SP4A_BACSU
ID SP4A_BACSU Reviewed; 492 AA.
AC P35149;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Stage IV sporulation protein A;
DE EC=3.6.1.-;
DE AltName: Full=Coat morphogenetic protein SpoIVA;
GN Name=spoIVA; Synonyms=spoVP; OrderedLocusNames=BSU22800;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DEVELOPMENTAL STAGE, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=168 / PY79;
RX PubMed=1729246; DOI=10.1128/jb.174.2.575-585.1992;
RA Roels S., Driks A., Losick R.;
RT "Characterization of spoIVA, a sporulation gene involved in coat
RT morphogenesis in Bacillus subtilis.";
RL J. Bacteriol. 174:575-585(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=1729247; DOI=10.1128/jb.174.2.586-594.1992;
RA Stevens C.M., Daniel R., Illing N., Errington J.;
RT "Characterization of a sporulation gene, spoIVA, involved in spore coat
RT morphogenesis in Bacillus subtilis.";
RL J. Bacteriol. 174:586-594(1992).
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 PROTEIN SEQUENCE OF 1-12, AND AMOUNT IN YABG MUTANT SPORES.
RC STRAIN=168;
RX PubMed=10714992; DOI=10.1128/jb.182.7.1883-1888.2000;
RA Takamatsu H., Kodama T., Imamura A., Asai K., Kobayashi K., Nakayama T.,
RA Ogasawara N., Watabe K.;
RT "The Bacillus subtilis yabG gene is transcribed by SigK RNA polymerase
RT during sporulation, and yabG mutant spores have altered coat protein
RT composition.";
RL J. Bacteriol. 182:1883-1888(2000).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=168 / PY79;
RX PubMed=8299942; DOI=10.1101/gad.8.2.234;
RA Driks A., Roels S., Beall B., Moran C.P. Jr., Losick R.;
RT "Subcellular localization of proteins involved in the assembly of the spore
RT coat of Bacillus subtilis.";
RL Genes Dev. 8:234-244(1994).
RN [6]
RP SUBCELLULAR LOCATION.
RC STRAIN=SG38;
RX PubMed=8936302; DOI=10.1099/00221287-142-4-733;
RA Lewis P.J., Errington J.;
RT "Use of green fluorescent protein for detection of cell-specific gene
RT expression and subcellular protein localization during sporulation in
RT Bacillus subtilis.";
RL Microbiology 142:733-740(1996).
RN [7]
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DOMAIN.
RC STRAIN=168 / PY79;
RX PubMed=9922240; DOI=10.1128/jb.181.3.781-790.1999;
RA Price K.D., Losick R.;
RT "A four-dimensional view of assembly of a morphogenetic protein during
RT sporulation in Bacillus subtilis.";
RL J. Bacteriol. 181:781-790(1999).
RN [8]
RP CLEAVAGE BY YABG.
RC STRAIN=168;
RX PubMed=11040425; DOI=10.1111/j.1574-6968.2000.tb09355.x;
RA Takamatsu H., Imamura A., Kodama T., Asai K., Ogasawara N., Watabe K.;
RT "The yabG gene of Bacillus subtilis encodes a sporulation specific protease
RT which is involved in the processing of several spore coat proteins.";
RL FEMS Microbiol. Lett. 192:33-38(2000).
RN [9]
RP MUTAGENESIS OF LEU-59; MET-69; CYS-98; ILE-210; ARG-230; VAL-241; HIS-256;
RP VAL-283; ILE-367; ILE-383; LEU-393; ILE-400; GLY-416; GLU-418; VAL-453 AND
RP ILE-457, AND DISRUPTION PHENOTYPE.
RC STRAIN=168 / PY79;
RX PubMed=11160095; DOI=10.1128/jb.183.5.1645-1654.2001;
RA Catalano F.A., Meador-Parton J., Popham D.L., Driks A.;
RT "Amino acids in the Bacillus subtilis morphogenetic protein SpoIVA with
RT roles in spore coat and cortex formation.";
RL J. Bacteriol. 183:1645-1654(2001).
