MCCA_WOLSU
ID MCCA_WOLSU Reviewed; 702 AA.
AC Q7MSJ8;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Dissimilatory sulfite reductase MccA {ECO:0000305};
DE EC=1.8.99.- {ECO:0000269|PubMed:22040142, ECO:0000269|PubMed:25642962};
DE Flags: Precursor;
GN Name=mccA {ECO:0000303|PubMed:22040142, ECO:0000303|PubMed:25642962};
GN OrderedLocusNames=WS0379 {ECO:0000312|EMBL:CAE09526.1};
OS Wolinella succinogenes (strain ATCC 29543 / DSM 1740 / LMG 7466 / NCTC
OS 11488 / FDC 602W) (Vibrio succinogenes).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Wolinella.
OX NCBI_TaxID=273121 {ECO:0000312|Proteomes:UP000000422};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29543 / DSM 1740 / CCUG 13145 / JCM 31913 / LMG 7466 / NCTC
RC 11488 / FDC 602W {ECO:0000312|Proteomes:UP000000422};
RX PubMed=14500908; DOI=10.1073/pnas.1932838100;
RA Baar C., Eppinger M., Raddatz G., Simon J., Lanz C., Klimmek O.,
RA Nandakumar R., Gross R., Rosinus A., Keller H., Jagtap P., Linke B.,
RA Meyer F., Lederer H., Schuster S.C.;
RT "Complete genome sequence and analysis of Wolinella succinogenes.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:11690-11695(2003).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, COFACTOR, SUBUNIT, SIGNAL PEPTIDE, AND
RP SUBCELLULAR LOCATION.
RX PubMed=17501927; DOI=10.1111/j.1365-2958.2007.05712.x;
RA Hartshorne R.S., Kern M., Meyer B., Clarke T.A., Karas M., Richardson D.J.,
RA Simon J.;
RT "A dedicated haem lyase is required for the maturation of a novel bacterial
RT cytochrome c with unconventional covalent haem binding.";
RL Mol. Microbiol. 64:1049-1060(2007).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, INDUCTION BY SULFITE, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF CYS-574; ALA-587; CYS-590 AND HIS-591.
RX PubMed=22040142; DOI=10.1111/j.1365-2958.2011.07906.x;
RA Kern M., Klotz M.G., Simon J.;
RT "The Wolinella succinogenes mcc gene cluster encodes an unconventional
RT respiratory sulphite reduction system.";
RL Mol. Microbiol. 82:1515-1530(2011).
RN [4] {ECO:0007744|PDB:4RKM, ECO:0007744|PDB:4RKN}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH HEME; HYDROGEN
RP SULFITE AND COPPER IONS, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP COFACTOR, AND SUBUNIT.
RX PubMed=25642962; DOI=10.1038/nature14109;
RA Hermann B., Kern M., La Pietra L., Simon J., Einsle O.;
RT "The octahaem MccA is a haem c-copper sulfite reductase.";
RL Nature 520:706-709(2015).
CC -!- FUNCTION: Respiratory sulfite reductase that catalyzes the reduction of
CC sulfite to sulfide in a single step, consuming six electrons in the
CC process (PubMed:22040142, PubMed:25642962). Required for sulfite
CC respiration under anaerobic growth conditions (PubMed:22040142). Has
CC only marginal activity with nitrite. {ECO:0000269|PubMed:22040142,
CC ECO:0000269|PubMed:25642962}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-disulfide + 2 A + 3 H2O + hydrogen sulfide =
CC [protein]-dithiol + 2 AH2 + H(+) + sulfite; Xref=Rhea:RHEA:51676,
CC Rhea:RHEA-COMP:10593, Rhea:RHEA-COMP:10594, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17359,
CC ChEBI:CHEBI:17499, ChEBI:CHEBI:29919, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:50058; Evidence={ECO:0000269|PubMed:22040142,
CC ECO:0000269|PubMed:25642962};
CC -!- COFACTOR:
CC Name=Cu(+); Xref=ChEBI:CHEBI:49552;
CC Evidence={ECO:0000269|PubMed:25642962};
CC Note=Exposure to oxygen reduces copper binding and leads to the
CC formation of a disulfide bond between the two Cys residues that bind
CC the copper ion. {ECO:0000269|PubMed:25642962};
CC -!- COFACTOR:
CC Name=heme c; Xref=ChEBI:CHEBI:61717;
CC Evidence={ECO:0000269|PubMed:17501927, ECO:0000269|PubMed:22040142,
CC ECO:0000269|PubMed:25642962};
CC Note=Binds 8 heme c groups covalently per monomer.
