BAT1_MYCRK
ID BAT1_MYCRK Reviewed; 771 AA.
AC E5AV36;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 1.
DT 25-MAY-2022, entry version 48.
DE RecName: Full=Burkholderia TALE-like protein 1 {ECO:0000303|PubMed:24792163};
DE AltName: Full=Modular DNA-binding domain protein BurrH1 {ECO:0000303|PubMed:24452192};
GN Name=bat1 {ECO:0000303|PubMed:24792163}; OrderedLocusNames=RBRH_01844;
OS Mycetohabitans rhizoxinica (strain DSM 19002 / CIP 109453 / HKI 454)
OS (Paraburkholderia rhizoxinica).
OG Plasmid pBRH01.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Mycetohabitans.
OX NCBI_TaxID=882378;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19002 / CIP 109453 / HKI 454; PLASMID=pBRH01;
RX PubMed=21131495; DOI=10.1128/jb.01318-10;
RA Lackner G., Moebius N., Partida-Martinez L., Hertweck C.;
RT "Complete genome sequence of Burkholderia rhizoxinica, an endosymbiont of
RT Rhizopus microsporus.";
RL J. Bacteriol. 193:783-784(2011).
RN [2]
RP FUNCTION, DOMAIN, BIOTECHNOLOGY, REPEAT, AND DNA-BINDING.
RC STRAIN=DSM 19002 / CIP 109453 / HKI 454;
RX PubMed=24792163; DOI=10.1093/nar/gku329;
RA de Lange O., Wolf C., Dietze J., Elsaesser J., Morbitzer R., Lahaye T.;
RT "Programmable DNA-binding proteins from Burkholderia provide a fresh
RT perspective on the TALE-like repeat domain.";
RL Nucleic Acids Res. 42:7436-7449(2014).
RN [3]
RP BIOTECHNOLOGY, DOMAIN, AND REPEAT.
RX PubMed=24452192; DOI=10.1038/srep03831;
RA Juillerat A., Bertonati C., Dubois G., Guyot V., Thomas S., Valton J.,
RA Beurdeley M., Silva G.H., Daboussi F., Duchateau P.;
RT "BurrH: a new modular DNA binding protein for genome engineering.";
RL Sci. Rep. 4:3831-3831(2014).
RN [4]
RP BIOTECHNOLOGY USES REVIEW.
RX PubMed=24602153; DOI=10.1111/tpj.12431;
RA de Lange O., Binder A., Lahaye T.;
RT "From dead leaf, to new life: TAL effectors as tools for synthetic
RT biology.";
RL Plant J. 78:753-771(2014).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 2-771 ALONE AND IN COMPLEX WITH
RP DNA, FUNCTION, DOMAIN, BIOTECHNOLOGY, AND DNA-BINDING.
RX PubMed=25004980; DOI=10.1107/s1399004714011183;
RA Stella S., Molina R., Lopez-Mendez B., Juillerat A., Bertonati C.,
RA Daboussi F., Campos-Olivas R., Duchateau P., Montoya G.;
RT "BuD, a helix-loop-helix DNA-binding domain for genome modification.";
RL Acta Crystallogr. D 70:2042-2052(2014).
CC -!- FUNCTION: Binds to dsDNA in a sequence-specific manner. Also binds a
CC DNA/RNA duplex when the recognized sequence is in the DNA strand. Each
CC tandem core repeat recognizes a single nucleotide in the target DNA via
CC its base-specifying residue (BSR, residue 13 of each repeat); altering
CC this amino acid changes sequence specificity.
CC {ECO:0000269|PubMed:24792163, ECO:0000269|PubMed:25004980}.
CC -!- DOMAIN: The protein is composed of 20 tandem core repeats (the BuD
CC domain) with 1 base-specifying residue (BSR, residue 13), which
CC recognizes 1 base pair in the target DNA. {ECO:0000269|PubMed:24452192,
CC ECO:0000269|PubMed:24792163, ECO:0000269|PubMed:25004980}.
