RPOB_MYCTU
ID RPOB_MYCTU Reviewed; 1178 AA.
AC P9WGY9; L0T4D5; O08406; P0A680; P47766; Q53424; Q59564; Q9X6Q3; Q9X6U9;
AC Q9XC82; Q9XC83; Q9XC84; Q9XC85;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=DNA-directed RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE Short=RNAP subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01321};
DE AltName: Full=RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE AltName: Full=Transcriptase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
GN Name=rpoB {ECO:0000255|HAMAP-Rule:MF_01321}; OrderedLocusNames=Rv0667;
GN ORFNames=MTCI376.08c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=8031050; DOI=10.1128/aac.38.4.805;
RA Miller L.P., Crawford J.T., Shinnick T.M.;
RT "The rpoB gene of Mycobacterium tuberculosis.";
RL Antimicrob. Agents Chemother. 38:805-811(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-1093.
RC STRAIN=ATCC 25618 / H37Rv;
RA Imboden P., Troller R., Marchesi F., Telenti A., Bodmer T., Cole S.,
RA Schopfer K., Burkart T.;
RT "The rpoB gene of Mycobacterium tuberculosis.";
RL Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 374-517.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=8095569; DOI=10.1016/0140-6736(93)90417-f;
RA Telenti A., Imboden P., Marchesi F., Lowrie D., Cole S.T., Colston J.,
RA Matter L., Schopfer K., Bodmer T.;
RT "Detection of rifampicin-resistance mutations in Mycobacterium
RT tuberculosis.";
RL Lancet 341:647-650(1993).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 424-475, AND VARIANTS RIFAMPICIN
RP RESISTANT.
RX PubMed=10921994; DOI=10.1128/jcm.38.8.3119-3122.2000;
RA Valim A.R.M., Rossetti M.L.R., Ribeiro M.O., Zaha A.;
RT "Mutations in the rpoB gene of multidrug-resistant Mycobacterium
RT tuberculosis isolates from Brazil.";
RL J. Clin. Microbiol. 38:3119-3122(2000).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 436-458.
RX PubMed=8027320; DOI=10.1128/jcm.32.4.1095-1098.1994;
RA Kapur V., Li L.L., Iordanescu S., Hamrick M.R., Wanger A., Kreiswirth B.N.,
RA Musser J.M.;
RT "Characterization by automated DNA sequencing of mutations in the gene
RT (rpoB) encoding the RNA polymerase beta subunit in rifampin-resistant
RT Mycobacterium tuberculosis strains from New York City and Texas.";
RL J. Clin. Microbiol. 32:1095-1098(1994).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [8]
RP INTERACTION WITH CARD AND TRCF, AND MUTAGENESIS OF GLU-138; ILE-147;
RP LYS-148 AND SER-149.
RC STRAIN=Erdman;
RX PubMed=22904282; DOI=10.1128/jb.00879-12;
RA Weiss L.A., Harrison P.G., Nickels B.E., Glickman M.S., Campbell E.A.,
RA Darst S.A., Stallings C.L.;
RT "Interaction of CarD with RNA polymerase mediates Mycobacterium
RT tuberculosis viability, rifampicin resistance, and pathogenesis.";
RL J. Bacteriol. 194:5621-5631(2012).
RN [9]
RP FUNCTION, INTERACTION WITH RBPA, AND SUBUNIT.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=22570422; DOI=10.1093/nar/gks346;
RA Hu Y., Morichaud Z., Chen S., Leonetti J.P., Brodolin K.;
RT "Mycobacterium tuberculosis RbpA protein is a new type of transcriptional
RT activator that stabilizes the sigma A-containing RNA polymerase
RT holoenzyme.";
RL Nucleic Acids Res. 40:6547-6557(2012).
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_01321, ECO:0000269|PubMed:22570422}.
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_01321};
CC -!- SUBUNIT: The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta'
CC and 1 omega subunit. When a sigma factor is associated with the core
CC the holoenzyme is formed, which can initiate transcription. Interacts
CC with CarD, TRCF (Mfd) and RbpA. {ECO:0000255|HAMAP-Rule:MF_01321,
CC ECO:0000269|PubMed:22570422, ECO:0000269|PubMed:22904282}.
