BSR_VIBCH
ID BSR_VIBCH Reviewed; 407 AA.
AC Q9KSE5;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 08-MAY-2019, sequence version 3.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Broad specificity amino-acid racemase {ECO:0000255|HAMAP-Rule:MF_02212, ECO:0000305|PubMed:24419381};
DE EC=5.1.1.10 {ECO:0000255|HAMAP-Rule:MF_02212, ECO:0000269|PubMed:24419381};
DE AltName: Full=Broad spectrum racemase {ECO:0000303|PubMed:19762646, ECO:0000303|PubMed:24419381};
DE Flags: Precursor;
GN Name=bsrV {ECO:0000303|PubMed:19762646}; OrderedLocusNames=VC_1312;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=19762646; DOI=10.1126/science.1178123;
RA Lam H., Oh D.C., Cava F., Takacs C.N., Clardy J., de Pedro M.A.,
RA Waldor M.K.;
RT "D-amino acids govern stationary phase cell wall remodeling in bacteria.";
RL Science 325:1552-1555(2009).
RN [3]
RP REVIEW.
RX PubMed=29446806; DOI=10.2436/20.1501.01.296;
RA Cava F.;
RT "Divergent functional roles of D-amino acids secreted by Vibrio cholerae.";
RL Int. Microbiol. 20:149-150(2017).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=29028003; DOI=10.1038/ismej.2017.176;
RA Alvarez L., Aliashkevich A., de Pedro M.A., Cava F.;
RT "Bacterial secretion of D-arginine controls environmental microbial
RT biodiversity.";
RL ISME J. 12:438-450(2018).
RN [5] {ECO:0007744|PDB:4BEQ, ECO:0007744|PDB:4BEU}
RP X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS) OF 24-407 OF WILD-TYPE AND MUTANT
RP ALA-173/ALA-174 IN COMPLEX WITH PYRIDOXAL PHOSPHATE, FUNCTION, CATALYTIC
RP ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY,
RP SUBUNIT, MUTAGENESIS OF PRO-25; CYS-70; ARG-119; ARG-121; ALA-165; ASN-167;
RP GLY-169; 173-ARG-ASN-174 AND PRO-391, AND BIOTECHNOLOGY.
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=24419381; DOI=10.1107/s1399004713024838;
RA Espaillat A., Carrasco-Lopez C., Bernardo-Garcia N., Pietrosemoli N.,
RA Otero L.H., Alvarez L., de Pedro M.A., Pazos F., Davis B.M., Waldor M.K.,
RA Hermoso J.A., Cava F.;
RT "Structural basis for the broad specificity of a new family of amino-acid
RT racemases.";
RL Acta Crystallogr. D 70:79-90(2014).
CC -!- FUNCTION: Amino-acid racemase able to utilize a broad range of
CC substrates. Reversibly racemizes ten of the 19 natural chiral amino
CC acids known, including both non-beta-branched aliphatic amino acids
CC (Ala, Leu, Met, Ser, Cys, Gln and Asn) and positively charged amino
CC acids (His, Lys and Arg). Among these substrates, is the most efficient
CC with lysine and arginine. Is also able to catalyze the racemization of
CC several amino acids that are not typically incorporated into proteins
CC such as ornithine and norleucine. Is not active on negatively charged
CC (Glu and Asp) or aromatic (Tyr, Trp and Phe) amino acids and displays
CC minimal activity towards beta-branched aliphatic (Ile, Val and Thr)
CC substrates (PubMed:24419381). Enables bacteria to produce and release
CC extracellular non-canonical D-amino acids (NCDAAs) that regulate
CC diverse cellular processes which may function as part of a cooperative
CC strategy in vibrio communities to protect non-producing members from
CC competing bacteria (PubMed:29446806, PubMed:29028003). D-amino acid
CC production by BsrV provides a cue for V.cholerae to decrease
CC peptidoglycan synthesis and to alter its cell wall via incorporation of
CC NCDAAs into the muropeptides, in adaption to stationary phase
CC conditions (PubMed:19762646, PubMed:29028003).