CC -!- BIOTECHNOLOGY: After addition of nuclear localization signals (NLS) and
CC a transcription activation domain, can be expressed in both human and
CC plant cells and will recognize and transcribe a target sequence; more
CC than 17 core repeats are necessary for this function. The N-terminal
CC cryptic repeats effect activation, while the C-terminal cryptic repeat
CC is absolutely required. When fused to the FokI restriction endonuclease
CC domain functions as a sequence-specific DNA nuclease in vitro (called
CC TALE-nuclease, TALEN, PubMed:24792163 or BuDN, PubMed:25004980) and
CC with an NLS, in human and yeast cells. The latter construct also allows
CC targeted gene insertion. Modification of the core repeat BSR allows
CC recognition of a user-defined DNA sequence, allowing these constructs
CC to target and modify a DNA sequence of interest, and thus be used for
CC genome engineering. Other potential uses as transcriptional repressors,
CC for transposon targeting, DNA methylation or histone tail modifictions
CC are also possible. {ECO:0000269|PubMed:24452192,
CC ECO:0000269|PubMed:24792163, ECO:0000269|PubMed:25004980,
CC ECO:0000303|PubMed:24602153}.
CC -!- SIMILARITY: Belongs to the transcription activator-like effector (TALE)
CC family. Bat subfamily. {ECO:0000303|PubMed:24792163}.
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DR EMBL; FR687360; CBW76960.1; -; Genomic_DNA.
DR RefSeq; WP_013428821.1; NC_014718.1.
DR PDB; 4CJ9; X-ray; 2.21 A; A/B=2-771.
DR PDB; 4CJA; X-ray; 2.65 A; A=2-771.
DR PDBsum; 4CJ9; -.
DR PDBsum; 4CJA; -.
DR AlphaFoldDB; E5AV36; -.
DR SMR; E5AV36; -.
DR STRING; 882378.RBRH_01844; -.
DR EnsemblBacteria; CBW76960; CBW76960; RBRH_01844.
DR KEGG; brh:RBRH_01844; -.
DR eggNOG; COG2201; Bacteria.
DR HOGENOM; CLU_362365_0_0_4; -.
DR OMA; KMAGNIG; -.
DR Proteomes; UP000007437; Plasmid pBRH01.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:UniProtKB.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR005042; TAL_effector_rpt.
DR Pfam; PF03377; TAL_effector; 21.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ANK repeat; DNA-binding; Plasmid; Reference proteome; Repeat.
FT CHAIN 1..771
FT /note="Burkholderia TALE-like protein 1"
FT /id="PRO_0000430623"
FT REPEAT 18..49
FT /note="Cryptic repeat -1"
FT /evidence="ECO:0000303|PubMed:24452192,
FT ECO:0000303|PubMed:24792163"
FT REPEAT 50..82
FT /note="Cryptic repeat 0"
FT /evidence="ECO:0000303|PubMed:24452192,
FT ECO:0000303|PubMed:24792163"
FT REPEAT 83..115
FT /note="Core repeat 1"
FT /evidence="ECO:0000303|PubMed:24452192,
FT ECO:0000303|PubMed:24792163"
FT REPEAT 116..148
FT /note="Core repeat 2"
FT /evidence="ECO:0000303|PubMed:24452192,
FT ECO:0000303|PubMed:24792163"
FT REPEAT 149..181
FT /note="Core repeat 3"
FT /evidence="ECO:0000303|PubMed:24452192,
FT ECO:0000303|PubMed:24792163"
FT REPEAT 182..214
FT /note="Core repeat 4"
FT /evidence="ECO:0000303|PubMed:24452192,
FT ECO:0000303|PubMed:24792163"