CC -!- INTERACTION:
CC P9WGY9; P9WJG3: carD; NbExp=5; IntAct=EBI-6419676, EBI-6421028;
CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC {ECO:0000255|HAMAP-Rule:MF_01321}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CCP43410.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; L27989; AAA21416.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP43410.1; ALT_INIT; Genomic_DNA.
DR EMBL; U12205; AAA20242.2; -; Genomic_DNA.
DR EMBL; L05910; AAB59068.1; -; Genomic_DNA.
DR EMBL; AF143771; AAD29720.1; -; Genomic_DNA.
DR EMBL; AF146567; AAD37379.1; -; Genomic_DNA.
DR EMBL; AF147030; AAD45505.1; -; Genomic_DNA.
DR EMBL; AF147031; AAD45506.1; -; Genomic_DNA.
DR EMBL; AF147033; AAD45507.1; -; Genomic_DNA.
DR EMBL; AF147034; AAD45508.1; -; Genomic_DNA.
DR EMBL; S71246; AAB31207.1; -; Genomic_DNA.
DR PIR; F70535; F70535.
DR RefSeq; NP_215181.1; NC_000962.3.
DR PDB; 4KBJ; X-ray; 2.45 A; A/B=53-439.
DR PDB; 4KBM; X-ray; 2.11 A; A=53-439.
DR PDB; 5UH5; X-ray; 3.75 A; C=1-1178.
DR PDB; 5UH6; X-ray; 3.84 A; C=1-1178.
DR PDB; 5UH8; X-ray; 4.18 A; C=1-1178.
DR PDB; 5UH9; X-ray; 4.40 A; C=1-1178.
DR PDB; 5UHA; X-ray; 3.91 A; C=1-1178.
DR PDB; 5UHB; X-ray; 4.29 A; C=1-1178.
DR PDB; 5UHC; X-ray; 3.80 A; C=1-1178.
DR PDB; 5UHD; X-ray; 4.01 A; C=1-1178.
DR PDB; 5UHE; X-ray; 4.04 A; C=1-1178.
DR PDB; 5UHF; X-ray; 4.34 A; C=1-1178.
DR PDB; 5UHG; X-ray; 3.97 A; C=1-1178.
DR PDB; 5ZX2; X-ray; 2.80 A; C=7-1178.
DR PDB; 5ZX3; X-ray; 2.75 A; C=7-1178.
DR PDB; 6BZO; EM; 3.38 A; C=7-1178.
DR PDB; 6C04; EM; 3.27 A; C=7-1178.
DR PDB; 6C05; EM; 5.15 A; C=7-1178.
DR PDB; 6C06; EM; 5.15 A; C=7-1178.
DR PDB; 6DV9; X-ray; 3.80 A; C=1-1178.
DR PDB; 6DVB; X-ray; 3.80 A; C=1-1178.
DR PDB; 6DVC; X-ray; 3.30 A; C=1-1178.
DR PDB; 6DVD; X-ray; 3.90 A; C=1-1178.
DR PDB; 6DVE; X-ray; 3.81 A; C=1-1178.
DR PDB; 6EDT; EM; -; C=7-1140.
DR PDB; 6EE8; EM; 3.92 A; C=7-1140.
DR PDB; 6EEC; EM; 3.55 A; C=7-1178.
DR PDB; 6FBV; EM; 3.50 A; C=1-1178.
DR PDB; 6JCX; X-ray; 2.90 A; C=7-1178.
DR PDB; 6JCY; X-ray; 3.11 A; C=7-1178.
DR PDB; 6KON; X-ray; 3.00 A; C=7-1178.
DR PDB; 6KOO; X-ray; 2.80 A; C=7-1178.
DR PDB; 6KOP; X-ray; 3.30 A; C=7-1178.
DR PDB; 6KOQ; X-ray; 3.35 A; C=7-1178.
DR PDB; 6M7J; EM; 4.40 A; C=7-1178.
DR PDB; 6TYE; X-ray; 3.79 A; C=1-1178.
DR PDB; 6TYF; X-ray; 3.80 A; C=1-1178.
DR PDB; 6TYG; X-ray; 3.50 A; C=1-1178.
