SRFAA_BACSU
ID SRFAA_BACSU Reviewed; 3587 AA.
AC P27206;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 4.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Surfactin synthase subunit 1;
GN Name=srfAA; Synonyms=srfA, srfA1; OrderedLocusNames=BSU03480;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8441623; DOI=10.1093/nar/21.1.93;
RA Fuma S., Fujishima Y., Corbell N., D'Souza C., Nakano M.M., Zuber P.,
RA Yamane K.;
RT "Nucleotide sequence of 5' portion of srfA that contains the region
RT required for competence establishment in Bacillus subtilis.";
RL Nucleic Acids Res. 21:93-97(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / JH642;
RX PubMed=8355609; DOI=10.1111/j.1365-2958.1993.tb01629.x;
RA Cosmina P., Rodriguez F., de Ferra F., Grandi G., Perego M., Venema G.,
RA van Sinderen D.;
RT "Sequence and analysis of the genetic locus responsible for surfactin
RT synthesis in Bacillus subtilis.";
RL Mol. Microbiol. 8:821-831(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8969502; DOI=10.1099/13500872-142-11-3047;
RA Yamane K., Kumano M., Kurita K.;
RT "The 25 degrees-36 degrees region of the Bacillus subtilis chromosome:
RT determination of the sequence of a 146 kb segment and identification of 113
RT genes.";
RL Microbiology 142:3047-3056(1996).
RN [4]
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 [5]
RP SEQUENCE REVISION.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-460.
RX PubMed=1847909; DOI=10.1128/jb.173.5.1770-1778.1991;
RA Nakano M.M., Magnuson R., Myers A.M., Curry J., Grossman A.D., Zuber P.;
RT "srfA is an operon required for surfactin production, competence
RT development, and efficient sporulation in Bacillus subtilis.";
RL J. Bacteriol. 173:1770-1778(1991).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-64.
RC STRAIN=168;
RX PubMed=7704255; DOI=10.1099/13500872-141-2-277;
RA Fujishima Y., Yamane K.;
RT "A 10 kb nucleotide sequence at the 5' flanking region (32 degrees) of
RT srfAA of the Bacillus subtilis chromosome.";
RL Microbiology 141:277-279(1995).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-38.
RX PubMed=1715856; DOI=10.1128/jb.173.17.5487-5493.1991;
RA Nakano M.M., Xia L., Zuber P.;
RT "Transcription initiation region of the srfA operon, which is controlled by
RT the comP-comA signal transduction system in Bacillus subtilis.";
RL J. Bacteriol. 173:5487-5493(1991).
RN [9]
RP PHOSPHOPANTETHEINYLATION [LARGE SCALE ANALYSIS] AT SER-1006, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=168;
RX PubMed=17218307; DOI=10.1074/mcp.m600464-mcp200;
RA Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R.,
RA Mann M.;
RT "The serine/threonine/tyrosine phosphoproteome of the model bacterium
RT Bacillus subtilis.";
RL Mol. Cell. Proteomics 6:697-707(2007).
CC -!- FUNCTION: This protein is a multifunctional enzyme able to activate and
CC polymerize the amino acids Leu, Glu, Asp and Val. Activation sites for
CC these AA consist of individual domains.
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Note=Binds 3 phosphopantetheines covalently.;
CC -!- PATHWAY: Antibiotic biosynthesis; surfactin biosynthesis.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
CC -!- CAUTION: The phosphoserine observed at Ser-1006 in PubMed:17218307
CC undoubtedly results from the secondary neutral loss of pantetheine from
CC the phosphodiester linked cofactor. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA08982.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA49816.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D13262; BAA02522.1; -; Genomic_DNA.
DR EMBL; X70356; CAA49816.1; ALT_FRAME; Genomic_DNA.
DR EMBL; D50453; BAA08982.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AL009126; CAB12142.2; -; Genomic_DNA.
DR EMBL; M59939; AAA22815.1; -; Genomic_DNA.
DR EMBL; D30762; BAA21034.1; -; Genomic_DNA.
DR EMBL; M64702; AAA22816.1; -; Genomic_DNA.
DR PIR; I40485; I40485.
DR RefSeq; NP_388230.2; NC_000964.3.
DR RefSeq; WP_010886402.1; NZ_CP053102.1.
