RPOB_MYCS2
ID RPOB_MYCS2 Reviewed; 1169 AA.
AC P60281; A0QS65; I7G3Q0;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2004, sequence version 1.
DT 03-AUG-2022, entry version 115.
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};
GN OrderedLocusNames=MSMEG_1367, MSMEI_1328;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Subramaniyan K., Gopalakrishnakone P.;
RT "Investigation of drug resistance in Mycobacterium smegmatis using
RT differential gene expression analysis by microarray technology.";
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [5]
RP PROTEIN SEQUENCE OF 200-210; 371-381 AND 1149-1159, FUNCTION, INTERACTION
RP WITH RBPA, SUBUNIT, ANTIBIOTIC RESISTANCE, AND MUTAGENESIS OF ASP-432 AND
RP SER-447.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=19926651; DOI=10.1099/mic.0.033670-0;
RA Dey A., Verma A.K., Chatterji D.;
RT "Role of an RNA polymerase interacting protein, MsRbpA, from Mycobacterium
RT smegmatis in phenotypic tolerance to rifampicin.";
RL Microbiology 156:873-883(2010).
RN [6]
RP ANTIBIOTIC RESISTANCE, AND MUTAGENESIS OF GLN-429; ASP-432; HIS-442;
RP ARG-445; SER-447 AND LEU-449.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17698424; DOI=10.1016/j.dnarep.2007.06.009;
RA Jain R., Kumar P., Varshney U.;
RT "A distinct role of formamidopyrimidine DNA glycosylase (MutM) in down-
RT regulation of accumulation of G, C mutations and protection against
RT oxidative stress in mycobacteria.";
RL DNA Repair 6:1774-1785(2007).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC This subunit often mutates to generate rifampicin (Rif) resistance.
CC Interaction with RbpA partially restores Rif-inhibited transcription;
CC once the subunit is Rif-resistant however RbpA no longer stimulates
CC transcription. {ECO:0000255|HAMAP-Rule:MF_01321,
CC ECO:0000269|PubMed:19926651}.
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 RbpA, which partially restores Rif-inhibited transcription.
CC {ECO:0000255|HAMAP-Rule:MF_01321, ECO:0000269|PubMed:19926651}.
CC -!- INTERACTION:
CC P60281; A0R561: carD; NbExp=2; IntAct=EBI-2408357, EBI-2408339;
CC -!- MISCELLANEOUS: Mutations in the RRDR sequence (residues 423-449) confer
CC rifampicin (Rif) resistance. Rif blocks transcription inititiation but
CC not elongation.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC {ECO:0000255|HAMAP-Rule:MF_01321}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AFP37801.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ605718; CAE53837.1; -; Genomic_DNA.
DR EMBL; CP000480; ABK70312.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP37801.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_011727628.1; NZ_SIJM01000030.1.
DR RefSeq; YP_885753.1; NC_008596.1.
DR PDB; 5TW1; X-ray; 2.76 A; C=1-1169.
DR PDB; 5VI5; X-ray; 3.20 A; C=1-1169.
DR PDB; 5VI8; X-ray; 2.76 A; C=1-1169.
DR PDB; 6CCE; X-ray; 3.05 A; C=1-1169.
DR PDB; 6CCV; X-ray; 3.05 A; C=1-1169.
DR PDB; 6DCF; X-ray; 3.45 A; C=1-1169.
DR PDB; 6EYD; EM; 4.20 A; C=2-1169.
DR PDB; 6F6W; EM; 3.80 A; C=2-1169.
DR PDB; 6VVS; X-ray; 3.11 A; C=1-1169.
DR PDB; 6VVT; X-ray; 2.90 A; C=1-1169.
DR PDB; 6VVV; X-ray; 3.20 A; C=1-1169.
DR PDB; 6YXU; EM; 3.08 A; C=1-1169.
DR PDB; 6YYS; EM; 3.08 A; C=1-1169.
DR PDB; 6Z11; EM; 3.36 A; C=1-1169.
DR PDB; 7P5X; EM; 3.20 A; AC=1-1169.
DR PDBsum; 5TW1; -.
DR PDBsum; 5VI5; -.
DR PDBsum; 5VI8; -.
DR PDBsum; 6CCE; -.
DR PDBsum; 6CCV; -.
DR PDBsum; 6DCF; -.
