RPOC_BACSU
ID RPOC_BACSU Reviewed; 1199 AA.
AC P37871; P70978;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 4.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=DNA-directed RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
DE Short=RNAP subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01322, ECO:0000269|PubMed:18289874};
DE AltName: Full=RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
DE AltName: Full=Transcriptase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
GN Name=rpoC {ECO:0000255|HAMAP-Rule:MF_01322}; Synonyms=lpm, std;
GN OrderedLocusNames=BSU01080;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND STREPTOLYDIGAN RESISTANCE.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=7592585; DOI=10.1074/jbc.270.41.23930;
RA Yang X., Price C.W.;
RT "Streptolydigin resistance can be conferred by alterations to either the
RT beta or beta' subunits of Bacillus subtilis RNA polymerase.";
RL J. Biol. Chem. 270:23930-23933(1995).
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 SEQUENCE REVISION TO 1026; 1173 AND 1176.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-466.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=7657605; DOI=10.1074/jbc.270.35.20329;
RA Boor K.J., Duncan M.L., Price C.W.;
RT "Genetic and transcriptional organization of the region encoding the beta
RT subunit of Bacillus subtilis RNA polymerase.";
RL J. Biol. Chem. 270:20329-20336(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 453-1199.
RC STRAIN=168;
RX PubMed=8969501; DOI=10.1099/13500872-142-11-3039;
RA Yasumoto K., Liu H., Jeong S.M., Ohashi Y., Kakinuma S., Tanaka K.,
RA Kawamura F., Yoshikawa H., Takahashi H.;
RT "Sequence analysis of a 50 kb region between spo0H and rrnH on the Bacillus
RT subtilis chromosome.";
RL Microbiology 142:3039-3046(1996).
RN [6]
RP SUBUNIT.
RC STRAIN=168;
RX PubMed=6802805; DOI=10.1128/jb.150.2.977-980.1982;
RA Achberger E.C., Tahara M., Whiteley H.R.;
RT "Interchangeability of delta subunits of RNA polymerase from different
RT species of the genus Bacillus.";
RL J. Bacteriol. 150:977-980(1982).
RN [7]
RP FUNCTION, AND SUBUNIT.
RC STRAIN=BS200;
RX PubMed=18289874; DOI=10.1016/j.pep.2008.01.006;
RA Yang X., Lewis P.J.;
RT "Overproduction and purification of recombinant Bacillus subtilis RNA
RT polymerase.";
RL Protein Expr. Purif. 59:86-93(2008).
RN [8]
RP SUBUNIT.
RC STRAIN=168;
RX PubMed=21710567; DOI=10.1002/pmic.201000790;
RA Delumeau O., Lecointe F., Muntel J., Guillot A., Guedon E., Monnet V.,
RA Hecker M., Becher D., Polard P., Noirot P.;
RT "The dynamic protein partnership of RNA polymerase in Bacillus subtilis.";
RL Proteomics 11:2992-3001(2011).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC {ECO:0000255|HAMAP-Rule:MF_01322, ECO:0000269|PubMed:18289874}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.6; Evidence={ECO:0000255|HAMAP-Rule:MF_01322,
CC ECO:0000269|PubMed:18289874};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01322};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01322};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01322};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01322};
CC -!- SUBUNIT: RNAP is composed of a core of 2 alpha, a beta and a beta'
CC subunit. The core is associated with a delta subunit, and at least one
CC of epsilon or omega (PubMed:6802805, PubMed:18289874, PubMed:21710567).
CC When a sigma factor is associated with the core the holoenzyme is
CC formed, which can initiate transcription (PubMed:18289874).
CC {ECO:0000255|HAMAP-Rule:MF_01322, ECO:0000269|PubMed:18289874,
CC ECO:0000269|PubMed:21710567, ECO:0000269|PubMed:6802805}.
CC -!- INTERACTION:
CC P37871; C0H3R4: rsoA; NbExp=3; IntAct=EBI-5244361, EBI-15816929;
CC P37871; O31602: spx; NbExp=2; IntAct=EBI-5244361, EBI-5248631;
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000255|HAMAP-Rule:MF_01322}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB59112.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L43593; AAB59112.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AL009126; CAB11884.2; -; Genomic_DNA.
DR EMBL; L24376; AAB00973.1; -; Genomic_DNA.