RN [10]
RP FUNCTION, INTERACTION WITH SPOVM, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP GLY-486.
RC STRAIN=168 / PY79;
RX PubMed=17427285; DOI=10.1111/j.1365-2958.2006.05468.x;
RA Ramamurthi K.S., Clapham K.R., Losick R.;
RT "Peptide anchoring spore coat assembly to the outer forespore membrane in
RT Bacillus subtilis.";
RL Mol. Microbiol. 62:1547-1557(2006).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
RP SUBCELLULAR LOCATION, ATP-BINDING, MOTIF, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF LYS-30.
RC STRAIN=168 / PY79;
RX PubMed=18691972; DOI=10.1016/j.molcel.2008.05.030;
RA Ramamurthi K.S., Losick R.;
RT "ATP-driven self-assembly of a morphogenetic protein in Bacillus
RT subtilis.";
RL Mol. Cell 31:406-414(2008).
RN [12]
RP SUBUNIT, AND INTERACTION WITH SPOVID AND SAFA.
RC STRAIN=168 / PY79;
RX PubMed=19702880; DOI=10.1111/j.1574-6968.2009.01737.x;
RA Mullerova D., Krajcikova D., Barak I.;
RT "Interactions between Bacillus subtilis early spore coat morphogenetic
RT proteins.";
RL FEMS Microbiol. Lett. 299:74-85(2009).
RN [13]
RP INTERACTION WITH SPOVID, AND SUBCELLULAR LOCATION.
RC STRAIN=168 / PY79;
RX PubMed=19775244; DOI=10.1111/j.1365-2958.2009.06886.x;
RA Wang K.H., Isidro A.L., Domingues L., Eskandarian H.A., McKenney P.T.,
RA Drew K., Grabowski P., Chua M.H., Barry S.N., Guan M., Bonneau R.,
RA Henriques A.O., Eichenberger P.;
RT "The coat morphogenetic protein SpoVID is necessary for spore encasement in
RT Bacillus subtilis.";
RL Mol. Microbiol. 74:634-649(2009).
RN [14]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
RP SUBCELLULAR LOCATION, ATP-BINDING, AND MUTAGENESIS OF THR-70; THR-71;
RP ASP-97 AND SER-189.
RC STRAIN=168 / PY79;
RX PubMed=23267091; DOI=10.1073/pnas.1210554110;
RA Castaing J.P., Nagy A., Anantharaman V., Aravind L., Ramamurthi K.S.;
RT "ATP hydrolysis by a domain related to translation factor GTPases drives
RT polymerization of a static bacterial morphogenetic protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:E151-E160(2013).
CC -!- FUNCTION: ATPase. Has a role at an early stage in the morphogenesis of
CC the spore coat outer layers. Its ATP hydrolysis is required for proper
CC assembly of the spore coat. Forms a basement layer around the outside
CC surface of the forespore and self-assembles irreversibly into higher
CC order structures by binding and hydrolyzing ATP thus creating a durable
CC and stable platform upon which thereafter morphogenesis of the coat can
CC take place. Required for proper localization of spore coat protein CotE
CC and sporulation-specific proteins including SpoVM.