DR SMR; P27206; -.
DR IntAct; P27206; 4.
DR MINT; P27206; -.
DR STRING; 224308.BSU03480; -.
DR jPOST; P27206; -.
DR PaxDb; P27206; -.
DR PRIDE; P27206; -.
DR EnsemblBacteria; CAB12142; CAB12142; BSU_03480.
DR GeneID; 938306; -.
DR KEGG; bsu:BSU03480; -.
DR PATRIC; fig|224308.179.peg.366; -.
DR eggNOG; COG1020; Bacteria.
DR InParanoid; P27206; -.
DR OMA; NRQHWNQ; -.
DR PhylomeDB; P27206; -.
DR BioCyc; BSUB:BSU03480-MON; -.
DR UniPathway; UPA00181; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0043604; P:amide biosynthetic process; IEA:UniProt.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1200.10; -; 2.
DR Gene3D; 3.30.300.30; -; 3.
DR Gene3D; 3.30.559.10; -; 4.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR036736; ACP-like_sf.
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; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR010060; NRPS_synth.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR Pfam; PF00501; AMP-binding; 3.
DR Pfam; PF13193; AMP-binding_C; 3.
DR Pfam; PF00668; Condensation; 4.
DR Pfam; PF00550; PP-binding; 3.
DR SMART; SM00823; PKS_PP; 3.
DR SUPFAM; SSF47336; SSF47336; 3.
DR TIGRFAMs; TIGR01733; AA-adenyl-dom; 3.
DR TIGRFAMs; TIGR01720; NRPS-para261; 1.
DR PROSITE; PS00455; AMP_BINDING; 3.
DR PROSITE; PS50075; CARRIER; 3.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 3.
PE 1: Evidence at protein level;
KW Antibiotic biosynthesis; Ligase; Multifunctional enzyme;
KW Phosphopantetheine; Phosphoprotein; Reference proteome; Repeat;
KW Sporulation.
FT CHAIN 1..3587
FT /note="Surfactin synthase subunit 1"
FT /id="PRO_0000193099"
FT DOMAIN 971..1046
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 2010..2085
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 3038..3112
FT /note="Carrier 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION ?..1047
FT /note="Domain 1 (glutamate-activating)"
FT REGION ?..2086
FT /note="Domain 2 (leucine-activating)"
FT REGION ?..3114
FT /note="Domain 3 (D-leucine-activating)"
FT MOD_RES 1006
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000269|PubMed:17218307"
FT MOD_RES 2045
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 3073
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT CONFLICT 146
FT /note="I -> M (in Ref. 2; CAA49816 and 3; BAA08982)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="L -> V (in Ref. 2; CAA49816 and 3; BAA08982)"
FT /evidence="ECO:0000305"
FT CONFLICT 165