DR PDB; 6VVX; EM; 3.39 A; C=7-1178.
DR PDB; 6VVY; EM; 3.42 A; C=7-1178.
DR PDB; 6VVZ; EM; 3.72 A; C=7-1178.
DR PDB; 6VW0; EM; 3.59 A; C=7-1178.
DR PDB; 7KIF; EM; 2.94 A; C=7-1178.
DR PDB; 7KIM; EM; 3.38 A; C=7-1178.
DR PDB; 7KIN; EM; 2.74 A; C=7-1178.
DR PDB; 7KUF; X-ray; 2.60 A; B=815-829.
DR PDB; 7KUG; X-ray; 1.55 A; B/D=815-829.
DR PDBsum; 4KBJ; -.
DR PDBsum; 4KBM; -.
DR PDBsum; 5UH5; -.
DR PDBsum; 5UH6; -.
DR PDBsum; 5UH8; -.
DR PDBsum; 5UH9; -.
DR PDBsum; 5UHA; -.
DR PDBsum; 5UHB; -.
DR PDBsum; 5UHC; -.
DR PDBsum; 5UHD; -.
DR PDBsum; 5UHE; -.
DR PDBsum; 5UHF; -.
DR PDBsum; 5UHG; -.
DR PDBsum; 5ZX2; -.
DR PDBsum; 5ZX3; -.
DR PDBsum; 6BZO; -.
DR PDBsum; 6C04; -.
DR PDBsum; 6C05; -.
DR PDBsum; 6C06; -.
DR PDBsum; 6DV9; -.
DR PDBsum; 6DVB; -.
DR PDBsum; 6DVC; -.
DR PDBsum; 6DVD; -.
DR PDBsum; 6DVE; -.
DR PDBsum; 6EDT; -.
DR PDBsum; 6EE8; -.
DR PDBsum; 6EEC; -.
DR PDBsum; 6FBV; -.
DR PDBsum; 6JCX; -.
DR PDBsum; 6JCY; -.
DR PDBsum; 6KON; -.
DR PDBsum; 6KOO; -.
DR PDBsum; 6KOP; -.
DR PDBsum; 6KOQ; -.
DR PDBsum; 6M7J; -.
DR PDBsum; 6TYE; -.
DR PDBsum; 6TYF; -.
DR PDBsum; 6TYG; -.
DR PDBsum; 6VVX; -.
DR PDBsum; 6VVY; -.
DR PDBsum; 6VVZ; -.
DR PDBsum; 6VW0; -.
DR PDBsum; 7KIF; -.
DR PDBsum; 7KIM; -.
DR PDBsum; 7KIN; -.
DR PDBsum; 7KUF; -.
DR PDBsum; 7KUG; -.
DR AlphaFoldDB; P9WGY9; -.
DR SASBDB; P9WGY9; -.
DR SMR; P9WGY9; -.
DR IntAct; P9WGY9; 3.
DR STRING; 83332.Rv0667; -.
DR BindingDB; P9WGY9; -.
DR ChEMBL; CHEMBL2006; -.
DR DrugCentral; P9WGY9; -.
DR PaxDb; P9WGY9; -.
DR DNASU; 888164; -.
DR GeneID; 888164; -.
DR KEGG; mtu:Rv0667; -.
DR PATRIC; fig|83332.12.peg.742; -.
DR TubercuList; Rv0667; -.
DR eggNOG; COG0085; Bacteria.
DR OMA; FMTWEGY; -.
DR BRENDA; 2.7.7.6; 3445.
DR Reactome; R-HSA-9639775; Antimicrobial action and antimicrobial resistance in Mtb.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
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:0032549; F:ribonucleoside binding; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR CDD; cd00653; RNA_pol_B_RPB2; 1.
DR Gene3D; 2.30.150.10; -; 1.
DR Gene3D; 2.40.270.10; -; 1.
DR Gene3D; 2.40.50.150; -; 1.
DR Gene3D; 3.90.1110.10; -; 1.
DR HAMAP; MF_01321; RNApol_bact_RpoB; 1.
DR InterPro; IPR042107; DNA-dir_RNA_pol_bsu_ext_1_sf.
DR InterPro; IPR019462; DNA-dir_RNA_pol_bsu_external_1.