DR EMBL; D64127; BAA10999.1; -; Genomic_DNA.
DR PIR; G69698; G69698.
DR RefSeq; NP_387989.2; NC_000964.3.
DR RefSeq; WP_004399688.1; NZ_JNCM01000029.1.
DR PDB; 6WVJ; EM; 3.36 A; D=1-1199.
DR PDB; 6WVK; EM; 3.36 A; D=1-1199.
DR PDB; 6ZCA; EM; 4.20 A; Y=1-1199.
DR PDB; 6ZFB; EM; 3.90 A; Y/y=1-1199.
DR PDB; 7CKQ; EM; 4.40 A; D=1-1199.
DR PDB; 7F75; EM; 4.20 A; D=1-1199.
DR PDBsum; 6WVJ; -.
DR PDBsum; 6WVK; -.
DR PDBsum; 6ZCA; -.
DR PDBsum; 6ZFB; -.
DR PDBsum; 7CKQ; -.
DR PDBsum; 7F75; -.
DR AlphaFoldDB; P37871; -.
DR SMR; P37871; -.
DR DIP; DIP-49022N; -.
DR IntAct; P37871; 7.
DR MINT; P37871; -.
DR STRING; 224308.BSU01080; -.
DR jPOST; P37871; -.
DR PaxDb; P37871; -.
DR PRIDE; P37871; -.
DR EnsemblBacteria; CAB11884; CAB11884; BSU_01080.
DR GeneID; 935977; -.
DR KEGG; bsu:BSU01080; -.
DR PATRIC; fig|224308.179.peg.111; -.
DR eggNOG; COG0086; Bacteria.
DR InParanoid; P37871; -.
DR OMA; YRNIRVE; -.
DR PhylomeDB; P37871; -.
DR BioCyc; BSUB:BSU01080-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.274.100; -; 1.
DR Gene3D; 4.10.860.120; -; 1.
DR HAMAP; MF_01322; RNApol_bact_RpoC; 1.
DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR InterPro; IPR012754; DNA-dir_RpoC_beta_prime_bact.
DR InterPro; IPR000722; RNA_pol_asu.
DR InterPro; IPR006592; RNA_pol_N.
DR InterPro; IPR007080; RNA_pol_Rpb1_1.
DR InterPro; IPR007066; RNA_pol_Rpb1_3.
DR InterPro; IPR042102; RNA_pol_Rpb1_3_sf.
DR InterPro; IPR007083; RNA_pol_Rpb1_4.
DR InterPro; IPR007081; RNA_pol_Rpb1_5.
DR InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR InterPro; IPR038120; Rpb1_funnel_sf.
DR PANTHER; PTHR19376; PTHR19376; 1.
DR Pfam; PF04997; RNA_pol_Rpb1_1; 1.
DR Pfam; PF00623; RNA_pol_Rpb1_2; 2.
DR Pfam; PF04983; RNA_pol_Rpb1_3; 1.
DR Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR Pfam; PF04998; RNA_pol_Rpb1_5; 1.
DR SMART; SM00663; RPOLA_N; 1.
DR TIGRFAMs; TIGR02386; rpoC_TIGR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; DNA-directed RNA polymerase;
KW Magnesium; Metal-binding; Nucleotidyltransferase; Reference proteome;
KW Transcription; Transferase; Zinc.