DR PDBsum; 6EYD; -.
DR PDBsum; 6F6W; -.
DR PDBsum; 6VVS; -.
DR PDBsum; 6VVT; -.
DR PDBsum; 6VVV; -.
DR PDBsum; 6YXU; -.
DR PDBsum; 6YYS; -.
DR PDBsum; 6Z11; -.
DR PDBsum; 7P5X; -.
DR AlphaFoldDB; P60281; -.
DR SMR; P60281; -.
DR IntAct; P60281; 2.
DR STRING; 246196.MSMEI_1328; -.
DR PRIDE; P60281; -.
DR EnsemblBacteria; ABK70312; ABK70312; MSMEG_1367.
DR EnsemblBacteria; AFP37801; AFP37801; MSMEI_1328.
DR GeneID; 66732827; -.
DR KEGG; msg:MSMEI_1328; -.
DR KEGG; msm:MSMEG_1367; -.
DR PATRIC; fig|246196.19.peg.1351; -.
DR eggNOG; COG0085; Bacteria.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR BRENDA; 2.7.7.6; 3512.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; 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: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; Direct protein sequencing;
KW DNA-directed RNA polymerase; Nucleotidyltransferase; Reference proteome;
KW Transcription; Transferase.
FT CHAIN 1..1169
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000047926"
FT MUTAGEN 429
FT /note="Q->K,L: Rifampicin (Rif) resistant."
FT /evidence="ECO:0000269|PubMed:17698424"
FT MUTAGEN 432
FT /note="D->V: Rifampicin (Rif) resistant."
FT /evidence="ECO:0000269|PubMed:17698424,
FT ECO:0000269|PubMed:19926651"
FT MUTAGEN 432
FT /note="D->Y: Rifampicin (Rif) resistant; RbpA no longer
FT rescues transcription in the presence of Rif. Decreased
FT affinity for Rif, no change in affinity for RbpA."
FT /evidence="ECO:0000269|PubMed:17698424,
FT ECO:0000269|PubMed:19926651"
FT MUTAGEN 442
FT /note="H->D,L,P,R,Y: Rifampicin (Rif) resistant."
FT /evidence="ECO:0000269|PubMed:17698424"
FT MUTAGEN 445
FT /note="R->L,P: Rifampicin (Rif) resistant."
FT /evidence="ECO:0000269|PubMed:17698424"
FT MUTAGEN 447
FT /note="S->L,P,W: Rifampicin (Rif) resistant; RbpA no longer
FT rescues transcription in the presence of Rif, decreased
FT affinity for Rif, no change in affinity for RbpA; tested in
FT the Leu mutation."
FT /evidence="ECO:0000269|PubMed:17698424,
FT ECO:0000269|PubMed:19926651"
FT MUTAGEN 449
FT /note="L->P: Rifampicin (Rif) resistant."
FT /evidence="ECO:0000269|PubMed:17698424"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:6CCE"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:5TW1"
FT HELIX 46..56
FT /evidence="ECO:0007829|PDB:5TW1"
FT HELIX 59..67
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:6DCF"
FT HELIX 76..84
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:6CCV"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:6DCF"
FT STRAND 93..103
FT /evidence="ECO:0007829|PDB:5TW1"
FT HELIX 110..116
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 121..132
FT /evidence="ECO:0007829|PDB:5TW1"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 138..149
FT /evidence="ECO:0007829|PDB:5TW1"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:6YYS"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 162..166
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 168..172
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 174..178
FT /evidence="ECO:0007829|PDB:5TW1"
FT TURN 184..186
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 209..212
FT /evidence="ECO:0007829|PDB:6Z11"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:6YYS"
FT STRAND 216..219
FT /evidence="ECO:0007829|PDB:6CCE"
FT HELIX 225..229
FT /evidence="ECO:0007829|PDB:5TW1"
FT TURN 230..233
FT /evidence="ECO:0007829|PDB:5TW1"
FT HELIX 236..243
FT /evidence="ECO:0007829|PDB:5TW1"
FT HELIX 247..255
FT /evidence="ECO:0007829|PDB:5TW1"
FT HELIX 261..272
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:6Z11"
