ID   MUTS2_BACSU             Reviewed;         785 AA.
AC   P94545;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 2.
DT   02-SEP-2026, entry version 161.
DE   RecName: Full=Putative endonuclease MutS2 {ECO:0000305};
DE   AltName: Full=Ribosome-associated protein quality control-upstream factor {ECO:0000303|PubMed:35264791};
DE            Short=RQC-upstream factor {ECO:0000303|PubMed:35264791};
DE            Short=RqcU {ECO:0000303|PubMed:35264791};
DE            EC=3.6.4.- {ECO:0000305|PubMed:35264791, ECO:0000305|PubMed:38177497};
GN   Name=mutSB {ECO:0000303|PubMed:9384377};
GN   Synonyms=mutS2, rqcU {ECO:0000303|PubMed:35264791}, yshD
GN   {ECO:0000303|PubMed:8969504}; OrderedLocusNames=BSU28580;
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].
RC   STRAIN=168;
RX   PubMed=8969504; DOI=10.1099/13500872-142-11-3067;
RA   Wipat A., Carter N., Brignell C.S., Guy J.B., Piper K., Sanders J.,
RA   Emmerson P.T., Harwood C.R.;
RT   "The dnaB-pheA (256 degrees-240 degrees) region of the Bacillus subtilis
RT   chromosome containing genes responsible for stress responses, the
RT   utilization of plant cell walls and primary metabolism.";
RL   Microbiology 142:3067-3078(1996).
RN   [2]
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   [3]
RP   NO FUNCTION IN MISMATCH REPAIR, INDUCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=168;
RX   PubMed=11254128; DOI=10.1007/s004380000370;
RA   Rossolillo P., Albertini A.M.;
RT   "Functional analysis of the Bacillus subtilis yshD gene, a mutS
RT   paralogue.";
RL   Mol. Gen. Genet. 264:809-818(2001).
RN   [4]
RP   SUBCELLULAR LOCATION, INDUCTION, DOMAIN, DISRUPTION PHENOTYPE, AND
RP   MUTAGENESIS OF 636-LYS--LYS-785.
RX   PubMed=27799325; DOI=10.1128/jb.00682-16;
RA   Burby P.E., Simmons L.A.;
RT   "MutS2 Promotes Homologous Recombination in Bacillus subtilis.";
RL   J. Bacteriol. 199:0-0(2017).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, ATPASE ACTIVITY, SUBUNIT, DOMAIN, DISRUPTION
RP   PHENOTYPE, AND MUTAGENESIS OF GLU-416; 668-GLN--LYS-673; 702-LYS--LYS-785;
RP   711-ASP--ARG-713 AND HIS-743.
RC   STRAIN=168;
RX   PubMed=38177497; DOI=10.1038/s44318-023-00010-3;
RA   Park E.N., Mackens-Kiani T., Berhane R., Esser H., Erdenebat C.,
RA   Burroughs A.M., Berninghausen O., Aravind L., Beckmann R., Green R.,
RA   Buskirk A.R.;
RT   "B. subtilis MutS2 splits stalled ribosomes into subunits without mRNA
RT   cleavage.";
RL   EMBO J. 43:484-506(2024).
RN   [6] {ECO:0007744|PDB:7QV3}
RP   STRUCTURE BY ELECTRON MICROSCOPY (5.14 ANGSTROMS) IN COMPLEX WITH 70S
RP   RIBOSOME, FUNCTION, CATALYTIC ACTIVITY, ATPASE ACTIVITY, SUBUNIT, DOMAIN,
RP   DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLY-340; LYS-341; GLU-416;
RP   702-LYS--LYS-785 AND ASP-711.
RC   STRAIN=168;
RX   PubMed=35264791; DOI=10.1038/s41586-022-04487-6;
RA   Cerullo F., Filbeck S., Patil P.R., Hung H.C., Xu H., Vornberger J.,
RA   Hofer F.W., Schmitt J., Kramer G., Bukau B., Hofmann K., Pfeffer S.,
RA   Joazeiro C.A.P.;
RT   "Bacterial ribosome collision sensing by a MutS DNA repair ATPase
RT   paralogue.";
RL   Nature 603:509-514(2022).