FT CHAIN 1..1199
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000067707"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 449
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 451
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 453
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 818
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 892
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 899
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 902
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT VARIANT 796
FT /note="D -> G (in streptolydigan resistant alleles stl6/
FT stl445)"
FT CONFLICT 781
FT /note="H -> P (in Ref. 5; BAA10999)"
FT /evidence="ECO:0000305"
FT CONFLICT 1026
FT /note="E -> G (in Ref. 5; BAA10999)"
FT /evidence="ECO:0000305"
FT CONFLICT 1173
FT /note="A -> G (in Ref. 5; BAA10999)"
FT /evidence="ECO:0000305"
FT CONFLICT 1176
FT /note="G -> A (in Ref. 5; BAA10999)"
FT /evidence="ECO:0000305"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:6WVJ"
FT HELIX 17..23
FT /evidence="ECO:0007829|PDB:6WVJ"
FT STRAND 24..27
FT /evidence="ECO:0007829|PDB:6WVK"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:6WVJ"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:6WVJ"
FT HELIX 49..52
FT /evidence="ECO:0007829|PDB:6WVJ"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:6WVK"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:6WVJ"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:6WVJ"
FT HELIX 85..89
FT /evidence="ECO:0007829|PDB:6WVJ"
FT STRAND 93..102
FT /evidence="ECO:0007829|PDB:6WVJ"
FT HELIX 104..107
FT /evidence="ECO:0007829|PDB:6WVJ"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:6WVJ"
FT HELIX 113..117
FT /evidence="ECO:0007829|PDB:6WVJ"
FT HELIX 122..129
FT /evidence="ECO:0007829|PDB:6WVJ"
FT STRAND 132..138
FT /evidence="ECO:0007829|PDB:6WVJ"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:6WVJ"
FT HELIX 152..162
FT /evidence="ECO:0007829|PDB:6WVJ"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:6WVK"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:6WVJ"
FT HELIX 173..179
FT /evidence="ECO:0007829|PDB:6WVJ"
FT HELIX 184..194
FT /evidence="ECO:0007829|PDB:6WVJ"
FT TURN 195..197
FT /evidence="ECO:0007829|PDB:6WVK"
FT HELIX 201..218
FT /evidence="ECO:0007829|PDB:6WVJ"
FT HELIX 223..226
FT /evidence="ECO:0007829|PDB:6WVJ"
FT STRAND 227..233
FT /evidence="ECO:0007829|PDB:6WVJ"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:6WVJ"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:6WVJ"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:6WVJ"
FT HELIX 253..274
FT /evidence="ECO:0007829|PDB:6WVJ"
FT HELIX 278..296
FT /evidence="ECO:0007829|PDB:6WVJ"
FT STRAND 300..303
FT /evidence="ECO:0007829|PDB:6WVJ"
FT STRAND 310..312
FT /evidence="ECO:0007829|PDB:6WVJ"
FT HELIX 316..320
FT /evidence="ECO:0007829|PDB:6WVJ"
FT HELIX 326..329
FT /evidence="ECO:0007829|PDB:6WVJ"
FT STRAND 337..346
FT /evidence="ECO:0007829|PDB:6WVJ"