CC {ECO:0000269|PubMed:17501927, ECO:0000269|PubMed:25642962};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=44 uM for sulfite {ECO:0000269|PubMed:25642962};
CC Vmax=151 umol/min/mg enzyme with sulfite as substrate
CC {ECO:0000269|PubMed:25642962};
CC -!- PATHWAY: Sulfur metabolism; sulfite reduction. {ECO:0000305}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:17501927,
CC ECO:0000269|PubMed:25642962}.
CC -!- INTERACTION:
CC Q7MSJ8; Q7MSJ8: mccA; NbExp=2; IntAct=EBI-16140995, EBI-16140995;
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:17501927}.
CC -!- INDUCTION: Repressed by fumarate and nitrate. Up-regulated by sulfite,
CC but only in the absence of fumarate and nitrate (at protein level).
CC {ECO:0000269|PubMed:22040142}.
CC -!- DISRUPTION PHENOTYPE: Loss of growth based on sulfite respiration.
CC {ECO:0000269|PubMed:22040142}.
CC -!- MISCELLANEOUS: The eighth heme binding site has an unusual CXXXXXCH
CC motif. {ECO:0000269|PubMed:25642962}.
CC -!- SIMILARITY: Belongs to the multiheme cytochrome c family.
CC {ECO:0000305}.
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DR EMBL; BX571658; CAE09526.1; -; Genomic_DNA.
DR PDB; 4RKM; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J/K/L=1-702.
DR PDB; 4RKN; X-ray; 2.10 A; A/B/C/D=1-702.
DR PDBsum; 4RKM; -.
DR PDBsum; 4RKN; -.
DR AlphaFoldDB; Q7MSJ8; -.
DR SMR; Q7MSJ8; -.
DR DIP; DIP-61512N; -.
DR STRING; 273121.WS0379; -.
DR EnsemblBacteria; CAE09526; CAE09526; WS0379.
DR KEGG; wsu:WS0379; -.
DR eggNOG; COG0484; Bacteria.
DR HOGENOM; CLU_406457_0_0_7; -.
DR OMA; CHPAQYE; -.
DR BioCyc; MetaCyc:MON-20223; -.
DR BRENDA; 1.8.99.5; 6642.
DR SABIO-RK; Q7MSJ8; -.
DR UniPathway; UPA00370; -.
DR Proteomes; UP000000422; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:1903136; F:cuprous ion binding; IDA:UniProtKB.
DR GO; GO:0020037; F:heme binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016667; F:oxidoreductase activity, acting on a sulfur group of donors; IDA:UniProtKB.
DR GO; GO:0016002; F:sulfite reductase activity; IDA:UniProtKB.
DR GO; GO:0009061; P:anaerobic respiration; IEA:UniProtKB-KW.
DR GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IDA:UniProtKB.
DR GO; GO:0070207; P:protein homotrimerization; IDA:UniProtKB.
DR HAMAP; MF_02023; Sulfite_red; 1.
DR InterPro; IPR036280; Multihaem_cyt_sf.
DR InterPro; IPR032897; Sulfite_reductase.
DR SUPFAM; SSF48695; SSF48695; 1.
DR PROSITE; PS51008; MULTIHEME_CYTC; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Copper; Electron transport; Heme; Iron; Metal-binding;
KW Oxidoreductase; Periplasm; Reference proteome; Signal; Sulfate respiration;
KW Transport.