DR InterPro; IPR015712; DNA-dir_RNA_pol_su2.
DR InterPro; IPR007120; DNA-dir_RNAP_su2_dom.
DR InterPro; IPR037033; DNA-dir_RNAP_su2_hyb_sf.
DR InterPro; IPR010243; RNA_pol_bsu_bac.
DR InterPro; IPR007121; RNA_pol_bsu_CS.
DR InterPro; IPR007644; RNA_pol_bsu_protrusion.
DR InterPro; IPR007642; RNA_pol_Rpb2_2.
DR InterPro; IPR037034; RNA_pol_Rpb2_2_sf.
DR InterPro; IPR007645; RNA_pol_Rpb2_3.
DR InterPro; IPR007641; RNA_pol_Rpb2_7.
DR InterPro; IPR014724; RNA_pol_RPB2_OB-fold.
DR PANTHER; PTHR20856; PTHR20856; 1.
DR Pfam; PF04563; RNA_pol_Rpb2_1; 1.
DR Pfam; PF04561; RNA_pol_Rpb2_2; 1.
DR Pfam; PF04565; RNA_pol_Rpb2_3; 1.
DR Pfam; PF10385; RNA_pol_Rpb2_45; 1.
DR Pfam; PF00562; RNA_pol_Rpb2_6; 1.
DR Pfam; PF04560; RNA_pol_Rpb2_7; 1.
DR TIGRFAMs; TIGR02013; rpoB; 1.
DR PROSITE; PS01166; RNA_POL_BETA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; DNA-directed RNA polymerase;
KW Nucleotidyltransferase; Reference proteome; Transcription; Transferase.
FT CHAIN 1..1178
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000047927"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 423
FT /note="V -> A (in strain: vr1; rifampicin-resistant)"
FT VARIANT 436
FT /note="L -> P (in strain: vr2; rifampicin-resistant)"
FT VARIANT 437
FT /note="S -> T (in strain: vr3; rifampicin-resistant)"
FT VARIANT 438..441
FT /note="QFMD -> H (in strain: RJ49; rifampicin-resistant)"
FT VARIANT 438
FT /note="Q -> L (in strain: vr4; rifampicin-resistant)"
FT VARIANT 439
FT /note="F -> V (in strain: RJ37; rifampicin-resistant)"
FT VARIANT 440..443
FT /note="Missing (in strain: RJ55; rifampicin-resistant)"
FT VARIANT 441
FT /note="D -> V (in strain: vr3; rifampicin-resistant)"
FT VARIANT 449..452
FT /note="LTHK -> WPQ (in strain: RJ48; rifampicin-resistant)"
FT VARIANT 451
FT /note="H -> D (in strain: vr5; rifampicin-resistant)"
FT VARIANT 451
FT /note="H -> L (in strain: SP28; rifampicin-resistant)"
FT VARIANT 451
FT /note="H -> N (in strain: vr6; rifampicin-resistant)"
FT VARIANT 451
FT /note="H -> P (in strain: vr8; rifampicin-resistant)"
FT VARIANT 451
FT /note="H -> Q (in strain: vr1; rifampicin-resistant)"
FT VARIANT 451
FT /note="H -> R (in strain: vr7; rifampicin-resistant)"
FT VARIANT 456
FT /note="S -> L (in strain: vr11 and RJ37; rifampicin-
FT resistant)"
FT VARIANT 456
FT /note="S -> Q (in strain: vr9; rifampicin-resistant)"
FT VARIANT 456
FT /note="S -> W (in strain: vr10; rifampicin-resistant)"
FT VARIANT 458
FT /note="L -> P (in strain: vr12 and SP22; rifampicin-
FT resistant)"
FT MUTAGEN 138
FT /note="E->R: Weakens interaction with TRCF and CarD."
FT /evidence="ECO:0000269|PubMed:22904282"
FT MUTAGEN 147
FT /note="I->A: Weakens interaction with TRCF and CarD."
FT /evidence="ECO:0000269|PubMed:22904282"
FT MUTAGEN 148
FT /note="K->A: Does not affect association with TRCF, but
FT weakens interaction with CarD."