CC   -!- FUNCTION: Acts as a ribosome collision sensor splitting the ribosome
CC       into its 2 subunits (PubMed:35264791). Detects stalled/collided disomes
CC       (pairs of ribosomes where the leading ribosome is stalled and a second
CC       ribosome has collided with it) which it binds and splits, by an ATP-
CC       hydrolysis driven conformational change (PubMed:35264791,
CC       PubMed:38177497). Does not seem to have endoribonuclease activity (in
CC       the context of ribosome stalling) (PubMed:38177497). Acts upstream of
CC       the ribosome quality control system (RQC), a ribosome-associated
CC       complex that mediates the extraction of incompletely synthesized
CC       nascent chains from stalled ribosomes and their subsequent degradation,
CC       probably generates substrates for RQC (Probable) (PubMed:35264791,
CC       PubMed:38177497). {ECO:0000269|PubMed:35264791,
CC       ECO:0000269|PubMed:38177497, ECO:0000305|PubMed:35264791,
CC       ECO:0000305|PubMed:38177497}.
CC   -!- FUNCTION: Does not seem to be involved in mismatch repair or in the
CC       prevention of interspecific recombination during DNA transformation
CC       (PubMed:11254128). Might be involved in homologous recombination
CC       (Probable) (PubMed:27799325). Putative endonuclease that may be
CC       involved in the suppression of homologous recombination and may
CC       therefore have a key role in the control of bacterial genetic diversity
CC       (By similarity). {ECO:0000255|HAMAP-Rule:MF_00092,
CC       ECO:0000269|PubMed:11254128, ECO:0000305|PubMed:27799325}.
CC   -!- SUBUNIT: Binds to ribosomes as a homodimer (PubMed:35264791,
CC       PubMed:38177497). Binds to stalled/collided disomes, association is
CC       greater in (ribosome-targeted) antibiotic-treated cells (with increased
CC       stalling at specific mRNA sites) (PubMed:35264791, PubMed:38177497).
CC       The clamp domain of one monomer binds the A-site finger, the 23S rRNA
CC       of the central protuberance and ribosomal protein uL5 of the leading
CC       (stalled) ribosome, while the other monomer binds in a gap between the
CC       ribosomal central protuberance and the L1 stalk of the leading ribosome
CC       (PubMed:35264791). {ECO:0000255|HAMAP-Rule:MF_00092,
CC       ECO:0000269|PubMed:35264791, ECO:0000269|PubMed:38177497}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27799325}. Note=A
CC       GFP-MutS2 fusion protein is diffuse over all the cell, no particular
CC       localization is seen (PubMed:27799325). {ECO:0000269|PubMed:27799325}.
CC   -!- INDUCTION: Constitutively transcribed in rich and minimal media,
CC       highest transcripts occur in stationary phase in minimal media
CC       (PubMed:11254128). In rich medium protein is expressed at a constant
CC       level during all growth stages (at protein level) (PubMed:27799325).
CC       Probably part of the polX-mutS2-yshE operon (Probable)
CC       (PubMed:11254128). {ECO:0000269|PubMed:11254128,
CC       ECO:0000269|PubMed:27799325, ECO:0000305|PubMed:11254128}.
CC   -!- DOMAIN: The KOW and Smr domain are required for mitomycin C resistance
CC       (PubMed:27799325). The ATPase and clamp domain (approximately residues
CC       1-586) form a tweezer that holds the lead (stalled) ribosome
CC       (PubMed:35264791). The long coiled-coil domain binds along the disome
CC       interface, coordinated by interactions with helix 39 of the 16S rRNA of
CC       both ribosomes (PubMed:35264791). Deletion of the Smr domain (residues
CC       702-785), which might have nuclease activity, has litle impact on
CC       ribosome rescue in vitro, but the strain is less competitive against
CC       wild-type in vivo (PubMed:35264791). In another cryo-EM structure only
CC       the KOW and Smr regions are visible in association with stalled disomes
CC       (PubMed:38177497). In this study the Smr domain interacts with uS7 and
CC       uS11 of the leading (stalled) ribosome, with uS3 on the collided
CC       ribosome, while the KOW regions contact uS10 in both ribosomal subunits
CC       (PubMed:38177497). {ECO:0000269|PubMed:27799325,
CC       ECO:0000269|PubMed:35264791, ECO:0000269|PubMed:38177497}.