FT SIGNAL 1..39
FT /evidence="ECO:0000269|PubMed:17501927"
FT CHAIN 40..702
FT /note="Dissimilatory sulfite reductase MccA"
FT /id="PRO_0000432940"
FT BINDING 155
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0007744|PDB:4RKN"
FT BINDING 158
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0007744|PDB:4RKN"
FT BINDING 159
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0007744|PDB:4RKN"
FT BINDING 171
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="4"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0007744|PDB:4RKN"
FT BINDING 220
FT /ligand="substrate"
FT /evidence="ECO:0007744|PDB:4RKN"
FT BINDING 297
FT /ligand="substrate"
FT /evidence="ECO:0007744|PDB:4RKN"
FT BINDING 314
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000305"
FT BINDING 317
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0007744|PDB:4RKN"
FT BINDING 318
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0007744|PDB:4RKN"
FT BINDING 351
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0007744|PDB:4RKN"
FT BINDING 354
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0007744|PDB:4RKN"
FT BINDING 355
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0007744|PDB:4RKN"
FT BINDING 360
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0007744|PDB:4RKN"
FT BINDING 372
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0007744|PDB:4RKN"
FT BINDING 375
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0007744|PDB:4RKN"
FT BINDING 376
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="4"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0007744|PDB:4RKN"
FT BINDING 378
FT /ligand="substrate"
FT /evidence="ECO:0007744|PDB:4RKN"
FT BINDING 411
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /evidence="ECO:0000269|PubMed:25642962,
FT ECO:0007744|PDB:4RKM"
FT BINDING 423
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="6"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0007744|PDB:4RKN"
FT BINDING 430
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="5"
FT /note="covalent"
FT /evidence="ECO:0007744|PDB:4RKN"
FT BINDING 433
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="5"
FT /note="covalent"
FT /evidence="ECO:0007744|PDB:4RKN"
FT BINDING 434
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="5"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0007744|PDB:4RKN"
FT BINDING 437
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0007744|PDB:4RKN"
FT BINDING 474
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="6"
FT /note="covalent"
FT /evidence="ECO:0007744|PDB:4RKN"
FT BINDING 477
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="6"
FT /note="covalent"
FT /evidence="ECO:0007744|PDB:4RKN"
FT BINDING 478
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="6"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0007744|PDB:4RKN"
FT BINDING 491
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="8"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0007744|PDB:4RKN"
FT BINDING 496
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="7"
FT /note="covalent"
FT /evidence="ECO:0007744|PDB:4RKN"
FT BINDING 499
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="7"
FT /note="covalent"
FT /evidence="ECO:0007744|PDB:4RKN"
FT BINDING 500
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="7"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0007744|PDB:4RKN"
FT BINDING 507
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /evidence="ECO:0000269|PubMed:25642962,
FT ECO:0007744|PDB:4RKM"
FT BINDING 528
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="5"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0007744|PDB:4RKN"
FT BINDING 574
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="8"
FT /note="covalent"
FT /evidence="ECO:0007744|PDB:4RKN"
FT BINDING 590
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="8"
FT /note="covalent"
FT /evidence="ECO:0007744|PDB:4RKN"
FT BINDING 591
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="8"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0007744|PDB:4RKN"
FT BINDING 675
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="7"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0007744|PDB:4RKN"
FT MUTAGEN 574
FT /note="C->A: Impairs protein stability and abolishes
FT sulfite reductase activity; when associated with C-587."
FT /evidence="ECO:0000269|PubMed:22040142"
FT MUTAGEN 587
FT /note="A->C: Impairs protein stability and abolishes
FT sulfite reductase activity; when associated with A-574."
FT /evidence="ECO:0000269|PubMed:22040142"
FT MUTAGEN 587
FT /note="A->S: No effect on protein stability and sulfite
FT reductase activity."