FT /note="G -> A (in Ref. 1; BAA02522)"
FT /evidence="ECO:0000305"
FT CONFLICT 281
FT /note="T -> Q (in Ref. 2; CAA49816 and 3; BAA08982)"
FT /evidence="ECO:0000305"
FT CONFLICT 460
FT /note="D -> T (in Ref. 6; AAA22815)"
FT /evidence="ECO:0000305"
FT CONFLICT 540
FT /note="P -> A (in Ref. 2; CAA49816 and 3; BAA08982)"
FT /evidence="ECO:0000305"
FT CONFLICT 562
FT /note="I -> Y (in Ref. 2; CAA49816 and 3; BAA08982)"
FT /evidence="ECO:0000305"
FT CONFLICT 639..640
FT /note="GS -> PT (in Ref. 2; CAA49816 and 3; BAA08982)"
FT /evidence="ECO:0000305"
FT CONFLICT 644
FT /note="R -> P (in Ref. 2; CAA49816 and 3; BAA08982)"
FT /evidence="ECO:0000305"
FT CONFLICT 647..649
FT /note="LLA -> FLP (in Ref. 2; CAA49816 and 3; BAA08982)"
FT /evidence="ECO:0000305"
FT CONFLICT 1026
FT /note="L -> Q (in Ref. 2; CAA49816 and 3; BAA08982)"
FT /evidence="ECO:0000305"
FT CONFLICT 1132..1133
FT /note="DS -> VC (in Ref. 2; CAA49816 and 3; BAA08982)"
FT /evidence="ECO:0000305"
FT CONFLICT 1164
FT /note="A -> R (in Ref. 1; BAA02522)"
FT /evidence="ECO:0000305"
FT CONFLICT 1458
FT /note="L -> V (in Ref. 1; BAA02522)"
FT /evidence="ECO:0000305"
FT CONFLICT 1850
FT /note="S -> T (in Ref. 2; CAA49816 and 3; BAA08982)"
FT /evidence="ECO:0000305"
FT CONFLICT 1894
FT /note="D -> T (in Ref. 2; CAA49816 and 3; BAA08982)"
FT /evidence="ECO:0000305"
FT CONFLICT 1911
FT /note="R -> A (in Ref. 2; CAA49816 and 3; BAA08982)"
FT /evidence="ECO:0000305"
FT CONFLICT 1973..1980
FT /note="PAVFIQMD -> LRCLSKWT (in Ref. 1; BAA02522)"
FT /evidence="ECO:0000305"
FT CONFLICT 2052
FT /note="L -> P (in Ref. 2; CAA49816 and 3; BAA08982)"
FT /evidence="ECO:0000305"
FT CONFLICT 2218
FT /note="H -> Q (in Ref. 2; CAA49816 and 3; BAA08982)"
FT /evidence="ECO:0000305"
FT CONFLICT 2265..2266
FT /note="QQ -> HR (in Ref. 2; CAA49816 and 3; BAA08982)"
FT /evidence="ECO:0000305"
FT CONFLICT 2291
FT /note="L -> V (in Ref. 1; BAA02522)"
FT /evidence="ECO:0000305"
FT CONFLICT 2349
FT /note="S -> C (in Ref. 2; CAA49816 and 3; BAA08982)"
FT /evidence="ECO:0000305"
FT CONFLICT 2428
FT /note="R -> S (in Ref. 2; CAA49816 and 3; BAA08982)"
FT /evidence="ECO:0000305"
FT CONFLICT 2611..2612
FT /note="AV -> RC (in Ref. 1; BAA02522)"
FT /evidence="ECO:0000305"
FT CONFLICT 2685
FT /note="E -> ENPE (in Ref. 2; CAA49816 and 3; BAA08982)"
FT /evidence="ECO:0000305"
FT CONFLICT 2755
FT /note="T -> S (in Ref. 2; CAA49816 and 3; BAA08982)"
FT /evidence="ECO:0000305"
FT CONFLICT 2896..2897