CC {ECO:0000269|PubMed:1729246, ECO:0000269|PubMed:17427285,
CC ECO:0000269|PubMed:18691972, ECO:0000269|PubMed:23267091,
CC ECO:0000269|PubMed:8299942}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:18691972, ECO:0000269|PubMed:23267091};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=412 uM for ATP {ECO:0000269|PubMed:18691972,
CC ECO:0000269|PubMed:23267091};
CC Note=The turnover rate is 2.7 pmol/min/pmol of SpoIVA at Vmax
CC (PubMed:18691972). The turnover rate is 1.0 pmol/min/pmol of SpoIVA
CC at Vmax (PubMed:23267091). {ECO:0000269|PubMed:18691972,
CC ECO:0000269|PubMed:23267091};
CC -!- SUBUNIT: Polymerizes to self-assemble into static filaments. ATP
CC hydrolysis is required by every subunit for incorporation into the
CC growing polymer by inducing a conformational change that drives
CC polymerization of a nucleotide-free filament. Polymerization requires a
CC critical concentration of the protein and only occurs after it is
CC localized to the surface of the developing spore. Interacts (via
CC extreme C-terminus Gly-486) with SpoVM (via Ile-6). Interacts (via
CC full-length) with SpoVID (via C-terminus 499-575 AA). Interacts with
CC SafA. {ECO:0000269|PubMed:17427285, ECO:0000269|PubMed:18691972,
CC ECO:0000269|PubMed:19702880, ECO:0000269|PubMed:19775244,
CC ECO:0000269|PubMed:23267091}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Note=Uniformly
CC distributed on the membrane around the forespore, lying close to or on
CC its outer surface. Expression only necessary in the mother cell chamber
CC of the sporangium for the formation of a mature spore. According to
CC PubMed:8299942, not a coat protein of the mature spore, is only
CC transiently associated with the assembling coat. According to
CC PubMed:9922240, present as a component of the fully mature spore.
CC Proper localization requires the expression of a gene spoVM which is
CC under the control of the mother cell transcription factor sigma E.
CC {ECO:0000269|PubMed:1729247, ECO:0000269|PubMed:17427285,
CC ECO:0000269|PubMed:18691972, ECO:0000269|PubMed:19775244,
CC ECO:0000269|PubMed:23267091, ECO:0000269|PubMed:8299942,
CC ECO:0000269|PubMed:8936302, ECO:0000269|PubMed:9922240}.
CC -!- DEVELOPMENTAL STAGE: Expressed soon after the formation of the
CC asymmetric septum during sporulation. Expression commences about 2
CC hours after the onset of sporulation. Assembly around the developing
CC forespore commences at the time of polar division and seems to continue
CC after engulfment of the forespore is complete. Remains present
CC throughout the late stages of morphogenesis and during this
CC accumulation process preferentially collects on the mother cell side of
CC the engulfed forespore, but eventually is deposited equally all around
CC the forespore. {ECO:0000269|PubMed:1729246, ECO:0000269|PubMed:1729247,
CC ECO:0000269|PubMed:9922240}.
CC -!- DOMAIN: Extreme C-terminal region (AA 487-492) is required for its
CC proper localization into a spherical shell around the developing
CC forespore. N-terminus (AA 1-64) is functionally important although
CC largely dispensable for proper localization.
CC {ECO:0000269|PubMed:9922240}.
CC -!- PTM: Seems to be cleaved by the YabG protease.
CC {ECO:0000269|PubMed:11040425}.
CC -!- DISRUPTION PHENOTYPE: Forespores lack a well-defined cortex, and the
CC coat is present as swirls in the mother cell compartment of the
CC sporangia rather than having been deposited around the forespore
CC protoplasts. According to PubMed:18691972, unable to sporulate.
CC {ECO:0000269|PubMed:11160095, ECO:0000269|PubMed:1729246,
CC ECO:0000269|PubMed:18691972}.
CC -!- MISCELLANEOUS: Present in an increased level in yabG mutant spores.
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DR EMBL; M81169; AAA22802.1; -; Genomic_DNA.
DR EMBL; M80926; AAB59029.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14196.1; -; Genomic_DNA.
DR PIR; A41970; A41970.
DR RefSeq; NP_390161.1; NC_000964.3.
DR RefSeq; WP_003230572.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P35149; -.
DR STRING; 224308.BSU22800; -.
DR PaxDb; P35149; -.
DR PRIDE; P35149; -.
DR EnsemblBacteria; CAB14196; CAB14196; BSU_22800.
DR GeneID; 938991; -.
DR KEGG; bsu:BSU22800; -.
DR PATRIC; fig|224308.179.peg.2485; -.
DR eggNOG; COG0699; Bacteria.
DR OMA; RMPENAQ; -.
DR PhylomeDB; P35149; -.
DR BioCyc; BSUB:BSU22800-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043595; C:endospore cortex; IMP:UniProtKB.
DR GO; GO:0042601; C:endospore-forming forespore; IDA:UniProtKB.