FT /evidence="ECO:0000269|PubMed:22040142"
FT MUTAGEN 590
FT /note="C->A,S: Impairs protein stability."
FT /evidence="ECO:0000269|PubMed:22040142"
FT MUTAGEN 591
FT /note="H->A: Impairs protein stability."
FT /evidence="ECO:0000269|PubMed:22040142"
FT HELIX 47..54
FT /evidence="ECO:0007829|PDB:4RKN"
FT HELIX 60..63
FT /evidence="ECO:0007829|PDB:4RKN"
FT HELIX 68..74
FT /evidence="ECO:0007829|PDB:4RKN"
FT HELIX 76..85
FT /evidence="ECO:0007829|PDB:4RKN"
FT HELIX 87..90
FT /evidence="ECO:0007829|PDB:4RKN"
FT TURN 91..94
FT /evidence="ECO:0007829|PDB:4RKN"
FT STRAND 96..102
FT /evidence="ECO:0007829|PDB:4RKN"
FT HELIX 105..108
FT /evidence="ECO:0007829|PDB:4RKN"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:4RKN"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:4RKN"
FT HELIX 115..121
FT /evidence="ECO:0007829|PDB:4RKN"
FT HELIX 124..127
FT /evidence="ECO:0007829|PDB:4RKN"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:4RKN"
FT HELIX 152..158
FT /evidence="ECO:0007829|PDB:4RKN"
FT HELIX 160..167
FT /evidence="ECO:0007829|PDB:4RKN"
FT HELIX 170..173
FT /evidence="ECO:0007829|PDB:4RKN"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:4RKN"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:4RKN"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:4RKN"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:4RKN"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:4RKN"
FT STRAND 210..215
FT /evidence="ECO:0007829|PDB:4RKN"
FT STRAND 219..225
FT /evidence="ECO:0007829|PDB:4RKN"
FT STRAND 233..238
FT /evidence="ECO:0007829|PDB:4RKN"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:4RKN"
FT STRAND 245..250
FT /evidence="ECO:0007829|PDB:4RKN"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:4RKN"
FT HELIX 256..260
FT /evidence="ECO:0007829|PDB:4RKN"
FT HELIX 264..273
FT /evidence="ECO:0007829|PDB:4RKN"
FT HELIX 281..287
FT /evidence="ECO:0007829|PDB:4RKN"
FT STRAND 297..300
FT /evidence="ECO:0007829|PDB:4RKN"
FT TURN 301..303
FT /evidence="ECO:0007829|PDB:4RKN"
FT STRAND 304..307
FT /evidence="ECO:0007829|PDB:4RKN"
FT HELIX 310..312
FT /evidence="ECO:0007829|PDB:4RKN"
FT HELIX 314..317
FT /evidence="ECO:0007829|PDB:4RKN"
FT STRAND 320..322
FT /evidence="ECO:0007829|PDB:4RKN"
FT HELIX 327..333
FT /evidence="ECO:0007829|PDB:4RKN"
FT HELIX 337..342
FT /evidence="ECO:0007829|PDB:4RKN"
FT STRAND 344..349
FT /evidence="ECO:0007829|PDB:4RKN"
FT HELIX 351..355
FT /evidence="ECO:0007829|PDB:4RKN"
FT TURN 357..360
