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CRP-like cAMP-activated global transcriptional regulator (cAMP receptor protein) (CRP) (cAMP regulatory protein)

 CRPL_MYCTU              Reviewed;         224 AA.
P9WMH3; F2GFB8; L0TDH2; O69644; Q7D534;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
16-APR-2014, sequence version 1.
12-SEP-2018, entry version 27.
RecName: Full=CRP-like cAMP-activated global transcriptional regulator {ECO:0000303|PubMed:16267303};
AltName: Full=cAMP receptor protein {ECO:0000303|PubMed:16267303};
Short=CRP {ECO:0000303|PubMed:16267303};
AltName: Full=cAMP regulatory protein {ECO:0000303|PubMed:16267303};
Name=crp {ECO:0000303|PubMed:16267303}; OrderedLocusNames=Rv3676;
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium; Mycobacterium tuberculosis complex.
NCBI_TaxID=83332;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 25618 / H37Rv;
PubMed=9634230; DOI=10.1038/31159;
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M.,
Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
"Deciphering the biology of Mycobacterium tuberculosis from the
complete genome sequence.";
Nature 393:537-544(1998).
[2]
DNA-BINDING, DNA-BENDING, AND PROBABLE CAMP-BINDING.
STRAIN=ATCC 25618 / H37Rv;
PubMed=16267303; DOI=10.1128/JB.187.22.7795-7804.2005;
Bai G., McCue L.A., McDonough K.A.;
"Characterization of Mycobacterium tuberculosis Rv3676 (CRPMt), a
cyclic AMP receptor protein-like DNA binding protein.";
J. Bacteriol. 187:7795-7804(2005).
[3]
FUNCTION AS A TRANSCRIPTION REGULATOR, DNA-BINDING, AND DISRUPTION
PHENOTYPE.
STRAIN=ATCC 25618 / H37Rv;
PubMed=15882420; DOI=10.1111/j.1365-2958.2005.04609.x;
Rickman L., Scott C., Hunt D.M., Hutchinson T., Menendez M.C.,
Whalan R., Hinds J., Colston M.J., Green J., Buxton R.S.;
"A member of the cAMP receptor protein family of transcription
regulators in Mycobacterium tuberculosis is required for virulence in
mice and controls transcription of the rpfA gene coding for a
resuscitation promoting factor.";
Mol. Microbiol. 56:1274-1286(2005).
[4]
FUNCTION, SUBUNIT, DNA-BINDING, AND CAMP-BINDING.
STRAIN=ATCC 25618 / H37Rv;
PubMed=20028978; DOI=10.1074/jbc.M109.047720;
Stapleton M., Haq I., Hunt D.M., Arnvig K.B., Artymiuk P.J.,
Buxton R.S., Green J.;
"Mycobacterium tuberculosis cAMP receptor protein (Rv3676) differs
from the Escherichia coli paradigm in its cAMP binding and DNA binding
properties and transcription activation properties.";
J. Biol. Chem. 285:7016-7027(2010).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 25618 / H37Rv;
PubMed=21969609; DOI=10.1074/mcp.M111.011627;
Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B.,
Yadav A.K., Shrivastava P., Marimuthu A., Anand S., Sundaram H.,
Kingsbury R., Harsha H.C., Nair B., Prasad T.S., Chauhan D.S.,
Katoch K., Katoch V.M., Kumar P., Chaerkady R., Ramachandran S.,
Dash D., Pandey A.;
"Proteogenomic analysis of Mycobacterium tuberculosis by high
resolution mass spectrometry.";
Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
[6]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF APO-CRP (OFF-STATE), AND
SUBUNIT.
STRAIN=ATCC 25618 / H37Rv;
PubMed=19193643; DOI=10.1074/jbc.C800215200;
Gallagher D.T., Smith N., Kim S.K., Robinson H., Reddy P.T.;
"Profound asymmetry in the structure of the cAMP-free cAMP receptor
protein (CRP) from Mycobacterium tuberculosis.";
J. Biol. Chem. 284:8228-8232(2009).
[7]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH CAMP (ON-STATE)
AND IN COMPLEX WITH A CAMP ANALOG, SUBUNIT, AND CAMP-BINDING.
STRAIN=ATCC 25618 / H37Rv;
PubMed=19740754; DOI=10.1074/jbc.M109.041343;
Reddy M.C., Palaninathan S.K., Bruning J.B., Thurman C., Smith D.,
Sacchettini J.C.;
"Structural insights into the mechanism of the allosteric transitions
of Mycobacterium tuberculosis cAMP receptor protein.";
J. Biol. Chem. 284:36581-36591(2009).
[8]
X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS).