DR GO; GO:0031160; C:spore wall; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:UniProtKB.
DR GO; GO:0000270; P:peptidoglycan metabolic process; IMP:UniProtKB.
DR GO; GO:0051259; P:protein complex oligomerization; IDA:UniProtKB.
DR GO; GO:0051258; P:protein polymerization; IDA:UniProtKB.
DR GO; GO:0009847; P:spore germination; IMP:UniProtKB.
DR GO; GO:0042244; P:spore wall assembly; IDA:UniProtKB.
DR GO; GO:0070590; P:spore wall biogenesis; IDA:UniProtKB.
DR GO; GO:0043934; P:sporulation; IDA:UniProtKB.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IDA:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014201; Spore_IV_A.
DR Pfam; PF09547; Spore_IV_A; 1.
DR PIRSF; PIRSF007466; SpoIVA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR02836; spore_IV_A; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Direct protein sequencing; Hydrolase;
KW Nucleotide-binding; Reference proteome; Sporulation.
FT CHAIN 1..492
FT /note="Stage IV sporulation protein A"
FT /id="PRO_0000072073"
FT MOTIF 24..31
FT /note="Walker A motif; involved in ATP-binding and
FT hydrolysis"
FT BINDING 24..31
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT MUTAGEN 30
FT /note="K->A: 20-fold reduction in sporulation efficiency.
FT Largely enriched at the forespore periphery, although some
FT localization to the cytosol. Binding of ATP reduced over
FT 23-fold. Leads to diminished ATP hydrolysis."
FT /evidence="ECO:0000269|PubMed:18691972"
FT MUTAGEN 30
FT /note="K->E: Mislocalized to the mother cell cytosol.
FT Misassembles the spore coat. Mislocalizes CotE but not
FT SpoVM. Does not multimerize. Almost complete block in spore
FT formation."
FT /evidence="ECO:0000269|PubMed:18691972"
FT MUTAGEN 59
FT /note="L->P: Spores form largely normal coats and possess
FT at least some cortex, but cannot remain dehydrated after
FT mother cell lysis. Abnormal synthesis and an insufficient
FT level of spore peptidoglycan, which contains amidated
FT diaminopimelic acid, which is normally found only in
FT vegetative cell peptidoglycan. Defective in germination;
FT when associated with P-256."
FT /evidence="ECO:0000269|PubMed:11160095"
FT MUTAGEN 69
FT /note="M->L: Altered cortex and coat formation; when
FT associated with S-230."
FT /evidence="ECO:0000269|PubMed:11160095"
FT MUTAGEN 70
FT /note="T->A: 500-fold decrease in sporulation efficiency.
FT 5-log decrease in sporulation efficiency; no ATPase
FT activity, but no change in ATP-binding ability; unable to
FT polymerize and fails to promote coat assembly; when
FT associated with A-71."
FT /evidence="ECO:0000269|PubMed:23267091"
FT MUTAGEN 71
FT /note="T->A: Does not abrogate sporulation. 5-log decrease
FT in sporulation efficiency; no ATPase activity, but no
FT change in ATP-binding ability; unable to polymerize and
FT fails to promote coat assembly; when associated with A-70."
FT /evidence="ECO:0000269|PubMed:23267091"
FT MUTAGEN 97
FT /note="D->A: Completely abolished sporulation efficiency.
FT No ATPase activity, but no change in ATP-binding ability.
FT Unable to polymerize and fails to promote coat assembly;."
FT /evidence="ECO:0000269|PubMed:23267091"
FT MUTAGEN 98
FT /note="C->S: Defective in germination; when associated with
FT N-283."
FT /evidence="ECO:0000269|PubMed:11160095"
FT MUTAGEN 189
FT /note="S->K: Unable to sporulate."
FT /evidence="ECO:0000269|PubMed:23267091"
FT MUTAGEN 210
FT /note="I->A: Defective in germination; when associated with
FT V-367 and R-383."
FT /evidence="ECO:0000269|PubMed:11160095"
FT MUTAGEN 210
FT /note="I->M: Altered cortex and coat formation; when
FT associated with V-367 and R-383."