CC {ECO:0000269|PubMed:19762646, ECO:0000269|PubMed:24419381,
CC ECO:0000269|PubMed:29028003, ECO:0000303|PubMed:29446806}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an L-alpha-amino acid = a D-alpha-amino acid;
CC Xref=Rhea:RHEA:18317, ChEBI:CHEBI:59869, ChEBI:CHEBI:59871;
CC EC=5.1.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_02212,
CC ECO:0000269|PubMed:24419381};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysine = D-lysine; Xref=Rhea:RHEA:22864, ChEBI:CHEBI:32551,
CC ChEBI:CHEBI:32557; Evidence={ECO:0000255|HAMAP-Rule:MF_02212,
CC ECO:0000269|PubMed:24419381};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-arginine = D-arginine; Xref=Rhea:RHEA:18069,
CC ChEBI:CHEBI:32682, ChEBI:CHEBI:32689; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_02212, ECO:0000269|PubMed:24419381,
CC ECO:0000305|PubMed:29028003};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-alanine = D-alanine; Xref=Rhea:RHEA:20249,
CC ChEBI:CHEBI:57416, ChEBI:CHEBI:57972;
CC Evidence={ECO:0000269|PubMed:24419381};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-serine = D-serine; Xref=Rhea:RHEA:10980, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:35247; Evidence={ECO:0000269|PubMed:24419381};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-methionine = D-methionine; Xref=Rhea:RHEA:12492,
CC ChEBI:CHEBI:57844, ChEBI:CHEBI:57932;
CC Evidence={ECO:0000269|PubMed:19762646, ECO:0000269|PubMed:24419381};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-leucine = D-leucine; Xref=Rhea:RHEA:59396,
CC ChEBI:CHEBI:57427, ChEBI:CHEBI:143079;
CC Evidence={ECO:0000269|PubMed:24419381, ECO:0000305|PubMed:29028003};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-cysteine = D-cysteine; Xref=Rhea:RHEA:59272,
CC ChEBI:CHEBI:35235, ChEBI:CHEBI:35236;
CC Evidence={ECO:0000269|PubMed:24419381};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamine = D-glutamine; Xref=Rhea:RHEA:59276,
CC ChEBI:CHEBI:58000, ChEBI:CHEBI:58359;
CC Evidence={ECO:0000269|PubMed:24419381};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-asparagine = D-asparagine; Xref=Rhea:RHEA:59280,
CC ChEBI:CHEBI:58048, ChEBI:CHEBI:74337;
CC Evidence={ECO:0000269|PubMed:24419381};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-histidine = D-histidine; Xref=Rhea:RHEA:59188,
CC ChEBI:CHEBI:57595, ChEBI:CHEBI:142967;
CC Evidence={ECO:0000269|PubMed:24419381};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-ornithine = D-ornithine; Xref=Rhea:RHEA:11584,
CC ChEBI:CHEBI:46911, ChEBI:CHEBI:57668;
CC Evidence={ECO:0000269|PubMed:24419381};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-2-aminohexanoate = D-2-aminohexanoate; Xref=Rhea:RHEA:59400,
CC ChEBI:CHEBI:58455, ChEBI:CHEBI:143080;
CC Evidence={ECO:0000269|PubMed:24419381};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-homoserine = D-homoserine; Xref=Rhea:RHEA:59404,
CC ChEBI:CHEBI:57476, ChEBI:CHEBI:143081;
CC Evidence={ECO:0000269|PubMed:24419381};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02212,
CC ECO:0000269|PubMed:24419381};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=11 mM for L-alanine {ECO:0000269|PubMed:24419381};
CC KM=28 mM for L-serine {ECO:0000269|PubMed:24419381};
CC KM=11 mM for L-methionine {ECO:0000269|PubMed:24419381};
CC KM=30 mM for L-leucine {ECO:0000269|PubMed:24419381};
CC KM=22 mM for L-glutamine {ECO:0000269|PubMed:24419381};
CC KM=15 mM for L-asparagine {ECO:0000269|PubMed:24419381};
CC KM=9 mM for L-lysine {ECO:0000269|PubMed:24419381};
CC KM=18 mM for L-arginine {ECO:0000269|PubMed:24419381};
CC Note=kcat is 1.68 sec(-1) with L-alanine as substrate. kcat is 4.68
CC sec(-1) with L-serine as substrate. kcat is 2.94 sec(-1) with L-
CC methionine as substrate. kcat is 2.30 sec(-1) with L-leucine as
CC substrate. kcat is 2.59 sec(-1) with L-glutamine as substrate. kcat
CC is 0.05 sec(-1) with L-asparagine as substrate. kcat is 4.76 sec(-1)
CC with L-lysine as substrate. kcat is 5.09 sec(-1) with L-arginine as
CC substrate. {ECO:0000269|PubMed:24419381};
CC -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:24419381}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_02212,
CC ECO:0000269|PubMed:19762646}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene have normal growth and
CC morphology but produce minimal D-Met, D-Leu, D-Val, and D-Ile. They
CC contain twice the amount of peptidoglycan (PG) of wild-type cells in
CC stationary phase, whereas PG levels do not differ in exponential phase.