STRAIN=ATCC 25618 / H37Rv;
PubMed=20338852; DOI=10.1016/j.bpj.2009.10.016;
Kumar P., Joshi D.C., Akif M., Akhter Y., Hasnain S.E., Mande S.C.;
"Mapping conformational transitions in cyclic AMP receptor protein:
crystal structure and normal-mode analysis of Mycobacterium
tuberculosis apo-cAMP receptor protein.";
Biophys. J. 98:305-314(2010).
[9]
X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN COMPLEX WITH CAMP AND DNA.
Akhter Y., Pogenberg V., Hasnain S.E., Wilmanns M.;
"Crystal structure of cAMP receptor protein from Mycobacterium
tuberculosis in complex with DNA and cAMP.";
Submitted (MAY-2010) to the PDB data bank.
[10]
STRUCTURE BY NMR.
STRAIN=ATCC 25618 / H37Rv;
PubMed=22074452; DOI=10.1021/ja206967d;
Godoy-Ruiz R., Krejcirikova A., Gallagher D.T., Tugarinov V.;
"Solution NMR evidence for symmetry in functionally or
crystallographically asymmetric homodimers.";
J. Am. Chem. Soc. 133:19578-19581(2011).
-!- FUNCTION: Global transcriptional regulator that complexes with
cAMP and binds to specific DNA promoter sites, causing DNA-
bending, to regulate transcription. cAMP improves binding to
specific DNA sequences, probably by altering protein conformation.
The CRP regulon is predicted to contain about 115 genes. Some
genes are activated by CRP (rpfA, whiB1) while others are
repressed (fadD10). There are 2 CRP-binding sites in the promoter
of whiB1, at low concentrations of CRP with or without cAMP
transcription of whiB1 is enhanced via site CRP1, then repressed
as site CRP2 is filled. {ECO:0000269|PubMed:15882420,
ECO:0000269|PubMed:20028978}.
-!- SUBUNIT: Homodimer; in the absence of cAMP the DNA-binding domains
are asymmetric in one structure; upon cAMP binding the dimer
becomes symmetric, preparing it to bind DNA.
{ECO:0000269|PubMed:19193643, ECO:0000269|PubMed:19740754,
ECO:0000269|PubMed:20028978, ECO:0000269|Ref.9}.
-!- DISRUPTION PHENOTYPE: Grows more slowly in aerobic liquid culture
and on plates, severely impaired growth in unactivated mouse bone
marrow-derived macrophages and in infected mice.
{ECO:0000269|PubMed:15882420}.
-----------------------------------------------------------------------
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EMBL; AL123456; CCP46499.1; -; Genomic_DNA.
PIR; E70790; E70790.
RefSeq; NP_218193.1; NC_000962.3.
RefSeq; WP_003419728.1; NZ_KK339374.1.
PDB; 3D0S; X-ray; 2.00 A; A/B=1-224.
PDB; 3H3U; X-ray; 2.90 A; A/B=1-224.
PDB; 3I54; X-ray; 2.20 A; A/B/C/D=1-224.
PDB; 3I59; X-ray; 2.29 A; A/B=1-224.
PDB; 3MZH; X-ray; 2.90 A; A/B=1-224.
PDBsum; 3D0S; -.
PDBsum; 3H3U; -.
PDBsum; 3I54; -.
PDBsum; 3I59; -.
PDBsum; 3MZH; -.
ProteinModelPortal; P9WMH3; -.
SMR; P9WMH3; -.
STRING; 83332.Rv3676; -.
PaxDb; P9WMH3; -.
EnsemblBacteria; CCP46499; CCP46499; Rv3676.
GeneID; 885502; -.
KEGG; mtu:Rv3676; -.
TubercuList; Rv3676; -.
eggNOG; ENOG4105IJJ; Bacteria.
eggNOG; COG0664; LUCA.
KO; K10914; -.
OMA; TECEVAE; -.
PhylomeDB; P9WMH3; -.
Proteomes; UP000001584; Chromosome.
GO; GO:0005618; C:cell wall; IDA:MTBBASE.
GO; GO:0005886; C:plasma membrane; IDA:MTBBASE.
GO; GO:0030552; F:cAMP binding; IDA:MTBBASE.
GO; GO:0003677; F:DNA binding; IDA:MTBBASE.
GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MTBBASE.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MTBBASE.
GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MTBBASE.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MTBBASE.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd00038; CAP_ED; 1.
Gene3D; 1.10.10.10; -; 1.
Gene3D; 2.60.120.10; -; 1.
InterPro; IPR018490; cNMP-bd-like.
InterPro; IPR000595; cNMP-bd_dom.
InterPro; IPR012318; HTH_CRP.
InterPro; IPR014710; RmlC-like_jellyroll.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR036390; WH_DNA-bd_sf.
Pfam; PF00027; cNMP_binding; 1.
Pfam; PF13545; HTH_Crp_2; 1.
SMART; SM00100; cNMP; 1.
SMART; SM00419; HTH_CRP; 1.
SUPFAM; SSF46785; SSF46785; 1.
SUPFAM; SSF51206; SSF51206; 1.
PROSITE; PS50042; CNMP_BINDING_3; 1.
PROSITE; PS51063; HTH_CRP_2; 1.
1: Evidence at protein level;
3D-structure; Activator; cAMP; cAMP-binding; Complete proteome;
DNA-binding; Nucleotide-binding; Reference proteome; Repressor;
Transcription; Transcription regulation; Virulence.
CHAIN 1 224 CRP-like cAMP-activated global
transcriptional regulator.
/FTId=PRO_0000420402.
DOMAIN 144 217 HTH crp-type. {ECO:0000255|PROSITE-
ProRule:PRU00387}.
NP_BIND 64 70 cAMP 1. {ECO:0000250|UniProtKB:P0ACJ8}.
NP_BIND 79 82 cAMP 1. {ECO:0000269|Ref.9}.
NP_BIND 89 90 cAMP 1. {ECO:0000269|Ref.9}.
NP_BIND 134 135 cAMP 1. {ECO:0000269|Ref.9}.
NP_BIND 142 143 cAMP 2. {ECO:0000250|UniProtKB:P0ACJ8}.
DNA_BIND 177 196 H-T-H motif. {ECO:0000255|PROSITE-
ProRule:PRU00387}.
NP_BIND 178 188 cAMP 2. {ECO:0000250|UniProtKB:P0ACJ8}.
HELIX 2 5 {ECO:0000244|PDB:3D0S}.
HELIX 9 11 {ECO:0000244|PDB:3I54}.
STRAND 12 14 {ECO:0000244|PDB:3MZH}.
HELIX 20 23 {ECO:0000244|PDB:3D0S}.
STRAND 28 31 {ECO:0000244|PDB:3D0S}.
STRAND 36 38 {ECO:0000244|PDB:3D0S}.
STRAND 42 44 {ECO:0000244|PDB:3H3U}.
STRAND 46 53 {ECO:0000244|PDB:3D0S}.
STRAND 55 60 {ECO:0000244|PDB:3D0S}.
STRAND 66 72 {ECO:0000244|PDB:3D0S}.
STRAND 77 79 {ECO:0000244|PDB:3D0S}.
HELIX 81 84 {ECO:0000244|PDB:3D0S}.
STRAND 90 97 {ECO:0000244|PDB:3D0S}.
STRAND 99 105 {ECO:0000244|PDB:3D0S}.
HELIX 106 111 {ECO:0000244|PDB:3D0S}.
HELIX 117 143 {ECO:0000244|PDB:3D0S}.
HELIX 146 161 {ECO:0000244|PDB:3D0S}.
STRAND 162 165 {ECO:0000244|PDB:3D0S}.
STRAND 168 172 {ECO:0000244|PDB:3D0S}.
HELIX 177 184 {ECO:0000244|PDB:3D0S}.
HELIX 188 200 {ECO:0000244|PDB:3D0S}.
STRAND 203 207 {ECO:0000244|PDB:3D0S}.
STRAND 210 214 {ECO:0000244|PDB:3D0S}.
HELIX 216 223 {ECO:0000244|PDB:3D0S}.
SEQUENCE 224 AA; 24791 MW; BAB89A61B64839E3 CRC64;
MDEILARAGI FQGVEPSAIA ALTKQLQPVD FPRGHTVFAE GEPGDRLYII ISGKVKIGRR
APDGRENLLT IMGPSDMFGE LSIFDPGPRT SSATTITEVR AVSMDRDALR SWIADRPEIS
EQLLRVLARR LRRTNNNLAD LIFTDVPGRV AKQLLQLAQR FGTQEGGALR VTHDLTQEEI
AQLVGASRET VNKALADFAH RGWIRLEGKS VLISDSERLA RRAR


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