CC   -!- DISRUPTION PHENOTYPE: Not essential, it can be deleted
CC       (PubMed:11254128, PubMed:27799325, PubMed:35264791, PubMed:38177497).
CC       No change in spontaneous mutation rate; does not genetically interact
CC       with mutS or mutL (PubMed:11254128, PubMed:27799325). About 10-fold
CC       increased sensitivity to mitomycin C (MMC) (PubMed:27799325). Decreased
CC       transformation efficiency of both chromosomal (5-fold decrease) and
CC       plasmid DNA; a double mutS2-recU deletion strain has a 57-fold decrease
CC       in chromosomal DNA transformation efficicency (PubMed:27799325).
CC       Hypersensitive to antibiotics that target the ribosome; erythromycin,
CC       chloramphencicol and tetracycline, but not to beta-lactam antibiotics
CC       (PubMed:38177497, PubMed:35264791). Double mutSB-rqcH, mutSB-ssrA and
CC       triple mutSB-rqcH-ssrA deletions are even more sensitive to
CC       erythromycin (PubMed:35264791). Decreases alanine-tailing by 80%; Ala-
CC       tailing by RqcH (which targets aberrant nascent chains for degradation)
CC       requires splitting of the 30S and 50S subunits of stalled ribosomes
CC       (PubMed:35264791, PubMed:38177497). Decreased rescue of stalled
CC       ribosomes (PubMed:38177497). {ECO:0000269|PubMed:11254128,
CC       ECO:0000269|PubMed:27799325, ECO:0000269|PubMed:35264791,
CC       ECO:0000269|PubMed:38177497}.
CC   -!- MISCELLANEOUS: The ssrA gene (for tmRNA) encodes the SsrA tag added to
CC       nascent proteins in stalled ribosomes by trans-translation, which
CC       targets the nascent protein for degradation.
CC   -!- SIMILARITY: Belongs to the DNA mismatch repair MutS family. MutS2
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00092}.
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DR   EMBL; Z75208; CAA99569.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14818.1; -; Genomic_DNA.
DR   PIR; D69985; D69985.
DR   RefSeq; NP_390736.1; NC_000964.3.
DR   RefSeq; WP_003229541.1; NC_000964.3.
DR   PDB; 7QV3; EM; 5.14 A; v/w=1-785.
DR   PDB; 8QPP; EM; 3.40 A; W=1-785.
DR   PDB; 8R55; EM; 3.57 A; z=1-785.
DR   AlphaFoldDB; P94545; -.
DR   EMDB; EMD-14159; -.
DR   SMR; P94545; -.
DR   FunCoup; P94545; 149.
DR   STRING; 224308.BSU28580; -.
DR   PaxDb; 224308-BSU28580; -.
DR   EnsemblBacteria; CAB14818; CAB14818; BSU_28580.
DR   GeneID; 937447; -.
DR   KEGG; bsu:BSU28580; -.
DR   PATRIC; fig|224308.179.peg.3105; -.
DR   eggNOG; COG1193; Bacteria.
DR   InParanoid; P94545; -.
DR   OrthoDB; 9808166at2; -.
DR   PhylomeDB; P94545; -.
DR   BioCyc; BSUB:BSU28580-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; EXP:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR   GO; GO:0030983; F:mismatched DNA binding; IEA:InterPro.
DR   GO; GO:0043023; F:ribosomal large subunit binding; IDA:UniProtKB.
DR   GO; GO:0019843; F:rRNA binding; IDA:UniProtKB.
DR   GO; GO:0006298; P:mismatch repair; IEA:InterPro.
DR   GO; GO:0045910; P:negative regulation of DNA recombination; IEA:InterPro.
DR   GO; GO:0072344; P:rescue of stalled cytosolic ribosome; IDA:UniProtKB.