FT /note="TA -> SP (in Ref. 1; BAA02522)"
FT /evidence="ECO:0000305"
FT CONFLICT 3025
FT /note="P -> N (in Ref. 2; CAA49816 and 3; BAA08982)"
FT /evidence="ECO:0000305"
FT CONFLICT 3096
FT /note="F -> N (in Ref. 2; CAA49816 and 3; BAA08982)"
FT /evidence="ECO:0000305"
FT CONFLICT 3271
FT /note="A -> S (in Ref. 2; CAA49816 and 3; BAA08982)"
FT /evidence="ECO:0000305"
FT CONFLICT 3316
FT /note="R -> S (in Ref. 2; CAA49816 and 3; BAA08982)"
FT /evidence="ECO:0000305"
FT CONFLICT 3451
FT /note="Y -> S (in Ref. 2; CAA49816 and 3; BAA08982)"
FT /evidence="ECO:0000305"
FT CONFLICT 3483..3495
FT /note="DEMSDAGLFTRSE -> HQMSHPPFFTTSH (in Ref. 2; CAA49816
FT and 3; BAA08982)"
FT /evidence="ECO:0000305"
FT CONFLICT 3499..3500
FT /note="GQ -> PH (in Ref. 2; CAA49816 and 3; BAA08982)"
FT /evidence="ECO:0000305"
FT CONFLICT 3507
FT /note="E -> R (in Ref. 1; BAA02522)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3587 AA; 402146 MW; 5CA8D98D71FD0A84 CRC64;
MEITFYPLTD AQKRIWYTEK FYPHTSISNL AGIGKLVSAD AIDYVLVEQA IQEFIRRNDA
MRLRLRLDEN GEPVQYISEY RPVDIKHTDT TEDPNAIEFI SQWSREETKK PLPLYDCDLF
RFSLFTIKEN EVWFYANVHH VISDGISMNI LGNAIMHIYL ELASGSETKE GISHSFIDHV
LSEQEYAQSK RFEKDKAFWN KQFESVPELV SLKRNASAGG SLDAERFSKD VPEALHQQIL
SFCEANKVSV LSVFQSLLAA YLYRVSGQND VVTGTFMGNR TNAKEKQMLG MFVSTVPLRT
NIDGGQAFSE FVKDRMKDLM KTLRHQKYPY NLLINDLRET KSSLTKLFTV SLEYQVMQWQ
KEEDLAFLTE PIFSGSGLND VSIHVKDRWD TGKLTIDFDY RTDLFSREEI NMICERMITM
LENALTHPEH TIDELTLISD AEKEKLLARA GGKSVSYRKD MTIPELFQEK AELLSDHPAV
VFEDRTLSYR TLHEQSARIA NVLKQKGVGP DSPVAVLIER SERMITAIMG ILKAGGAYVP
IDPGFPAERI QYILEDCGAD FILTESKVAA PEADAELIDL DQAIEEGAEE SLNADVNARN
LAYIIYTSGT TGRPKGVMIE HRQVHHLVES LQQTIYQSGS QTLRMALLAP FHFDASVKQI
FASLLLGQTL YIVPKKTVTN GAALTAYYRK NSIEATDGTP AHLQMLAAAG DFEGLKLKHM
LIGGEGLSSV VADKLLKLFK EAGTAPRLTN VYGPTETCVD ASVHPVIPEN AVQSAYVPIG
KALGNNRLYI LDQKGRLQPE GVAGELYIAG DGVGRGYLHL PELTEEKFLQ DPFVPGDRMY
RTGDVVRWLP DGTIEYLGRE DDQVKVRGYR IELGEIEAVI QQAPDVAKAV VLARPDEQGN
LEVCAYVVQK PGSEFAPAGL REHAARQLPD YMVPAYFTEV TEIPLTPSGK VDRRKLFALE
VKAVSGTAYT APRNETEKAI AAIWQDVLNV EKAGIFDNFF ETGGHSLKAM TLLTKIHKET
GIEIPLQFLF EHPTITALAE EADHRESKAF AVIEPAEKQE HYPLSLAQQR TYIVSQFEDA
GVGYNMPAAA ILEGPLDIQK LERAFQGLIR RHESLRTSFV LENSTPRQKI HDSVDFNIEM
IERGGRSDEA IMASFVRTFD LAKAPLFRIG LLGLEENRHM LLFDMHHLIS DGVSIGIMLE
ELARIYKGEQ LPDLRLQYKD YAVWQSRQAA EGYKKDQAYW KEVFAGELPV LQLLSDYPRP
PVQSFEGDRV SIKLDAGVKD RLNRLAEQNG ATLYMVMLSA YYTLLSKYTG QDDIIVGTPS
AGRNHSDTEG IIGMFVNTLA IRSEVKQNET FTQLISRVRK RVLDAFSHQD YPFEWLVEDL
