene3D; 2.40.30.20; -; 1.
DR Gene3D; 1.20.150.20; ATP synthase alpha/beta chain, C-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_01346; ATP_synth_alpha_bact; 1.
DR InterPro; IPR023366; ATP_synth_asu-like_sf.
DR InterPro; IPR000793; ATP_synth_asu_C.
DR InterPro; IPR038376; ATP_synth_asu_C_sf.
DR InterPro; IPR033732; ATP_synth_F1_a_nt-bd_dom.
DR InterPro; IPR005294; ATP_synth_F1_asu.
DR InterPro; IPR020003; ATPase_a/bsu_AS.
DR InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR InterPro; IPR036121; ATPase_F1/V1/A1_a/bsu_N_sf.
DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR00962; atpA; 1.
DR PANTHER; PTHR48082; ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR PANTHER; PTHR48082:SF2; ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF00306; ATP-synt_ab_C; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR SUPFAM; SSF47917; C-terminal domain of alpha and beta subunits of F1 ATP synthase; 1.
DR SUPFAM; SSF50615; N-terminal domain of alpha and beta subunits of F1 ATP synthase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP synthesis; ATP-binding; Cell inner membrane;
KW Cell membrane; CF(1); Direct protein sequencing; Hydrogen ion transport;
KW Ion transport; Membrane; Nucleotide-binding; Reference proteome;
KW Translocase; Transport.
FT CHAIN 1..513
FT /note="ATP synthase subunit alpha"
FT /id="PRO_0000144325"
FT BINDING 169..176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT SITE 373
FT /note="Required for activity"
FT MUTAGEN 175
FT /note="K->E: Reduced activity and reduced ATP-binding."
FT /evidence="ECO:0000269|PubMed:2903146"
FT MUTAGEN 175
FT /note="K->I: Reduced activity and loss of ATP-binding."
FT /evidence="ECO:0000269|PubMed:2903146"
FT CONFLICT 91
FT /note="T -> I (in Ref. 4; AAA83873)"
FT /evidence="ECO:0000305"
FT CONFLICT 239..244
FT /note="PYAGCA -> RMPVAL (in Ref. 4; CAA25780/AAA24735)"
FT /evidence="ECO:0000305"
FT CONFLICT 300..302
FT /note="RAA -> MLQ (in Ref. 2; CAA23519)"
FT /evidence="ECO:0000305"
FT HELIX 9..17
FT /evidence="ECO:0007829|PDB:6OQR"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:6OQW"
FT STRAND 28..35
FT /evidence="ECO:0007829|PDB:6OQR"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:6OQR"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:6OQR"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:6OQR"
FT STRAND 59..67
FT /evidence="ECO:0007829|PDB:6OQR"
FT STRAND 70..77
FT /evidence="ECO:0007829|PDB:6OQR"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:6OQR"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:6OQR"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:6OQR"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:6OQR"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:6OQR"
FT STRAND 126..130
FT /evidence="ECO:0007829|PDB:6OQR"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:6OQR"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:6OQW"
FT HELIX 151..156
FT /evidence="ECO:0007829|PDB:6OQR"
FT STRAND 164..169
FT /evidence="ECO:0007829|PDB:6OQR"
FT STRAND 171..174
FT /evidence="ECO:0007829|PDB:6OQR"
FT HELIX 175..184
FT /evidence="ECO:0007829|PDB:6OQR"
FT TURN 185..189
FT /evidence="ECO:0007829|PDB:6OQR"
FT STRAND 190..199
FT /evidence="ECO:0007829|PDB:6OQR"
FT HELIX 202..214
FT /evidence="ECO:0007829|PDB:6OQR"
FT TURN 215..217
FT /evidence="ECO:0007829|PDB:6OQR"
FT HELIX 218..220
FT /evidence="ECO:0007829|PDB:6OQR"
FT STRAND 221..226
FT /evidence="ECO:0007829|PDB:6OQR"
FT HELIX 232..250
FT /evidence="ECO:0007829|PDB:6OQR"
FT TURN 251..253
FT /evidence="ECO:0007829|PDB:6OQR"
FT STRAND 255..261
FT /evidence="ECO:0007829|PDB:6OQR"
FT HELIX 263..276
FT /evidence="ECO:0007829|PDB:6OQR"
FT HELIX 283..285
FT /evidence="ECO:0007829|PDB:6OQR"
FT HELIX 290..298
FT /evidence="ECO:0007829|PDB:6OQR"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:3OAA"
FT HELIX 306..312
FT /evidence="ECO:0007829|PDB:6OQR"
FT TURN 313..315
FT /evidence="ECO:0007829|PDB:6OQR"
FT STRAND 322..326
FT /evidence="ECO:0007829|PDB:6OQR"
FT STRAND 329..331
FT /evidence="ECO:0007829|PDB:6OQR"
FT HELIX 333..335
FT /evidence="ECO:0007829|PDB:6OQR"
FT HELIX 340..348
FT /evidence="ECO:0007829|PDB:6OQR"
FT STRAND 349..355
FT /evidence="ECO:0007829|PDB:6OQR"
FT HELIX 357..361
FT /evidence="ECO:0007829|PDB:6OQR"
FT TURN 370..372
FT /evidence="ECO:0007829|PDB:6OQR"
FT STRAND 374..377
FT /evidence="ECO:0007829|PDB:6OQR"
FT HELIX 378..381
FT /evidence="ECO:0007829|PDB:6OQR"
FT HELIX 384..403
FT /evidence="ECO:0007829|PDB:6OQR"
FT HELIX 404..412
FT /evidence="ECO:0007829|PDB:6OQR"
FT HELIX 415..430
FT /evidence="ECO:0007829|PDB:6OQR"
FT HELIX 441..452
FT /evidence="ECO:0007829|PDB:6OQR"
FT HELIX 455..457
FT /evidence="ECO:0007829|PDB:6OQR"
FT HELIX 461..463
FT /evidence="ECO:0007829|PDB:6OQR"
FT HELIX 464..478
FT /evidence="ECO:0007829|PDB:6OQR"
FT HELIX 480..489
FT /evidence="ECO:0007829|PDB:6OQR"
FT HELIX 494..510
FT /evidence="ECO:0007829|PDB:6OQR"
SQ SEQUENCE 513 AA; 55222 MW; DD1F3859375E9103 CRC64;
MQLNSTEISE LIKQRIAQFN VVSEAHNEGT IVSVSDGVIR IHGLADCMQG EMISLPGNRY
AIALNLERDS VGAVVMGPYA DLAEGMKVKC TGRILEVPVG RGLLGRVVNT LGAPIDGKGP
LDHDGFSAVE AIAPGVIERQ SVDQPVQTGY KAVDSMIPIG RGQRELIIGD RQTGKTALAI
DAIINQRDSG IKCIYVAIGQ KASTISNVVR KLEEHGALAN TIVVVATASE SAALQYLAPY
AGCAMGEYFR DRGEDALIIY DDLSKQAVAY RQISLLLRRP PGREAFPGDV FYLHSRLLER
AARVNAEYVE AFTKGEVKGK TGSLTALPII ETQAGDVSAF VPTNVISITD GQIFLETNLF
NAGIRPAVNP GISVSRVGGA AQTKIMKKLS GGIRTALAQY RELAAFSQFA SDLDDATRKQ
LDHGQKVTEL LKQKQYAPMS VAQQSLVLFA AERGYLADVE LSKIGSFEAA LLAYVDRDHA
PLMQEINQTG GYNDEIEGKL KGILDSFKAT QSW
//