DR   CDD; cd03280; ABC_MutS2; 1.
DR   CDD; cd06503; ATP-synt_Fo_b; 1.
DR   FunFam; 3.30.1370.110:FF:000013; Endonuclease MutS2; 1.
DR   FunFam; 3.40.50.300:FF:000830; Endonuclease MutS2; 1.
DR   Gene3D; 3.30.1370.110; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_00092; MutS2; 1.
DR   InterPro; IPR000432; DNA_mismatch_repair_MutS_C.
DR   InterPro; IPR007696; DNA_mismatch_repair_MutS_core.
DR   InterPro; IPR036187; DNA_mismatch_repair_MutS_sf.
DR   InterPro; IPR046893; MSSS.
DR   InterPro; IPR045076; MutS.
DR   InterPro; IPR005747; MutS2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR002625; Smr_dom.
DR   InterPro; IPR036063; Smr_dom_sf.
DR   NCBIfam; TIGR01069; mutS2; 1.
DR   PANTHER; PTHR48466:SF2; OS10G0509000 PROTEIN; 1.
DR   PANTHER; PTHR48466; OS10G0509000 PROTEIN-RELATED; 1.
DR   Pfam; PF20297; MSSS; 1.
DR   Pfam; PF00488; MutS_V; 1.
DR   Pfam; PF01713; Smr; 1.
DR   PIRSF; PIRSF005814; MutS_YshD; 1.
DR   SMART; SM00534; MUTSac; 1.
DR   SMART; SM00533; MUTSd; 1.
DR   SMART; SM00463; SMR; 1.
DR   SUPFAM; SSF48334; DNA repair protein MutS, domain III; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF160443; SMR domain-like; 1.
DR   PROSITE; PS00486; DNA_MISMATCH_REPAIR_2; 1.
DR   PROSITE; PS50828; SMR; 1.
DR   PDBsum; 7QV3; -.
DR   PDBsum; 8QPP; -.
DR   PDBsum; 8R55; -.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Coiled coil; Cytoplasm; DNA-binding; Hydrolase;
KW   Nucleotide-binding; Reference proteome; RNA-binding; rRNA-binding.
FT   CHAIN           1..785
FT                   /note="Putative endonuclease MutS2"
FT                   /id="PRO_0000115217"
FT   DOMAIN          710..785
FT                   /note="Smr"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
FT   REGION          636..785
FT                   /note="Partially complements a deletion for mitomycin C
FT                   (MMC) resistance and for chromosomal DNA transformation"
FT                   /evidence="ECO:0000269|PubMed:27799325"
FT   REGION          641..681
FT                   /note="KOW region"
FT                   /evidence="ECO:0000305|PubMed:35264791,
FT                   ECO:0000305|PubMed:38177497"
FT   COILED          513..586
FT                   /evidence="ECO:0000305|PubMed:35264791"
FT   BINDING         335..342
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00092"
FT   MUTAGEN         340
FT                   /note="G->R: Prevents disome splitting."
FT                   /evidence="ECO:0000269|PubMed:35264791"
FT   MUTAGEN         341
FT                   /note="K->A: Probably binds less ATP, more associated with
FT                   polysomes than disomes or trisomes, does not restore
FT                   alanine-tailing, does not restore erythromycin sensitivity,
FT                   outcompeted by wild-type strain in vivo."
FT                   /evidence="ECO:0000269|PubMed:35264791"
FT   MUTAGEN         416
FT                   /note="E->A: Probably decreased ATP hydrolysis, more
FT                   associated with polysomes than disomes or trisomes, does
FT                   not restore alanine-tailing, does not restore erythromycin
FT                   sensitivity, prevents disome splitting."
FT                   /evidence="ECO:0000269|PubMed:35264791,
FT                   ECO:0000269|PubMed:38177497"
FT   MUTAGEN         636..785
FT                   /note="Missing: Does not complement sensitivity to MMC, nor
FT                   chromosomal DNA transformation."
FT                   /evidence="ECO:0000269|PubMed:27799325"
FT   MUTAGEN         668..673
FT                   /note="QIGILK->AIGAAA: Decreased binding to
FT                   stalled/collided disomes."