FT REPEAT 215..247
FT /note="Core repeat 5"
FT /evidence="ECO:0000303|PubMed:24452192,
FT ECO:0000303|PubMed:24792163"
FT REPEAT 216..245
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 248..280
FT /note="Core repeat 6"
FT /evidence="ECO:0000303|PubMed:24452192,
FT ECO:0000303|PubMed:24792163"
FT REPEAT 281..313
FT /note="Core repeat 7"
FT /evidence="ECO:0000303|PubMed:24452192,
FT ECO:0000303|PubMed:24792163"
FT REPEAT 314..346
FT /note="Core repeat 8"
FT /evidence="ECO:0000303|PubMed:24452192,
FT ECO:0000303|PubMed:24792163"
FT REPEAT 347..379
FT /note="Core repeat 9"
FT /evidence="ECO:0000303|PubMed:24452192,
FT ECO:0000303|PubMed:24792163"
FT REPEAT 348..377
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT REPEAT 380..412
FT /note="Core repeat 10"
FT /evidence="ECO:0000303|PubMed:24452192,
FT ECO:0000303|PubMed:24792163"
FT REPEAT 413..445
FT /note="Core repeat 11"
FT /evidence="ECO:0000303|PubMed:24452192,
FT ECO:0000303|PubMed:24792163"
FT REPEAT 446..478
FT /note="Core repeat 12"
FT /evidence="ECO:0000303|PubMed:24452192,
FT ECO:0000303|PubMed:24792163"
FT REPEAT 479..511
FT /note="Core repeat 13"
FT /evidence="ECO:0000303|PubMed:24452192,
FT ECO:0000303|PubMed:24792163"
FT REPEAT 512..544
FT /note="Core repeat 14"
FT /evidence="ECO:0000303|PubMed:24452192,
FT ECO:0000303|PubMed:24792163"
FT REPEAT 545..577
FT /note="Core repeat 15"
FT /evidence="ECO:0000303|PubMed:24452192,
FT ECO:0000303|PubMed:24792163"
FT REPEAT 578..610
FT /note="Core repeat 16"
FT /evidence="ECO:0000303|PubMed:24452192,
FT ECO:0000303|PubMed:24792163"
FT REPEAT 579..608
FT /note="ANK 3"
FT /evidence="ECO:0000255"
FT REPEAT 611..643
FT /note="Core repeat 17"
FT /evidence="ECO:0000303|PubMed:24452192,
FT ECO:0000303|PubMed:24792163"
FT REPEAT 644..676
FT /note="Core repeat 18"
FT /evidence="ECO:0000303|PubMed:24452192,
FT ECO:0000303|PubMed:24792163"
FT REPEAT 645..674
FT /note="ANK 4"
FT /evidence="ECO:0000255"
FT REPEAT 677..709
FT /note="Core repeat 19"
FT /evidence="ECO:0000303|PubMed:24452192,
FT ECO:0000303|PubMed:24792163"
FT REPEAT 710..741
FT /note="Core repeat 20"
FT /evidence="ECO:0000303|PubMed:24452192,
FT ECO:0000303|PubMed:24792163"
FT REPEAT 742..771
FT /note="Cryptic repeat +1"
FT /evidence="ECO:0000303|PubMed:24792163"
FT REGION 83..709
FT /note="BuD domain"
FT /evidence="ECO:0000303|PubMed:25004980"
FT HELIX 20..27
FT /evidence="ECO:0007829|PDB:4CJ9"
FT HELIX 32..41
FT /evidence="ECO:0007829|PDB:4CJ9"
FT HELIX 43..47
FT /evidence="ECO:0007829|PDB:4CJ9"
FT HELIX 52..58
FT /evidence="ECO:0007829|PDB:4CJ9"
FT HELIX 64..80
FT /evidence="ECO:0007829|PDB:4CJ9"
FT HELIX 85..92
FT /evidence="ECO:0007829|PDB:4CJ9"
FT HELIX 97..113
FT /evidence="ECO:0007829|PDB:4CJ9"
FT HELIX 118..125
FT /evidence="ECO:0007829|PDB:4CJ9"
FT HELIX 130..146
FT /evidence="ECO:0007829|PDB:4CJ9"
FT HELIX 151..158
FT /evidence="ECO:0007829|PDB:4CJ9"
FT TURN 159..162
FT /evidence="ECO:0007829|PDB:4CJ9"
FT HELIX 163..179