FT HELIX 280..290
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:6Z11"
FT TURN 294..296
FT /evidence="ECO:0007829|PDB:5TW1"
FT HELIX 301..310
FT /evidence="ECO:0007829|PDB:5TW1"
FT TURN 312..316
FT /evidence="ECO:0007829|PDB:5VI5"
FT HELIX 326..340
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 344..346
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 349..351
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 353..355
FT /evidence="ECO:0007829|PDB:6YYS"
FT STRAND 361..363
FT /evidence="ECO:0007829|PDB:6CCE"
FT HELIX 364..366
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 367..370
FT /evidence="ECO:0007829|PDB:5TW1"
FT HELIX 372..397
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 400..402
FT /evidence="ECO:0007829|PDB:5VI5"
FT HELIX 405..408
FT /evidence="ECO:0007829|PDB:5TW1"
FT HELIX 412..422
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 426..430
FT /evidence="ECO:0007829|PDB:5TW1"
FT HELIX 436..442
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 445..448
FT /evidence="ECO:0007829|PDB:5TW1"
FT TURN 456..458
FT /evidence="ECO:0007829|PDB:5TW1"
FT HELIX 461..464
FT /evidence="ECO:0007829|PDB:5TW1"
FT HELIX 468..470
FT /evidence="ECO:0007829|PDB:5TW1"
FT TURN 471..473
FT /evidence="ECO:0007829|PDB:5TW1"
FT HELIX 476..478
FT /evidence="ECO:0007829|PDB:6DCF"
FT TURN 483..487
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 488..491
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 499..501
FT /evidence="ECO:0007829|PDB:6VVT"
FT STRAND 503..511
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 514..522
FT /evidence="ECO:0007829|PDB:5TW1"
FT HELIX 524..527
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 541..543
FT /evidence="ECO:0007829|PDB:6CCE"
FT STRAND 544..546
FT /evidence="ECO:0007829|PDB:6Z11"
FT STRAND 547..553
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 555..557
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 559..563
FT /evidence="ECO:0007829|PDB:5TW1"
FT HELIX 564..566
FT /evidence="ECO:0007829|PDB:5VI8"
FT STRAND 569..573
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 576..578
FT /evidence="ECO:0007829|PDB:5TW1"
FT HELIX 582..584
FT /evidence="ECO:0007829|PDB:5TW1"
FT HELIX 588..590
FT /evidence="ECO:0007829|PDB:5TW1"
FT HELIX 593..603
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 609..611
FT /evidence="ECO:0007829|PDB:6YXU"
FT STRAND 616..618
FT /evidence="ECO:0007829|PDB:5TW1"
FT HELIX 622..627
FT /evidence="ECO:0007829|PDB:5TW1"
FT TURN 628..630
FT /evidence="ECO:0007829|PDB:6Z11"
FT STRAND 632..634
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 639..644
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 646..653
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 658..662
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 666..668
FT /evidence="ECO:0007829|PDB:6VVT"
FT STRAND 672..675
FT /evidence="ECO:0007829|PDB:6VVT"
FT STRAND 692..695
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 697..700
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 707..713
FT /evidence="ECO:0007829|PDB:5TW1"
FT TURN 718..720
FT /evidence="ECO:0007829|PDB:5TW1"
FT HELIX 722..724
FT /evidence="ECO:0007829|PDB:6Z11"
FT STRAND 726..729
FT /evidence="ECO:0007829|PDB:5TW1"
FT HELIX 731..734
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 740..753
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 754..757
FT /evidence="ECO:0007829|PDB:6VVT"
FT STRAND 759..762
FT /evidence="ECO:0007829|PDB:5VI5"
FT HELIX 771..774
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 779..781
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 786..788