FT /evidence="ECO:0000269|PubMed:22904282"
FT MUTAGEN 149
FT /note="S->A: Does not affect association with TRCF, but
FT weakens interaction with CarD."
FT /evidence="ECO:0000269|PubMed:22904282"
FT CONFLICT 441
FT /note="D -> E (in Ref. 6; AAB31207)"
FT /evidence="ECO:0000305"
FT CONFLICT 527
FT /note="E -> G (in Ref. 3; AAA20242)"
FT /evidence="ECO:0000305"
FT CONFLICT 639..645
FT /note="GDVVVAE -> ATSSSQ (in Ref. 1; AAA21416 and 3;
FT AAA20242)"
FT /evidence="ECO:0000305"
FT CONFLICT 967..968
FT /note="QP -> HA (in Ref. 1; AAA21416)"
FT /evidence="ECO:0000305"
FT CONFLICT 1174
FT /note="V -> F (in Ref. 1; AAA21416)"
FT /evidence="ECO:0000305"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:5ZX3"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:7KIF"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:6KON"
FT HELIX 54..64
FT /evidence="ECO:0007829|PDB:4KBM"
FT HELIX 68..77
FT /evidence="ECO:0007829|PDB:4KBM"
FT HELIX 85..93
FT /evidence="ECO:0007829|PDB:4KBM"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:6BZO"
FT STRAND 101..112
FT /evidence="ECO:0007829|PDB:4KBM"
FT HELIX 119..124
FT /evidence="ECO:0007829|PDB:4KBM"
FT STRAND 130..141
FT /evidence="ECO:0007829|PDB:4KBM"
FT TURN 142..145
FT /evidence="ECO:0007829|PDB:4KBM"
FT STRAND 146..158
FT /evidence="ECO:0007829|PDB:4KBM"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:7KIM"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:4KBM"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:4KBM"
FT STRAND 178..181
FT /evidence="ECO:0007829|PDB:4KBM"
FT STRAND 183..191
FT /evidence="ECO:0007829|PDB:4KBM"
FT TURN 193..195
FT /evidence="ECO:0007829|PDB:4KBM"
FT STRAND 198..205
FT /evidence="ECO:0007829|PDB:4KBM"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:4KBM"
FT STRAND 212..216
FT /evidence="ECO:0007829|PDB:4KBM"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 222..226
FT /evidence="ECO:0007829|PDB:4KBM"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:6DVC"
FT HELIX 234..240
FT /evidence="ECO:0007829|PDB:4KBM"
FT HELIX 245..252
FT /evidence="ECO:0007829|PDB:4KBM"
FT HELIX 256..264
FT /evidence="ECO:0007829|PDB:4KBM"
FT HELIX 269..281
FT /evidence="ECO:0007829|PDB:4KBM"
FT STRAND 282..285
FT /evidence="ECO:0007829|PDB:5ZX2"
FT HELIX 289..300
FT /evidence="ECO:0007829|PDB:4KBM"
FT TURN 303..305
FT /evidence="ECO:0007829|PDB:4KBM"
FT HELIX 309..320
FT /evidence="ECO:0007829|PDB:4KBM"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:4KBJ"
FT HELIX 335..349
FT /evidence="ECO:0007829|PDB:4KBM"
FT STRAND 353..356
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 362..364
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 370..372
FT /evidence="ECO:0007829|PDB:6DVC"
FT STRAND 375..379
FT /evidence="ECO:0007829|PDB:4KBM"
FT HELIX 381..406
FT /evidence="ECO:0007829|PDB:4KBM"
FT TURN 409..411
FT /evidence="ECO:0007829|PDB:4KBM"
FT HELIX 414..417
FT /evidence="ECO:0007829|PDB:4KBM"
FT HELIX 421..430
FT /evidence="ECO:0007829|PDB:4KBM"
FT STRAND 435..439
FT /evidence="ECO:0007829|PDB:7KIN"
FT HELIX 445..451
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 452..459
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 465..467
FT /evidence="ECO:0007829|PDB:7KIN"
FT HELIX 470..473
