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   13-SEP-2023, entry version 129.
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; Pseudomonadota; 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
CC         L-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   KEGG; vch:VC_1312; -.
DR   eggNOG; COG0787; Bacteria.
DR   HOGENOM; CLU_028393_2_2_6; -.
DR   BioCyc; MetaCyc:FY484_RS06640-MONOMER; -.
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; 3.20.20.10; Alanine racemase; 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   NCBIfam; TIGR00492; alr; 1.
DR   PANTHER; PTHR30511; ALANINE RACEMASE; 1.
DR   PANTHER; PTHR30511:SF0; ALANINE RACEMASE, CATABOLIC-RELATED; 1.
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; Alanine racemase C-terminal domain-like; 1.
DR   SUPFAM; SSF51419; PLP-binding barrel; 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 highly 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: Highly 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 highly 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 highly 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 highly 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 highly 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 highly 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
//