FT /evidence="ECO:0007829|PDB:6YYS"
FT STRAND 792..794
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 796..799
FT /evidence="ECO:0007829|PDB:5TW1"
FT HELIX 807..816
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 822..825
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 836..849
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 856..868
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 875..878
FT /evidence="ECO:0007829|PDB:5TW1"
FT TURN 879..881
FT /evidence="ECO:0007829|PDB:6YXU"
FT STRAND 883..890
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 892..895
FT /evidence="ECO:0007829|PDB:6VVT"
FT STRAND 905..908
FT /evidence="ECO:0007829|PDB:5TW1"
FT HELIX 912..915
FT /evidence="ECO:0007829|PDB:5TW1"
FT HELIX 920..933
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 940..942
FT /evidence="ECO:0007829|PDB:5TW1"
FT HELIX 946..949
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 954..957
FT /evidence="ECO:0007829|PDB:6VVT"
FT STRAND 962..964
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 967..969
FT /evidence="ECO:0007829|PDB:5TW1"
FT HELIX 973..980
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 986..989
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 997..999
FT /evidence="ECO:0007829|PDB:5TW1"
FT TURN 1004..1006
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 1014..1025
FT /evidence="ECO:0007829|PDB:5TW1"
FT HELIX 1028..1031
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 1033..1037
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 1040..1044
FT /evidence="ECO:0007829|PDB:5TW1"
FT TURN 1051..1054
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 1057..1059
FT /evidence="ECO:0007829|PDB:5TW1"
FT HELIX 1061..1070
FT /evidence="ECO:0007829|PDB:5TW1"
FT HELIX 1073..1080
FT /evidence="ECO:0007829|PDB:5TW1"
FT TURN 1081..1085
FT /evidence="ECO:0007829|PDB:5TW1"
FT HELIX 1087..1098
FT /evidence="ECO:0007829|PDB:5TW1"
FT HELIX 1110..1120
FT /evidence="ECO:0007829|PDB:5TW1"
FT TURN 1121..1123
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 1127..1129
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 1131..1136
FT /evidence="ECO:0007829|PDB:5TW1"
FT STRAND 1138..1140
FT /evidence="ECO:0007829|PDB:5VI5"
SQ SEQUENCE 1169 AA; 128531 MW; D17F0E28A863FE15 CRC64;
MLEGCILAVS SQSKSNAITN NSVPGAPNRV SFAKLREPLE VPGLLDVQTD SFEWLVGSDR
WRQAAIDRGE ENPVGGLEEV LAELSPIEDF SGSMSLSFSD PRFDEVKASV DECKDKDMTY
AAPLFVTAEF INNNTGEIKS QTVFMGDFPM MTEKGTFIIN GTERVVVSQL VRSPGVYFDE
TIDKSTEKTL HSVKVIPGRG AWLEFDVDKR DTVGVRIDRK RRQPVTVLLK ALGWTNEQIV
ERFGFSEIMM GTLEKDTTSG TDEALLDIYR KLRPGEPPTK ESAQTLLENL FFKEKRYDLA
RVGRYKVNKK LGLNAGKPIT SSTLTEEDVV ATIEYLVRLH EGQTSMTVPG GVEVPVEVDD
IDHFGNRRLR TVGELIQNQI RVGLSRMERV VRERMTTQDV EAITPQTLIN IRPVVAAIKE
FFGTSQLSQF MDQNNPLSGL THKRRLSALG PGGLSRERAG LEVRDVHPSH YGRMCPIETP
EGPNIGLIGS LSVYARVNPF GFIETPYRKV ENGVVTDQID YLTADEEDRH VVAQANSPTD
ENGRFTEDRV MVRKKGGEVE FVSADQVDYM DVSPRQMVSV ATAMIPFLEH DDANRALMGA
NMQRQAVPLV RSEAPLVGTG MELRAAIDAG DVVVADKTGV IEEVSADYIT VMADDGTRQS
YRLRKFARSN HGTCANQRPI VDAGQRVEAG QVIADGPCTQ NGEMALGKNL LVAIMPWEGH
NYEDAIILSN RLVEEDVLTS IHIEEHEIDA RDTKLGAEEI TRDIPNVSDE VLADLDERGI
VRIGAEVRDG DILVGKVTPK GETELTPEER LLRAIFGEKA REVRDTSLKV PHGESGKVIG
IRVFSREDDD ELPAGVNELV RVYVAQKRKI SDGDKLAGRH GNKGVIGKIL PVEDMPFLPD
GTPVDIILNT HGVPRRMNIG QILETHLGWV AKAGWNIDVA AGVPDWASKL PEELYSAPAD
STVATPVFDG AQEGELAGLL GSTLPNRDGE VMVDADGKST LFDGRSGEPF PYPVTVGYMY
ILKLHHLVDD KIHARSTGPY SMITQQPLGG KAQFGGQRFG EMECWAMQAY GAAYTLQELL
TIKSDDTVGR VKVYEAIVKG ENIPEPGIPE SFKVLLKELQ SLCLNVEVLS SDGAAIEMRD
GDDEDLERAA ANLGINLSRN ESASVEDLA