FT /evidence="ECO:0007829|PDB:4RKN"
FT HELIX 373..376
FT /evidence="ECO:0007829|PDB:4RKN"
FT STRAND 379..381
FT /evidence="ECO:0007829|PDB:4RKN"
FT HELIX 383..387
FT /evidence="ECO:0007829|PDB:4RKN"
FT HELIX 390..392
FT /evidence="ECO:0007829|PDB:4RKN"
FT HELIX 396..399
FT /evidence="ECO:0007829|PDB:4RKN"
FT STRAND 400..402
FT /evidence="ECO:0007829|PDB:4RKN"
FT STRAND 408..410
FT /evidence="ECO:0007829|PDB:4RKN"
FT HELIX 414..419
FT /evidence="ECO:0007829|PDB:4RKN"
FT HELIX 422..425
FT /evidence="ECO:0007829|PDB:4RKN"
FT HELIX 430..433
FT /evidence="ECO:0007829|PDB:4RKN"
FT HELIX 459..462
FT /evidence="ECO:0007829|PDB:4RKN"
FT HELIX 474..477
FT /evidence="ECO:0007829|PDB:4RKN"
FT HELIX 479..485
FT /evidence="ECO:0007829|PDB:4RKN"
FT STRAND 487..489
FT /evidence="ECO:0007829|PDB:4RKN"
FT TURN 490..493
FT /evidence="ECO:0007829|PDB:4RKN"
FT HELIX 496..500
FT /evidence="ECO:0007829|PDB:4RKN"
FT STRAND 505..508
FT /evidence="ECO:0007829|PDB:4RKN"
FT HELIX 511..513
FT /evidence="ECO:0007829|PDB:4RKN"
FT HELIX 516..518
FT /evidence="ECO:0007829|PDB:4RKN"
FT STRAND 540..542
FT /evidence="ECO:0007829|PDB:4RKN"
FT HELIX 570..575
FT /evidence="ECO:0007829|PDB:4RKN"
FT HELIX 582..586
FT /evidence="ECO:0007829|PDB:4RKN"
FT TURN 587..591
FT /evidence="ECO:0007829|PDB:4RKN"
FT TURN 593..595
FT /evidence="ECO:0007829|PDB:4RKN"
FT HELIX 600..602
FT /evidence="ECO:0007829|PDB:4RKN"
FT HELIX 607..638
FT /evidence="ECO:0007829|PDB:4RKN"
FT STRAND 642..644
FT /evidence="ECO:0007829|PDB:4RKN"
FT HELIX 646..669
FT /evidence="ECO:0007829|PDB:4RKN"
FT TURN 672..675
FT /evidence="ECO:0007829|PDB:4RKN"
FT HELIX 677..700
FT /evidence="ECO:0007829|PDB:4RKN"
SQ SEQUENCE 702 AA; 78939 MW; 7F03B02298162E28 CRC64;
MLSGWSVLKG GNMKYWDKAL LSLFMCVSTL SIAATHAVAM EGMQMTKEAR EIIAHPKGTK
ESRGVISLQD YIVEEQAMYD WLFKNHPIFT KYGGKTVGKL VVKDRGEEWI EEGRGNDFSK
ASKRSGGEGF SSMMYRVARN STLQYPNKFI GPEKCGECHP AQYETWSRSR HATTIRFPGE
HPEVNNKLND PVFDKDTASI LPQGITPDVV YCTVGHIRTK FGFFDAWLLR GTYHVEGGLL
KNGTGQIVAG GNQWQRTWAL NLSPEVAKKI KKWVPDFPVT LEEYGDNGGY VRGLASYAAK
YKKSMSFQAS TSYCEVCHPW KFDFKNESEF YAALGNAKEL QKHTISKGVS CEECHGAGGH
LEGGSGLLIS NCERCHQRFS YSPDLMRNNP LNAGKPDLAL SSKFKSMGPG CGSEGSQTYF
TAHYEKGMRC ATCHDPHDVT GNVTGEKGIK GVSYNSEQGY LSSLYSKPKL KKECTDCHKE
QAYIQSKADT HSKNSCASCH MPFMMSCENF YAIQFQDQAG FDTQRRAHIW KIDVDPARKS
LVAGSTSKDP RDGKDWHFER NEEGRNFVDL MWACARTTWA DKDQAEAKGC HSPVVSELKE
TLHFKDQKQV YNEVMGWQTP VKDKFTQVKV GIQGLYSLLE VKKLAPSDKT RVYELIEKAQ
DTVDLIEKDG SWGMHGFKYT KQRLDAAVEY INEAQRIMKK SL