CC Addition of physiological amounts of D-Met and D-Leu to cultures with a
CC deletion in bsrV reduce the amount of PG to wild-type levels, which
CC confirms that the absence of D-amino acids accounts for the increased
CC PG in the bsrV mutant. Moreover, the structure of wild-type and bsrV
CC mutant PG isolated from stationary phase cells differed significantly.
CC The glycan chains in stationary phase PG from the bsrV mutant are about
CC 80% the length of the wild type, pentapeptides are reduced by about
CC 50%, and there is an increase in trimer muropeptides. Despite being
CC less abundant, the PG in wild-type cells appears to be stronger than in
CC bsrV mutant cells. Wild-type cells survive 20 times more than bsrV
CC mutant cells when subjected to an osmotic challenge (PubMed:19762646).
CC D-Arg is not detected in the supernatant of cells lacking this gene.
CC Production of other D-amino acids (for example, D-Leu) is also impaired
CC in the deletion mutant (PubMed:29028003). {ECO:0000269|PubMed:19762646,
CC ECO:0000269|PubMed:29028003}.
CC -!- BIOTECHNOLOGY: The substrate range of BsrV, which includes activity
CC towards non-natural substrates (e.g. ornithine, norleucine, homoserine,
CC N-acetyl lysine methyl ester, diaminobutyrate and aminobutyrate), is
CC broader than any other known amino-acid racemase and suggests that it
CC has great potential for biotechnological and industrial applications.
CC Currently, production of DAA is an expensive process that is typically
CC reliant upon inefficient chemical catalysts.
CC {ECO:0000305|PubMed:24419381}.
CC -!- SIMILARITY: Belongs to the alanine racemase family. Bsr subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_02212, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF94470.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE003852; AAF94470.1; ALT_INIT; Genomic_DNA.
DR PIR; A82215; A82215.
DR RefSeq; NP_230956.2; NC_002505.1.
DR RefSeq; WP_000545503.1; NZ_LT906614.1.
DR PDB; 4BEQ; X-ray; 1.50 A; A=24-407.
DR PDB; 4BEU; X-ray; 1.15 A; A=24-407.
DR PDB; 7AGZ; X-ray; 1.52 A; A/B=24-407.
DR PDBsum; 4BEQ; -.
DR PDBsum; 4BEU; -.
DR PDBsum; 7AGZ; -.
DR AlphaFoldDB; Q9KSE5; -.
DR SMR; Q9KSE5; -.
DR STRING; 243277.VC_1312; -.
DR DNASU; 2614766; -.
DR EnsemblBacteria; AAF94470; AAF94470; VC_1312.
DR GeneID; 57739977; -.
DR KEGG; vch:VC_1312; -.
DR eggNOG; COG0787; Bacteria.
DR HOGENOM; CLU_028393_2_2_6; -.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0008784; F:alanine racemase activity; IBA:GO_Central.
DR GO; GO:0047679; F:arginine racemase activity; IEA:RHEA.
DR GO; GO:0018113; F:lysine racemase activity; IEA:RHEA.
DR GO; GO:0018111; F:methionine racemase activity; IEA:RHEA.
DR GO; GO:0050157; F:ornithine racemase activity; IEA:RHEA.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0030378; F:serine racemase activity; IEA:RHEA.
DR GO; GO:0030632; P:D-alanine biosynthetic process; IBA:GO_Central.
DR CDD; cd06826; PLPDE_III_AR2; 1.