FT STRAND 354..358
FT /evidence="ECO:0007829|PDB:6WVJ"
FT HELIX 359..365
FT /evidence="ECO:0007829|PDB:6WVJ"
FT HELIX 367..376
FT /evidence="ECO:0007829|PDB:6WVJ"
FT STRAND 379..382
FT /evidence="ECO:0007829|PDB:6WVJ"
FT HELIX 383..391
FT /evidence="ECO:0007829|PDB:6WVJ"
FT HELIX 396..404
FT /evidence="ECO:0007829|PDB:6WVJ"
FT STRAND 405..407
FT /evidence="ECO:0007829|PDB:6WVK"
FT STRAND 410..413
FT /evidence="ECO:0007829|PDB:6WVJ"
FT HELIX 420..422
FT /evidence="ECO:0007829|PDB:6WVJ"
FT STRAND 423..438
FT /evidence="ECO:0007829|PDB:6WVJ"
FT HELIX 440..442
FT /evidence="ECO:0007829|PDB:6WVJ"
FT HELIX 443..446
FT /evidence="ECO:0007829|PDB:6WVJ"
FT TURN 450..452
FT /evidence="ECO:0007829|PDB:6WVJ"
FT STRAND 454..458
FT /evidence="ECO:0007829|PDB:6WVJ"
FT HELIX 463..471
FT /evidence="ECO:0007829|PDB:6WVJ"
FT TURN 475..477
FT /evidence="ECO:0007829|PDB:6WVJ"
FT TURN 482..484
FT /evidence="ECO:0007829|PDB:6WVJ"
FT HELIX 494..503
FT /evidence="ECO:0007829|PDB:6WVJ"
FT TURN 510..513
FT /evidence="ECO:0007829|PDB:6WVJ"
FT STRAND 515..518
FT /evidence="ECO:0007829|PDB:6WVJ"
FT HELIX 519..528
FT /evidence="ECO:0007829|PDB:6WVJ"
FT STRAND 538..540
FT /evidence="ECO:0007829|PDB:6WVJ"
FT HELIX 541..543
FT /evidence="ECO:0007829|PDB:6WVJ"
FT TURN 551..555
FT /evidence="ECO:0007829|PDB:6WVJ"
FT STRAND 556..559
FT /evidence="ECO:0007829|PDB:6WVJ"
FT HELIX 564..567
FT /evidence="ECO:0007829|PDB:6WVJ"
FT TURN 568..570
FT /evidence="ECO:0007829|PDB:6WVJ"
FT STRAND 580..582
FT /evidence="ECO:0007829|PDB:6WVK"
FT HELIX 583..587
FT /evidence="ECO:0007829|PDB:6WVJ"
FT HELIX 602..608
FT /evidence="ECO:0007829|PDB:6WVJ"
FT HELIX 617..630
FT /evidence="ECO:0007829|PDB:6WVJ"
FT HELIX 634..654
FT /evidence="ECO:0007829|PDB:6WVJ"
FT HELIX 660..662
FT /evidence="ECO:0007829|PDB:6WVJ"
FT HELIX 669..689
FT /evidence="ECO:0007829|PDB:6WVJ"
FT HELIX 694..719
FT /evidence="ECO:0007829|PDB:6WVJ"
FT HELIX 725..731
FT /evidence="ECO:0007829|PDB:6WVJ"
FT HELIX 738..745
FT /evidence="ECO:0007829|PDB:6WVJ"
FT STRAND 756..758
FT /evidence="ECO:0007829|PDB:6WVJ"
FT TURN 767..769
FT /evidence="ECO:0007829|PDB:6WVJ"
FT HELIX 773..778
FT /evidence="ECO:0007829|PDB:6WVJ"
FT HELIX 781..807
FT /evidence="ECO:0007829|PDB:6WVJ"
FT STRAND 812..816
FT /evidence="ECO:0007829|PDB:6WVK"
FT STRAND 824..826
FT /evidence="ECO:0007829|PDB:6WVJ"
FT STRAND 829..831
FT /evidence="ECO:0007829|PDB:6WVJ"
FT STRAND 834..837
FT /evidence="ECO:0007829|PDB:6WVJ"
FT HELIX 839..843
FT /evidence="ECO:0007829|PDB:6WVJ"
FT STRAND 847..850
FT /evidence="ECO:0007829|PDB:6WVJ"
FT STRAND 852..854
FT /evidence="ECO:0007829|PDB:6WVJ"
FT STRAND 857..862
FT /evidence="ECO:0007829|PDB:6WVJ"
FT STRAND 864..867
FT /evidence="ECO:0007829|PDB:6WVJ"
FT HELIX 870..879
FT /evidence="ECO:0007829|PDB:6WVJ"
FT STRAND 884..886
FT /evidence="ECO:0007829|PDB:6WVJ"
FT HELIX 889..891
FT /evidence="ECO:0007829|PDB:6WVJ"
FT STRAND 895..899
FT /evidence="ECO:0007829|PDB:6WVK"
FT HELIX 900..903