FT /evidence="ECO:0000269|PubMed:11160095"
FT MUTAGEN 230
FT /note="R->S: Altered cortex and coat formation; when
FT associated with L-69."
FT /evidence="ECO:0000269|PubMed:11160095"
FT MUTAGEN 241
FT /note="V->G: Altered cortex and coat formation."
FT /evidence="ECO:0000269|PubMed:11160095"
FT MUTAGEN 256
FT /note="H->P: Defective in germination; when associated with
FT P-59."
FT /evidence="ECO:0000269|PubMed:11160095"
FT MUTAGEN 283
FT /note="V->N: Defective in germination; when associated with
FT S-98."
FT /evidence="ECO:0000269|PubMed:11160095"
FT MUTAGEN 367
FT /note="I->V: Defective in germination; when associated with
FT A-210 and R-383. Altered cortex and coat formation; when
FT associated with M-210 and R-383."
FT /evidence="ECO:0000269|PubMed:11160095"
FT MUTAGEN 383
FT /note="I->R: Defective in germination; when associated with
FT A-210 and V-367. Altered cortex and coat formation; when
FT associated with M-210 and R-383."
FT /evidence="ECO:0000269|PubMed:11160095"
FT MUTAGEN 393
FT /note="L->P: Altered cortex and coat formation. Possesses
FT swirls of coat in the mother cell cytoplasm and does not
FT possess a cortex."
FT /evidence="ECO:0000269|PubMed:11160095"
FT MUTAGEN 400
FT /note="I->P: Altered cortex and coat formation, affects
FT localization to the forespore; when associated with R-457
FT and V-418."
FT /evidence="ECO:0000269|PubMed:11160095"
FT MUTAGEN 416
FT /note="G->R: Altered cortex and coat formation."
FT /evidence="ECO:0000269|PubMed:11160095"
FT MUTAGEN 418
FT /note="E->V: Altered cortex and coat formation, affects
FT localization to the forespore; when associated with P-400
FT and R-457."
FT /evidence="ECO:0000269|PubMed:11160095"
FT MUTAGEN 453
FT /note="V->G: Altered cortex and coat formation, affects
FT localization to the forespore."
FT /evidence="ECO:0000269|PubMed:11160095"
FT MUTAGEN 457
FT /note="I->R: Altered cortex and coat formation, affects
FT localization to the forespore; when associated with P-400
FT and V-418."
FT /evidence="ECO:0000269|PubMed:11160095"
FT MUTAGEN 486
FT /note="G->V: Suppressor mutation that reverses the
FT mislocalization and sporulation defect of the A-6 mutation
FT in SpoVM. Causes little impairment of sporulation."
FT /evidence="ECO:0000269|PubMed:17427285"
SQ SEQUENCE 492 AA; 55175 MW; 29EBA349DD18D12A CRC64;
MEKVDIFKDI AERTGGDIYL GVVGAVRTGK STFIKKFMEL VVLPNISNEA DRARAQDELP
QSAAGKTIMT TEPKFVPNQA MSVHVSDGLD VNIRLVDCVG YTVPGAKGYE DENGPRMINT
PWYEEPIPFH EAAEIGTRKV IQEHSTIGVV ITTDGTIGDI ARSDYIEAEE RVIEELKEVG
KPFIMVINSV RPYHPETEAM RQDLSEKYDI PVLAMSVESM RESDVLSVLR EALYEFPVLE
VNVNLPSWVM VLKENHWLRE SYQESVKETV KDIKRLRDVD RVVGQFSEFE FIESAGLAGI
ELGQGVAEID LYAPDHLYDQ ILKEVVGVEI RGRDHLLELM QDFAHAKTEY DQVSDALKMV
KQTGYGIAAP ALADMSLDEP EIIRQGSRFG VRLKAVAPSI HMIKVDVESE FAPIIGTEKQ
SEELVRYLMQ DFEDDPLSIW NSDIFGRSLS SIVREGIQAK LSLMPENARY KLKETLERII
NEGSGGLIAI IL