FT /evidence="ECO:0007829|PDB:4CJ9"
FT HELIX 184..191
FT /evidence="ECO:0007829|PDB:4CJ9"
FT HELIX 196..213
FT /evidence="ECO:0007829|PDB:4CJ9"
FT HELIX 217..224
FT /evidence="ECO:0007829|PDB:4CJ9"
FT HELIX 229..245
FT /evidence="ECO:0007829|PDB:4CJ9"
FT HELIX 250..257
FT /evidence="ECO:0007829|PDB:4CJ9"
FT HELIX 262..278
FT /evidence="ECO:0007829|PDB:4CJ9"
FT HELIX 283..290
FT /evidence="ECO:0007829|PDB:4CJ9"
FT HELIX 295..310
FT /evidence="ECO:0007829|PDB:4CJ9"
FT TURN 311..313
FT /evidence="ECO:0007829|PDB:4CJ9"
FT HELIX 316..323
FT /evidence="ECO:0007829|PDB:4CJ9"
FT HELIX 328..344
FT /evidence="ECO:0007829|PDB:4CJ9"
FT HELIX 349..356
FT /evidence="ECO:0007829|PDB:4CJ9"
FT HELIX 361..377
FT /evidence="ECO:0007829|PDB:4CJ9"
FT HELIX 382..389
FT /evidence="ECO:0007829|PDB:4CJ9"
FT HELIX 394..411
FT /evidence="ECO:0007829|PDB:4CJ9"
FT HELIX 415..422
FT /evidence="ECO:0007829|PDB:4CJ9"
FT HELIX 427..444
FT /evidence="ECO:0007829|PDB:4CJ9"
FT HELIX 448..455
FT /evidence="ECO:0007829|PDB:4CJ9"
FT HELIX 460..476
FT /evidence="ECO:0007829|PDB:4CJ9"
FT HELIX 481..488
FT /evidence="ECO:0007829|PDB:4CJ9"
FT HELIX 493..509
FT /evidence="ECO:0007829|PDB:4CJ9"
FT HELIX 514..521
FT /evidence="ECO:0007829|PDB:4CJ9"
FT HELIX 526..542
FT /evidence="ECO:0007829|PDB:4CJ9"
FT HELIX 547..554
FT /evidence="ECO:0007829|PDB:4CJ9"
FT HELIX 559..575
FT /evidence="ECO:0007829|PDB:4CJ9"
FT HELIX 580..587
FT /evidence="ECO:0007829|PDB:4CJ9"
FT HELIX 592..608
FT /evidence="ECO:0007829|PDB:4CJ9"
FT HELIX 613..620
FT /evidence="ECO:0007829|PDB:4CJ9"
FT HELIX 625..642
FT /evidence="ECO:0007829|PDB:4CJ9"
FT HELIX 646..653
FT /evidence="ECO:0007829|PDB:4CJ9"
FT HELIX 658..674
FT /evidence="ECO:0007829|PDB:4CJ9"
FT HELIX 679..686
FT /evidence="ECO:0007829|PDB:4CJ9"
FT HELIX 691..708
FT /evidence="ECO:0007829|PDB:4CJ9"
FT HELIX 712..721
FT /evidence="ECO:0007829|PDB:4CJ9"
FT HELIX 723..739
FT /evidence="ECO:0007829|PDB:4CJ9"
FT HELIX 744..751
FT /evidence="ECO:0007829|PDB:4CJ9"
FT HELIX 756..764
FT /evidence="ECO:0007829|PDB:4CJ9"
SQ SEQUENCE 771 AA; 80267 MW; CF969DC0A5463364 CRC64;
MSTAFVDQDK QMANRLNLSP LERSKIEKQY GGATTLAFIS NKQNELAQIL SRADILKIAS
YDCAAHALQA VLDCGPMLGK RGFSQSDIVK IAGNIGGAQA LQAVLDLESM LGKRGFSRDD
IAKMAGNIGG AQTLQAVLDL ESAFRERGFS QADIVKIAGN NGGAQALYSV LDVEPTLGKR
GFSRADIVKI AGNTGGAQAL HTVLDLEPAL GKRGFSRIDI VKIAANNGGA QALHAVLDLG
PTLRECGFSQ ATIAKIAGNI GGAQALQMVL DLGPALGKRG FSQATIAKIA GNIGGAQALQ
TVLDLEPALC ERGFSQATIA KMAGNNGGAQ ALQTVLDLEP ALRKRDFRQA DIIKIAGNDG
GAQALQAVIE HGPTLRQHGF NLADIVKMAG NIGGAQALQA VLDLKPVLDE HGFSQPDIVK
MAGNIGGAQA LQAVLSLGPA LRERGFSQPD IVKIAGNTGG AQALQAVLDL ELTLVEHGFS
QPDIVRITGN RGGAQALQAV LALELTLRER GFSQPDIVKI AGNSGGAQAL QAVLDLELTF
RERGFSQADI VKIAGNDGGT QALHAVLDLE RMLGERGFSR ADIVNVAGNN GGAQALKAVL
EHEATLNERG FSRADIVKIA GNGGGAQALK AVLEHEATLD ERGFSRADIV RIAGNGGGAQ
ALKAVLEHGP TLNERGFNLT DIVEMAANSG GAQALKAVLE HGPTLRQRGL SLIDIVEIAS
NGGAQALKAV LKYGPVLMQA GRSNEEIVHV AARRGGAGRI RKMVAPLLER Q