NIPRDVSRHP LFDTMFSLQN ATEGIPAVGD LSLSVQETNF KIAKFDLTVQ ARETDEGIEI
DVDYSTKLFK QSTADRLLTH FARLLEDAAA DPEKPISEYK LLSEEEAASQ IQQFNPGRTP
YPKDKTIVQL FEEQAANTPD HTALQYEGES LTYRELNERA NRLARGILSL GAGEGRTAAV
LCERSMDMIV SILAVLKSGS AYVPIDPEHP IQRMQHFFRD SGAKVLLTQR KLKALAEEAE
FKGVIVLADE EESYHADARN LALPLDSAAM ANLTYTSGTT GTPKGNIVTH ANILRTVKET
NYLSITEQDT ILGLSNYVFD AFMFDMFGSL LNGAKLVLIP KETVLDMARL SRVIERENIS
ILMITTALFH LLVDLNPACL STLRKIMFGG ERASVEHVRK ALQTVGKGKL LHMYGPSEST
VFATYHPVDE LEEHTLSVPI GKPVSNTEVY ILDRTGHVQP AGIAGELCVS GEGLVKGYYN
RPELTEEKFV PHPFTSGERM YKTGDLARWL PNGDIEFIGR IDHQVKIRGQ RIELGEIEHQ
LQTHDRVQES VVLAVDQGAG DKLLCAYYVG EGDISSQEMR EHAAKDLPAY MVPAVFIQMD
ELPLTGNGKI DRRALPIPDA NVSRGVSYVA PRNGTEQKVA DIWAQVLQAE QVGAYDHFFD
IGGHSLAGMK MLALVHQELG VELSLKDLFQ SPTVEGLAQV IASAEKGTAA SISPAEKQDT
YPVSSPQKRM YVLQQLEDAQ TSYNMPAVLR LTGELDVERL NSVMQQLMQR HEALRTTFEI
KDGETVQRIW EEAECEIAYF EAPEEETERI VSEFIKPFKI DQLPLFRIGL IKHSDTEHVL
LFDMHHIISD GASVGVLIEE LSKLYDGETL EPLRIQYKDY AVWQQQFIQS ELYKKQEEHW
LKELDGELPV LTLPTDYSRP AVQTFEGDRI AFSLEAGKAD ALRRLAKETD STLYMVLLAS
YSAFLSKISG QDDIIVGSPV AGRSQADVSR VIGMFVNTLA LRTYPKGEKT FADYLNEVKE
TALSAFDAQD YPLEDLIGNV QVQRDTSRNP LFDAVFSMQN ANIKDLTMKG IQLEPHPFER
KTAKFDLTLT ADETDGGLTF VLEYNTALFK QETIERWKQY WMELLDAVTG NPNQPLSSLS
LVTETEKQAL LEAWKGKALP VPTDKTVHQL FEETAQRHKD RPAVTYNGQS WTYGELNAKA
NRLARILMDC GISPDDRVGV LTKPSLEMSA AVLGVLKAGA AFVPIDPDYP DQRIEYILQD
SGAKLLLKQE GISVPDSYTG DVILLDGSRT ILSLPLDEND EENPETAVTA ENLAYMIYTS
GTTGQPKGVM VEHHALVNLC FWHHDAFSMT AEDRSAKYAG FGFDASIWEM FPTWTIGAEL
HVIEEAIRLD IVRLNDYFET NGVTITFLPT QLAEQFMELE NTSLRVLLTG GDKLKRAVKK
PYTLVNNYGP TENTVVATSA EIHPEEGSLS IGRAIANTRV YILGEGNQVQ PEGVAGELCV
AGRGLARGYL NREDETAKRF VADPFVPGER MYRTGDLVKW TGGGIEYIGR IDQQVKVRGY
RIELSEIEVQ LAQLSEVQDA AVTAVKDKGG NTAIAAYVTP ESADIEALKS ALKETLPDYM
IPAFWVTLNE LPVTANGKVD RKALPEPDIE AGSGEYKAPT TDMEELLAGI WQDVLGMSEV
GVTDNFFSLG GDSIKGIQMA SRLNQHGWKL EMKDLFQHPT IEELTQYVER AEGKQADQGP
VEGEVILTPI QRWFFEKNFT NKHHWNQSVM LHAKKGFDPE RVEKTLQALI EHHDALRMVY
REGQEDVIQY NRGLEAASAQ LEVIQIEGQA ADYEDRIERE AERLQSSIDL QEGGLLKAGL
FQAEDGDHLL LAIHHLVVDG VSWRILLEDF AAVYTQLEQG NEPVLPQKTH SFAEYAERLQ
DFANSKAFLK EKEYWRQLEE QAVAAKLPKD RESGDQRMKH TKTIEFSLTA EETEQLTTKV
HEAYHTEMND ILLTAFGLAM KEWTGQDRVS VHLEGHGREE IIEDLTISRT VGWFTSMYPM
VLDMKHADDL GYQLKQMKED IRHVPNKGVG YGILRYLTAP EHKEDVAFSI QPDVSFNYLG
QFDEMSDAGL FTRSELPSGQ SLSPETEKPN ALDVVGYIEN GKLTMSLAYH SLEFHEKTVQ
TFSDSFKAHL LRIIEHCLSQ DGTELTPSDL GDDDLTLDEL DKLMEIF