DR Gene3D; 2.40.37.10; -; 1.
DR Gene3D; 3.20.20.10; -; 1.
DR HAMAP; MF_02212; Bsr_racemase; 1.
DR InterPro; IPR000821; Ala_racemase.
DR InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR InterPro; IPR011079; Ala_racemase_C.
DR InterPro; IPR001608; Ala_racemase_N.
DR InterPro; IPR020622; Ala_racemase_pyridoxalP-BS.
DR InterPro; IPR029066; PLP-binding_barrel.
DR InterPro; IPR043698; Racemase_Bsr/Lyr.
DR Pfam; PF00842; Ala_racemase_C; 1.
DR Pfam; PF01168; Ala_racemase_N; 1.
DR PRINTS; PR00992; ALARACEMASE.
DR SMART; SM01005; Ala_racemase_C; 1.
DR SUPFAM; SSF50621; SSF50621; 1.
DR SUPFAM; SSF51419; SSF51419; 1.
DR TIGRFAMs; TIGR00492; alr; 1.
DR PROSITE; PS00395; ALANINE_RACEMASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Isomerase; Periplasm; Pyridoxal phosphate;
KW Reference proteome; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02212"
FT CHAIN 24..407
FT /note="Broad specificity amino-acid racemase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02212"
FT /id="PRO_0000114592"
FT ACT_SITE 74
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02212"
FT ACT_SITE 299
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02212"
FT BINDING 173
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02212"
FT BINDING 347
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02212"
FT SITE 391
FT /note="Specificity determinant that enlarges the space
FT within the active site of Bsr compared to Alr, allowing the
FT accomodation of a wider range of substrates"
FT /evidence="ECO:0000305|PubMed:24419381"
FT MOD_RES 74
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02212,
FT ECO:0000269|PubMed:24419381, ECO:0007744|PDB:4BEQ,
FT ECO:0007744|PDB:4BEU"
FT DISULFID 70..96
FT /evidence="ECO:0000250|UniProtKB:I0J1I6, ECO:0000255|HAMAP-
FT Rule:MF_02212"
FT MUTAGEN 25
FT /note="P->E: Completely abolishes the catalytic activity
FT towards Ala and Met and dramatically impairs (70%
FT reduction) activity towards Arg."
FT /evidence="ECO:0000269|PubMed:24419381"
FT MUTAGEN 70
FT /note="C->A: Completely abolishes or hihgly reduces the
FT catalytic activity towards Ala, Ser and large aliphatic
FT side chains, while activity towards basic amino acids is
FT preserved."
FT /evidence="ECO:0000269|PubMed:24419381"
FT MUTAGEN 119
FT /note="R->A: Hihgly reduces the catalytic activity towards
FT Ala and Ser and completely abolishes activity towards Met,
FT Leu, Asn, Gln, Lys and Arg."
FT /evidence="ECO:0000269|PubMed:24419381"
FT MUTAGEN 121
FT /note="R->A: Completely abolishes or hihgly reduces the
FT catalytic activity towards all the amino acids."
FT /evidence="ECO:0000269|PubMed:24419381"
FT MUTAGEN 165
FT /note="A->K: Completely abolishes or hihgly reduces the
FT catalytic activity towards all the amino acids except Gln."
FT /evidence="ECO:0000269|PubMed:24419381"
FT MUTAGEN 167
FT /note="N->A: Completely abolishes or hihgly reduces the
FT catalytic activity towards all the amino acids."
FT /evidence="ECO:0000269|PubMed:24419381"
FT MUTAGEN 169
FT /note="G->A: Completely abolishes or hihgly reduces the
FT catalytic activity towards all the amino acids except Gln
FT and Arg."
FT /evidence="ECO:0000269|PubMed:24419381"
FT MUTAGEN 173..174
FT /note="RN->AA: Completely abolishes or hihgly reduces the
FT catalytic activity towards all the amino acids."
FT /evidence="ECO:0000269|PubMed:24419381"
FT MUTAGEN 391
FT /note="P->N: Completely abolishes the catalytic activity
FT towards Ala, Ser and large aliphatic side chains, while
FT activity towards basic amino acids is preserved."