FT /evidence="ECO:0007829|PDB:5ZX3"
FT HELIX 477..479
FT /evidence="ECO:0007829|PDB:7KIN"
FT TURN 480..482
FT /evidence="ECO:0007829|PDB:7KIN"
FT TURN 492..496
FT /evidence="ECO:0007829|PDB:5ZX3"
FT STRAND 497..500
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 508..510
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 512..520
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 523..531
FT /evidence="ECO:0007829|PDB:7KIN"
FT HELIX 533..538
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 539..542
FT /evidence="ECO:0007829|PDB:6FBV"
FT STRAND 544..546
FT /evidence="ECO:0007829|PDB:7KIF"
FT STRAND 550..560
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 561..563
FT /evidence="ECO:0007829|PDB:6JCX"
FT STRAND 564..566
FT /evidence="ECO:0007829|PDB:5ZX2"
FT STRAND 567..569
FT /evidence="ECO:0007829|PDB:6JCX"
FT STRAND 570..572
FT /evidence="ECO:0007829|PDB:7KIN"
FT TURN 573..575
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 578..581
FT /evidence="ECO:0007829|PDB:7KIN"
FT TURN 583..586
FT /evidence="ECO:0007829|PDB:7KIN"
FT TURN 589..593
FT /evidence="ECO:0007829|PDB:7KIN"
FT HELIX 597..599
FT /evidence="ECO:0007829|PDB:7KIN"
FT HELIX 602..611
FT /evidence="ECO:0007829|PDB:7KIN"
FT HELIX 612..614
FT /evidence="ECO:0007829|PDB:6KOP"
FT STRAND 618..620
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 625..627
FT /evidence="ECO:0007829|PDB:7KIN"
FT TURN 630..632
FT /evidence="ECO:0007829|PDB:7KIN"
FT HELIX 633..636
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 637..639
FT /evidence="ECO:0007829|PDB:7KIM"
FT STRAND 641..643
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 648..653
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 655..665
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 667..671
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 675..677
FT /evidence="ECO:0007829|PDB:5ZX3"
FT STRAND 681..684
FT /evidence="ECO:0007829|PDB:5ZX3"
FT STRAND 701..703
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 706..709
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 716..722
FT /evidence="ECO:0007829|PDB:7KIN"
FT TURN 727..732
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 735..737
FT /evidence="ECO:0007829|PDB:7KIN"
FT HELIX 740..743
FT /evidence="ECO:0007829|PDB:7KIN"
FT TURN 744..747
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 749..761
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 763..766
FT /evidence="ECO:0007829|PDB:7KIF"
FT STRAND 768..771
FT /evidence="ECO:0007829|PDB:6VVX"
FT HELIX 779..781
FT /evidence="ECO:0007829|PDB:7KIF"
FT STRAND 782..784
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 788..790
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 795..797
FT /evidence="ECO:0007829|PDB:5ZX2"
FT STRAND 801..803
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 805..808
FT /evidence="ECO:0007829|PDB:7KIN"
FT HELIX 811..813
FT /evidence="ECO:0007829|PDB:5ZX3"
FT HELIX 816..825
FT /evidence="ECO:0007829|PDB:7KUG"
FT HELIX 826..828
FT /evidence="ECO:0007829|PDB:7KUG"
FT STRAND 831..834
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 845..854
FT /evidence="ECO:0007829|PDB:7KIN"
FT TURN 855..858
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 865..877