FT                   /evidence="ECO:0000269|PubMed:38177497"
FT   MUTAGEN         702..785
FT                   /note="Missing: Slightly reduced ability to restore
FT                   erythromycin resistance in vivo, outcompeted by wild-type
FT                   strain in vivo. Dramatically decreased binding to
FT                   stalled/collided disomes."
FT                   /evidence="ECO:0000269|PubMed:35264791,
FT                   ECO:0000269|PubMed:38177497"
FT   MUTAGEN         711..713
FT                   /note="DLR->ALA: Dramatically decreased binding to
FT                   stalled/collided disomes, no change in disome splitting in
FT                   vitro."
FT                   /evidence="ECO:0000269|PubMed:38177497"
FT   MUTAGEN         711
FT                   /note="D->A: Slightly reduced ability to restore
FT                   erythromycin resistance in vivo, outcompeted by wild-type
FT                   strain in vivo."
FT                   /evidence="ECO:0000269|PubMed:35264791"
FT   MUTAGEN         743
FT                   /note="H->A: Dramatically decreased binding to
FT                   stalled/collided disomes."
FT                   /evidence="ECO:0000269|PubMed:38177497"
FT   STRAND          708..711
FT                   /evidence="ECO:0007829|PDB:8QPP"
FT   HELIX           717..730
FT                   /evidence="ECO:0007829|PDB:8QPP"
FT   TURN            731..733
FT                   /evidence="ECO:0007829|PDB:8QPP"
FT   STRAND          737..742
FT                   /evidence="ECO:0007829|PDB:8QPP"
FT   HELIX           751..760
FT                   /evidence="ECO:0007829|PDB:8QPP"
FT   STRAND          762..769
FT                   /evidence="ECO:0007829|PDB:8QPP"
FT   HELIX           772..774
FT                   /evidence="ECO:0007829|PDB:8QPP"
FT   HELIX           776..778
FT                   /evidence="ECO:0007829|PDB:8QPP"
FT   STRAND          779..784
FT                   /evidence="ECO:0007829|PDB:8QPP"
SQ   SEQUENCE   785 AA;  87417 MW;  20D14CDB931167C2 CRC64;
     MQQKVLSALE FHKVKEQVIG HAASSLGKEM LLELKPSASI DEIKKQLDEV DEASDIIRLR
     GQAPFGGLVD IRGALRRAEI GSVLSPSEFT EISGLLYAVK QMKHFITQMA EDGVDIPLIH
     QHAEQLITLS DLERDINSCI DDHGEVLDHA SETLRGIRTQ LRTLESRVRD RLESMLRSSS
     ASKMLSDTIV TIRNDRFVIP VKQEYRSSYG GIVHDTSSSG ATLFIEPQAI VDMNNSLQQA
     KVKEKQEIER ILRVLTEKTA EYTEELFLDL QVLQTLDFIF AKARYAKAVK ATKPIMNDTG
     FIRLKKARHP LLPPDQVVAN DIELGRDFST IVITGPNTGG KTVTLKTLGL LTLMAQSGLH
     IPADEGSEAA VFEHVFADIG DEQSIEQSLS TFSSHMVNIV GILEQVNENS LVLFDELGAG
     TDPQEGAALA MSILDDVHRT NARVLATTHY PELKAYGYNR EGVMNASVEF DIETLSPTYK
     LLIGVPGRSN AFEISKRLGL PDHIIGQAKS EMTAEHNEVD TMIASLEQSK KRAEEELSET
     ESIRKEAEKL HKELQQQIIE LNSKKDKMLE EAEQQAAEKV KAAMKEAEDI IHELRTIKEE
     HKSFKDHELI NAKKRLEGAM PAFEKSKKPE KPKTQKRDFK PGDEVKVLTF GQKGTLLEKT
     GGNEWNVQIG ILKMKVKEKD LEFIKSAPEP KKEKMITAVK GKDYHVSLEL DLRGERYENA
     LSRVEKYLDD AVLAGYPRVS IIHGKGTGAL RKGVQDLLKN HRSVKSSRFG EAGEGGSGVT
     VVELK
//