FT /evidence="ECO:0000269|PubMed:24419381"
FT HELIX 35..39
FT /evidence="ECO:0007829|PDB:4BEU"
FT STRAND 41..48
FT /evidence="ECO:0007829|PDB:4BEU"
FT HELIX 49..60
FT /evidence="ECO:0007829|PDB:4BEU"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:4BEU"
FT HELIX 74..78
FT /evidence="ECO:0007829|PDB:4BEU"
FT HELIX 82..91
FT /evidence="ECO:0007829|PDB:4BEU"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:4BEU"
FT HELIX 102..110
FT /evidence="ECO:0007829|PDB:4BEU"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:4BEU"
FT HELIX 125..130
FT /evidence="ECO:0007829|PDB:4BEU"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:4BEU"
FT STRAND 137..140
FT /evidence="ECO:0007829|PDB:4BEU"
FT HELIX 143..156
FT /evidence="ECO:0007829|PDB:4BEU"
FT STRAND 160..166
FT /evidence="ECO:0007829|PDB:4BEU"
FT STRAND 173..176
FT /evidence="ECO:0007829|PDB:4BEU"
FT HELIX 181..191
FT /evidence="ECO:0007829|PDB:4BEU"
FT STRAND 196..202
FT /evidence="ECO:0007829|PDB:4BEU"
FT HELIX 210..230
FT /evidence="ECO:0007829|PDB:4BEU"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:4BEU"
FT STRAND 239..243
FT /evidence="ECO:0007829|PDB:4BEU"
FT HELIX 245..250
FT /evidence="ECO:0007829|PDB:4BEU"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:4BEU"
FT TURN 263..267
FT /evidence="ECO:0007829|PDB:4BEU"
FT STRAND 279..284
FT /evidence="ECO:0007829|PDB:4BEU"
FT STRAND 287..291
FT /evidence="ECO:0007829|PDB:4BEU"
FT STRAND 296..298
FT /evidence="ECO:0007829|PDB:4BEU"
FT HELIX 299..301
FT /evidence="ECO:0007829|PDB:4BEU"
FT STRAND 309..315
FT /evidence="ECO:0007829|PDB:4BEU"
FT HELIX 318..320
FT /evidence="ECO:0007829|PDB:4BEU"
FT HELIX 324..326
FT /evidence="ECO:0007829|PDB:4BEU"
FT TURN 327..329
FT /evidence="ECO:0007829|PDB:4BEU"
FT STRAND 331..334
FT /evidence="ECO:0007829|PDB:4BEU"
FT STRAND 337..341
FT /evidence="ECO:0007829|PDB:4BEU"
FT STRAND 350..353
FT /evidence="ECO:0007829|PDB:4BEU"
FT STRAND 365..372
FT /evidence="ECO:0007829|PDB:4BEU"
FT STRAND 375..377
FT /evidence="ECO:0007829|PDB:7AGZ"
FT HELIX 379..386
FT /evidence="ECO:0007829|PDB:4BEU"
FT HELIX 390..400
FT /evidence="ECO:0007829|PDB:4BEU"
FT STRAND 403..406
FT /evidence="ECO:0007829|PDB:4BEU"
SQ SEQUENCE 407 AA; 44066 MW; 61B86E8502172FC1 CRC64;
MHFKATLLSL SIAATLPSFS LSAAPLHIDT ALPDAAQIQQ SNSWLEISLG QFQSNIEQFK
SHMNANTKIC AIMKADAYGN GIRGLMPTII AQGIPCVGVA SNAEARAVRE SGFKGELIRV
RSASLSEMSS ALDLNIEELI GTHQQALDLA ELAKQSGKTL KVHIALNDGG MGRNGIDMTT
EAGKKEAVSI ATQPSLSVVG IMTHFPNYNA DEVRAKLAQF KESSTWLMQQ ANLKREEITL
HVANSYTALN VPEAQLDMVR PGGVLFGDLP TNPEYPSIVS FKTRVSSLHH LPKDSTVGYD
STFTTSRDSV LANLPVGYSD GYPRKMGNKA EVLINGQRAK VVGVTSMNTT VVDVTEIKGV
LPGQEVVLFG QQQKQSIAVS EMENNAELIF PELYTLWGTS NPRFYVK