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 884..886
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 888..890
FT /evidence="ECO:0007829|PDB:6KOO"
FT STRAND 893..898
FT /evidence="ECO:0007829|PDB:7KIN"
FT HELIX 901..903
FT /evidence="ECO:0007829|PDB:5ZX3"
FT STRAND 908..910
FT /evidence="ECO:0007829|PDB:7KIF"
FT STRAND 914..916
FT /evidence="ECO:0007829|PDB:7KIN"
FT HELIX 919..921
FT /evidence="ECO:0007829|PDB:5ZX2"
FT TURN 923..925
FT /evidence="ECO:0007829|PDB:7KIN"
FT HELIX 929..942
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 949..951
FT /evidence="ECO:0007829|PDB:7KIN"
FT HELIX 954..956
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 957..959
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 963..966
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 976..978
FT /evidence="ECO:0007829|PDB:7KIN"
FT HELIX 982..990
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 996..998
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 1006..1008
FT /evidence="ECO:0007829|PDB:7KIN"
FT TURN 1013..1015
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 1023..1034
FT /evidence="ECO:0007829|PDB:7KIN"
FT HELIX 1037..1040
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 1042..1046
FT /evidence="ECO:0007829|PDB:5ZX3"
FT STRAND 1051..1053
FT /evidence="ECO:0007829|PDB:7KIN"
FT TURN 1060..1063
FT /evidence="ECO:0007829|PDB:5ZX3"
FT STRAND 1066..1068
FT /evidence="ECO:0007829|PDB:7KIN"
FT HELIX 1070..1079
FT /evidence="ECO:0007829|PDB:7KIN"
FT HELIX 1082..1089
FT /evidence="ECO:0007829|PDB:7KIN"
FT TURN 1090..1094
FT /evidence="ECO:0007829|PDB:7KIN"
FT HELIX 1096..1108
FT /evidence="ECO:0007829|PDB:7KIN"
FT HELIX 1119..1130
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 1136..1138
FT /evidence="ECO:0007829|PDB:7KIN"
FT STRAND 1140..1142
FT /evidence="ECO:0007829|PDB:6KOO"
FT HELIX 1152..1162
FT /evidence="ECO:0007829|PDB:5ZX3"
SQ SEQUENCE 1178 AA; 129865 MW; 3DA88DEC6A7DF661 CRC64;
MLEGCILADS RQSKTAASPS PSRPQSSSNN SVPGAPNRVS FAKLREPLEV PGLLDVQTDS
FEWLIGSPRW RESAAERGDV NPVGGLEEVL YELSPIEDFS GSMSLSFSDP RFDDVKAPVD
ECKDKDMTYA APLFVTAEFI NNNTGEIKSQ TVFMGDFPMM TEKGTFIING TERVVVSQLV
RSPGVYFDET IDKSTDKTLH SVKVIPSRGA WLEFDVDKRD TVGVRIDRKR RQPVTVLLKA
LGWTSEQIVE RFGFSEIMRS TLEKDNTVGT DEALLDIYRK LRPGEPPTKE SAQTLLENLF
FKEKRYDLAR VGRYKVNKKL GLHVGEPITS STLTEEDVVA TIEYLVRLHE GQTTMTVPGG
VEVPVETDDI DHFGNRRLRT VGELIQNQIR VGMSRMERVV RERMTTQDVE AITPQTLINI
RPVVAAIKEF FGTSQLSQFM DQNNPLSGLT HKRRLSALGP GGLSRERAGL EVRDVHPSHY
GRMCPIETPE GPNIGLIGSL SVYARVNPFG FIETPYRKVV DGVVSDEIVY LTADEEDRHV
VAQANSPIDA DGRFVEPRVL VRRKAGEVEY VPSSEVDYMD VSPRQMVSVA TAMIPFLEHD
DANRALMGAN MQRQAVPLVR SEAPLVGTGM ELRAAIDAGD VVVAEESGVI EEVSADYITV
MHDNGTRRTY RMRKFARSNH GTCANQCPIV DAGDRVEAGQ VIADGPCTDD GEMALGKNLL
VAIMPWEGHN YEDAIILSNR LVEEDVLTSI HIEEHEIDAR DTKLGAEEIT RDIPNISDEV
LADLDERGIV RIGAEVRDGD ILVGKVTPKG ETELTPEERL LRAIFGEKAR EVRDTSLKVP
HGESGKVIGI RVFSREDEDE LPAGVNELVR VYVAQKRKIS DGDKLAGRHG NKGVIGKILP
VEDMPFLADG TPVDIILNTH GVPRRMNIGQ ILETHLGWCA HSGWKVDAAK GVPDWAARLP
DELLEAQPNA IVSTPVFDGA QEAELQGLLS CTLPNRDGDV LVDADGKAML FDGRSGEPFP
YPVTVGYMYI MKLHHLVDDK IHARSTGPYS MITQQPLGGK AQFGGQRFGE MECWAMQAYG
AAYTLQELLT IKSDDTVGRV KVYEAIVKGE NIPEPGIPES FKVLLKELQS LCLNVEVLSS
DGAAIELREG EDEDLERAAA NLGINLSRNE SASVEDLA
