CRP_HAEIN
ID CRP_HAEIN Reviewed; 224 AA.
AC P29281;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=cAMP-activated global transcriptional regulator CRP;
DE AltName: Full=Catabolite activator protein;
DE Short=CAP;
DE AltName: Full=cAMP receptor protein;
DE Short=CRP;
DE AltName: Full=cAMP regulatory protein;
GN Name=crp; Synonyms=cap; OrderedLocusNames=HI_0957;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PROBABLE AUTOREGULATION, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=1542653; DOI=10.1073/pnas.89.5.1626;
RA Chandler M.S.;
RT "The gene encoding cAMP receptor protein is required for competence
RT development in Haemophilus influenzae Rd.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:1626-1630(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [3]
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=8226661; DOI=10.1128/jb.175.22.7142-7149.1993;
RA Dorocicz I.R., Williams P.M., Redfield R.J.;
RT "The Haemophilus influenzae adenylate cyclase gene: cloning, sequence, and
RT essential role in competence.";
RL J. Bacteriol. 175:7142-7149(1993).
RN [4]
RP FUNCTION, REGULON, AND INDUCTION.
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=15769466; DOI=10.1016/j.jmb.2005.01.012;
RA Redfield R.J., Cameron A.D., Qian Q., Hinds J., Ali T.R., Kroll J.S.,
RA Langford P.R.;
RT "A novel CRP-dependent regulon controls expression of competence genes in
RT Haemophilus influenzae.";
RL J. Mol. Biol. 347:735-747(2005).
RN [5]
RP DNA-BINDING.
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=18761017; DOI=10.1016/j.jmb.2008.08.027;
RA Cameron A.D., Redfield R.J.;
RT "CRP binding and transcription activation at CRP-S sites.";
RL J. Mol. Biol. 383:313-323(2008).
CC -!- FUNCTION: A global transcription regulator required for bacterial
CC competence. Complexes with cyclic AMP (cAMP) which allosterically
CC activates DNA binding (to consensus sequence 5'-AAATGTGATCTAGATCACATTT-
CC 3') to regulate transcription at 54 promoters (PubMed:15769466). There
CC are 2 consensus subclasses; CRP-N (above) and CRP-S (T6 changed to C
CC and A17 changed to G) which obligatorily also requires Sxy for
CC expression. CRP-S sites bind DNA but do not activate transcription in
CC the absence of Sxy. Probably induces a severe bend in DNA. Probably
CC acts as a negative regulator of its own synthesis as well as for
CC adenylate cyclase (cyaA), which generates cAMP.
CC {ECO:0000269|PubMed:1542653, ECO:0000269|PubMed:15769466}.
CC -!- SUBUNIT: Homodimer, which upon binding cAMP is able to bind DNA
CC (Probable). Binds RNA polymerase subunit RpoA (By similarity).
CC {ECO:0000250, ECO:0000305}.
CC -!- INDUCTION: Constitutively expressed; slightly induced on shifting to
CC starvation media. {ECO:0000269|PubMed:15769466}.
CC -!- DOMAIN: The N-terminal domain binds cAMP and is responsible for
CC homodimerization, while the C-terminal domain binds DNA when cAMP is
CC bound. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Loss of competence, the ability to bind, take-up
CC and integrate exogenous DNA. Loss of the ability to ferment ribose or
CC xylose. {ECO:0000269|PubMed:1542653, ECO:0000269|PubMed:8226661}.
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DR EMBL; M77207; AAA24952.1; -; Genomic_DNA.
DR EMBL; L42023; AAC22618.1; -; Genomic_DNA.
DR PIR; B38225; B38225.
DR RefSeq; NP_439118.1; NC_000907.1.
DR RefSeq; WP_005647998.1; NC_000907.1.
DR AlphaFoldDB; P29281; -.
DR SMR; P29281; -.
DR STRING; 71421.HI_0957; -.
DR EnsemblBacteria; AAC22618; AAC22618; HI_0957.
DR KEGG; hin:HI_0957; -.
DR PATRIC; fig|71421.8.peg.999; -.
DR eggNOG; COG0664; Bacteria.
DR HOGENOM; CLU_075053_3_5_6; -.
DR OMA; VLCRDFG; -.
DR PhylomeDB; P29281; -.
DR BioCyc; HINF71421:G1GJ1-998-MON; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0030552; F:cAMP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0030420; P:establishment of competence for transformation; IEA:UniProtKB-KW.
DR CDD; cd00038; CAP_ED; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 2.60.120.10; -; 1.
DR InterPro; IPR018490; cNMP-bd-like.
DR InterPro; IPR018488; cNMP-bd_CS.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR012318; HTH_CRP.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR018335; Tscrpt_reg_HTH_Crp-type_CS.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF13545; HTH_Crp_2; 1.
DR PRINTS; PR00034; HTHCRP.
DR SMART; SM00100; cNMP; 1.
DR SMART; SM00419; HTH_CRP; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF51206; SSF51206; 1.
DR PROSITE; PS00888; CNMP_BINDING_1; 1.
DR PROSITE; PS00889; CNMP_BINDING_2; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
DR PROSITE; PS00042; HTH_CRP_1; 1.
DR PROSITE; PS51063; HTH_CRP_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; cAMP; cAMP-binding; Competence; DNA-binding;
KW Nucleotide-binding; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..224
FT /note="cAMP-activated global transcriptional regulator CRP"
FT /id="PRO_0000100147"
FT DOMAIN 152..224
FT /note="HTH crp-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00387"
FT DNA_BIND 194..200
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00387"
FT REGION 34..36
FT /note="Activating region 2 (AR2); probably contacts the N-
FT terminus of RpoA"
FT /evidence="ECO:0000250"
FT REGION 67..73
FT /note="Activating region 3 (AR3); probably contacts sigma-
FT 70 (RpoD)"
FT /evidence="ECO:0000250"
FT REGION 168..177
FT /note="Activating region 1 (AR1); probably contacts the C-
FT terminus of RpoA"
FT /evidence="ECO:0000250"
FT BINDING 71..77
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 86..88
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 97..98
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 142..143
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 150..151
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 185..195
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT SITE 111
FT /note="Activating region 2 (AR2); probably contacts the N-
FT terminus of RpoA"
FT /evidence="ECO:0000250"
FT SITE 116
FT /note="Activating region 2 (AR2); probably contacts the N-
FT terminus of RpoA"
FT /evidence="ECO:0000250"
FT MOD_RES 115
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 224 AA; 25152 MW; 421B7790A48FF50C CRC64;
MSNELTEIDE VVTSSQEEAT QRDPVLDWFL THCHLHKYPA KSTLIHAGED ATTLYYVIKG
SVMVSSKDDE GKEMILTYLG AGQFFGEAGL FDEGSKRSAW VKTKTTCEIA EISYKKYRQL
IQANPEILMF LTAQLARRLQ NTSRQVTNLA FLDVAGRIAQ TLMNLAKQPE AMTHPDGMQI
KITRQEIGQM VGCSRETVGR IIKMLEDQNL IHAHGKTIVV YGAR
