BLAI_MYCTU
ID BLAI_MYCTU Reviewed; 138 AA.
AC P9WMJ5; L0T7V6; P95163; Q7D7W9;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 33.
DE RecName: Full=Transcriptional regulator BlaI;
GN Name=blaI; OrderedLocusNames=Rv1846c;
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 [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 [2]
RP IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA Raman K., Yeturu K., Chandra N.;
RT "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT through an interactome, reactome and genome-scale structural analysis.";
RL BMC Syst. Biol. 2:109-109(2008).
RN [3]
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 [4]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), FUNCTION, SUBUNIT, INDUCTION, AND
RP DNA-BINDING.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=19154333; DOI=10.1111/j.1365-2958.2008.06583.x;
RA Sala C., Haouz A., Saul F.A., Miras I., Rosenkrands I., Alzari P.M.,
RA Cole S.T.;
RT "Genome-wide regulon and crystal structure of BlaI (Rv1846c) from
RT Mycobacterium tuberculosis.";
RL Mol. Microbiol. 71:1102-1116(2009).
CC -!- FUNCTION: Transcription regulator that binds to an inverted DNA repeat
CC with the consensus sequence 5'-TAC[GT]AC-NNNNN-GT[AC]GTA-3' and
CC regulates genes involved in antibiotic transport, detoxification and
CC cell wall function. Also regulates its own transcription. Binds DNA as
CC a dimer. {ECO:0000269|PubMed:19154333}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19154333}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Autoregulated. Up-regulated by amoxicillin.
CC {ECO:0000269|PubMed:19154333}.
CC -!- PTM: Upon exposure to beta-lactams, proteolytic cleavage at a single
CC site may impair dimerization and abolish repressor activity.
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC -!- SIMILARITY: Belongs to the BlaI transcriptional regulatory family.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP44612.1; -; Genomic_DNA.
DR PIR; F70664; F70664.
DR RefSeq; NP_216362.1; NC_000962.3.
DR RefSeq; WP_003409301.1; NZ_NVQJ01000013.1.
DR PDB; 2G9W; X-ray; 1.80 A; A/B=1-138.
DR PDBsum; 2G9W; -.
DR AlphaFoldDB; P9WMJ5; -.
DR SMR; P9WMJ5; -.
DR STRING; 83332.Rv1846c; -.
DR PaxDb; P9WMJ5; -.
DR GeneID; 45425819; -.
DR GeneID; 885747; -.
DR KEGG; mtu:Rv1846c; -.
DR TubercuList; Rv1846c; -.
DR eggNOG; COG3682; Bacteria.
DR OMA; MDHLWST; -.
DR PhylomeDB; P9WMJ5; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IDA:MTBBASE.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MTBBASE.
DR GO; GO:0046677; P:response to antibiotic; IEP:MTBBASE.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR005650; BlaI_family.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR34134; PTHR34134; 1.
DR Pfam; PF03965; Penicillinase_R; 1.
DR PIRSF; PIRSF019455; CopR_AtkY; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; Cytoplasm; DNA-binding;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..138
FT /note="Transcriptional regulator BlaI"
FT /id="PRO_0000371419"
FT DNA_BIND 6..71
FT /note="H-T-H motif"
FT REGION 74..138
FT /note="Important for dimerization"
FT /evidence="ECO:0000250"
FT SITE 102..103
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT HELIX 4..6
FT /evidence="ECO:0007829|PDB:2G9W"
FT HELIX 9..19
FT /evidence="ECO:0007829|PDB:2G9W"
FT HELIX 27..34
FT /evidence="ECO:0007829|PDB:2G9W"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:2G9W"
FT HELIX 42..54
FT /evidence="ECO:0007829|PDB:2G9W"
FT STRAND 57..61
FT /evidence="ECO:0007829|PDB:2G9W"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:2G9W"
FT HELIX 75..87
FT /evidence="ECO:0007829|PDB:2G9W"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:2G9W"
FT HELIX 93..106
FT /evidence="ECO:0007829|PDB:2G9W"
FT HELIX 109..123
FT /evidence="ECO:0007829|PDB:2G9W"
SQ SEQUENCE 138 AA; 15211 MW; 86F073B72F3CBD98 CRC64;
MAKLTRLGDL ERAVMDHLWS RTEPQTVRQV HEALSARRDL AYTTVMTVLQ RLAKKNLVLQ
IRDDRAHRYA PVHGRDELVA GLMVDALAQA EDSGSRQAAL VHFVERVGAD EADALRRALA
ELEAGHGNRP PAGAATET