FT /evidence="ECO:0007829|PDB:6WVJ"
FT TURN 907..909
FT /evidence="ECO:0007829|PDB:6WVJ"
FT STRAND 910..912
FT /evidence="ECO:0007829|PDB:6WVJ"
FT HELIX 919..928
FT /evidence="ECO:0007829|PDB:6WVJ"
FT HELIX 929..933
FT /evidence="ECO:0007829|PDB:6WVJ"
FT HELIX 943..945
FT /evidence="ECO:0007829|PDB:6WVK"
FT HELIX 953..960
FT /evidence="ECO:0007829|PDB:6WVJ"
FT STRAND 966..968
FT /evidence="ECO:0007829|PDB:6WVK"
FT STRAND 978..981
FT /evidence="ECO:0007829|PDB:6WVJ"
FT TURN 984..986
FT /evidence="ECO:0007829|PDB:6WVJ"
FT STRAND 990..994
FT /evidence="ECO:0007829|PDB:6WVJ"
FT STRAND 999..1003
FT /evidence="ECO:0007829|PDB:6WVJ"
FT STRAND 1025..1028
FT /evidence="ECO:0007829|PDB:6WVJ"
FT HELIX 1031..1037
FT /evidence="ECO:0007829|PDB:6WVJ"
FT HELIX 1040..1058
FT /evidence="ECO:0007829|PDB:6WVJ"
FT HELIX 1064..1072
FT /evidence="ECO:0007829|PDB:6WVJ"
FT STRAND 1077..1082
FT /evidence="ECO:0007829|PDB:6WVJ"
FT STRAND 1086..1088
FT /evidence="ECO:0007829|PDB:6WVJ"
FT STRAND 1093..1095
FT /evidence="ECO:0007829|PDB:6WVJ"
FT HELIX 1096..1106
FT /evidence="ECO:0007829|PDB:6WVJ"
FT STRAND 1109..1111
FT /evidence="ECO:0007829|PDB:6WVJ"
FT STRAND 1115..1118
FT /evidence="ECO:0007829|PDB:6WVJ"
FT HELIX 1123..1127
FT /evidence="ECO:0007829|PDB:6WVJ"
FT HELIX 1134..1137
FT /evidence="ECO:0007829|PDB:6WVJ"
FT HELIX 1142..1152
FT /evidence="ECO:0007829|PDB:6WVJ"
FT STRAND 1155..1157
FT /evidence="ECO:0007829|PDB:6WVJ"
FT HELIX 1161..1167
FT /evidence="ECO:0007829|PDB:6WVJ"
FT HELIX 1174..1176
FT /evidence="ECO:0007829|PDB:6WVJ"
FT HELIX 1178..1181
FT /evidence="ECO:0007829|PDB:6WVJ"
SQ SEQUENCE 1199 AA; 134252 MW; 33263510698FC12B CRC64;
MLDVNNFEYM NIGLASPDKI RSWSFGEVKK PETINYRTLK PEKDGLFCER IFGPTKDWEC
HCGKYKRVRY KGVVCDRCGV EVTRAKVRRE RMGHIELAAP VSHIWYFKGI PSRMGLVLDM
SPRALEEVIY FASYVVTDPA NTPLEKKQLL SEKEYRAYLD KYGNKFQASM GAEAIHKLLQ
DIDLVKEVDM LKEELKTSQG QRRTRAIKRL EVLEAFRNSG NKPSWMILDV LPVIPPELRP
MVQLDGGRFA TSDLNDLYRR VINRNNRLKR LLDLGAPSII VQNEKRMLQE AVDALIDNGR
RGRPVTGPGN RPLKSLSHML KGKQGRFRQN LLGKRVDYSG RSVIVVGPHL KMYQCGLPKE
MALELFKPFV MKELVEKGLA HNIKSAKRKI ERVQPEVWDV LESVIKEHPV LLNRAPTLHR
LGIQAFEPTL VEGRAIRLHP LVCTAYNADF DGDQMAVHVP LSAEAQAEAR ILMLAAQNIL
NPKDGKPVVT PSQDMVLGNY YLTLERAGAV GEGMVFKNTD EALLAYQNGY VHLHTRVAVA
ANSLKNVTFT EEQRSKLLIT TVGKLVFNEI LPESFPYMNE PTKSNIEEKT PDRFFLEKGA
DVKAVIAQQP INAPFKKGIL GKIIAEIFKR FHITETSKML DRMKNLGFKY STKAGITVGV
SDIVVLDDKQ EILEEAQSKV DNVMKQFRRG LITEEERYER VISIWSAAKD VIQGKLMKSL
DELNPIYMMS DSGARGNASN FTQLAGMRGL MANPAGRIIE LPIKSSFREG LTVLEYFIST
HGARKGLADT ALKTADSGYL TRRLVDVAQD VIIRETDCGT DRGILAKPLK EGTETIERLE
ERLIGRFARK QVKHPETGEV LVNENELIDE DKALEIVEAG IEEVWIRSAF TCNTPHGVCK
RCYGRNLATG SDVEVGEAVG IIAAQSIGEP GTQLTMRTFH TGGVAGDDIT QGLPRIQELF
EARNPKGQAT ITEIDGTVVE INEVRDKQQE IVVQGAVETR SYTAPYNSRL KVAEGDKITR
GQVLTEGSID PKELLKVTDL TTVQEYLLHE VQKVYRMQGV EIGDKHVEVM VRQMLRKVRV
IDAGDTDVLP GTLLDIHQFT EANKKVLLEG NRPATGRPVL LGITKASLET DSFLSAASFQ
ETTRVLTDAA IKGKRDELLG LKENVIIGKL VPAGTGMMKY RKVKPVSNVQ PTDDMVPVE