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CMPR_SYNE7
ID   CMPR_SYNE7              Reviewed;         323 AA.
AC   Q9F1R2;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=HTH-type transcriptional activator CmpR;
GN   Name=cmpR; OrderedLocusNames=Synpcc7942_1310;
OS   Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS   R2).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX   NCBI_TaxID=1140;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION AS A TRANSCRIPTIONAL
RP   REGULATOR.
RX   PubMed=11222586; DOI=10.1128/jb.183.6.1891-1898.2001;
RA   Omata T., Gohta S., Takahashi Y., Harano Y., Maeda S.;
RT   "Involvement of a CbbR homolog in low CO2-induced activation of the
RT   bicarbonate transporter operon in cyanobacteria.";
RL   J. Bacteriol. 183:1891-1898(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7942 / FACHB-805;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Activates transcription of the cmpABCD operon under carbon
CC       dioxide-limited conditions. {ECO:0000269|PubMed:11222586}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the LysR transcriptional regulatory family.
CC       {ECO:0000305}.
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DR   EMBL; AB047379; BAB18722.1; -; Genomic_DNA.
DR   EMBL; CP000100; ABB57340.1; -; Genomic_DNA.
DR   RefSeq; WP_011242557.1; NC_007604.1.
DR   PDB; 5Z49; X-ray; 2.15 A; A/B=94-323.
DR   PDBsum; 5Z49; -.
DR   AlphaFoldDB; Q9F1R2; -.
DR   SMR; Q9F1R2; -.
DR   STRING; 1140.Synpcc7942_1310; -.
DR   PRIDE; Q9F1R2; -.
DR   EnsemblBacteria; ABB57340; ABB57340; Synpcc7942_1310.
DR   KEGG; syf:Synpcc7942_1310; -.
DR   eggNOG; COG0583; Bacteria.
DR   HOGENOM; CLU_039613_6_1_3; -.
DR   OMA; FLRTYMY; -.
DR   OrthoDB; 750230at2; -.
DR   BioCyc; SYNEL:SYNPCC7942_1310-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR005119; LysR_subst-bd.
DR   InterPro; IPR000847; Tscrpt_reg_HTH_LysR.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF00126; HTH_1; 1.
DR   Pfam; PF03466; LysR_substrate; 1.
DR   PRINTS; PR00039; HTHLYSR.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   PROSITE; PS50931; HTH_LYSR; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; Cytoplasm; DNA-binding; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..323
FT                   /note="HTH-type transcriptional activator CmpR"
FT                   /id="PRO_0000341942"
FT   DOMAIN          4..61
FT                   /note="HTH lysR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00253"
FT   DNA_BIND        21..40
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00253"
FT   REGION          304..323
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   STRAND          94..101
FT                   /evidence="ECO:0007829|PDB:5Z49"
FT   HELIX           102..106
FT                   /evidence="ECO:0007829|PDB:5Z49"
FT   HELIX           109..118
FT                   /evidence="ECO:0007829|PDB:5Z49"
FT   STRAND          122..129
FT                   /evidence="ECO:0007829|PDB:5Z49"
FT   HELIX           131..140
FT                   /evidence="ECO:0007829|PDB:5Z49"
FT   STRAND          144..150
FT                   /evidence="ECO:0007829|PDB:5Z49"
FT   STRAND          153..155
FT                   /evidence="ECO:0007829|PDB:5Z49"
FT   STRAND          157..164
FT                   /evidence="ECO:0007829|PDB:5Z49"
FT   STRAND          167..172
FT                   /evidence="ECO:0007829|PDB:5Z49"
FT   HELIX           176..179
FT                   /evidence="ECO:0007829|PDB:5Z49"
FT   STRAND          181..183
FT                   /evidence="ECO:0007829|PDB:5Z49"
FT   HELIX           185..189
FT                   /evidence="ECO:0007829|PDB:5Z49"
FT   STRAND          193..195
FT                   /evidence="ECO:0007829|PDB:5Z49"
FT   HELIX           201..212
FT                   /evidence="ECO:0007829|PDB:5Z49"
FT   STRAND          219..222
FT                   /evidence="ECO:0007829|PDB:5Z49"
FT   HELIX           226..234
FT                   /evidence="ECO:0007829|PDB:5Z49"
FT   STRAND          239..243
FT                   /evidence="ECO:0007829|PDB:5Z49"
FT   HELIX           244..247
FT                   /evidence="ECO:0007829|PDB:5Z49"
FT   STRAND          256..259
FT                   /evidence="ECO:0007829|PDB:5Z49"
FT   STRAND          269..278
FT                   /evidence="ECO:0007829|PDB:5Z49"
FT   HELIX           282..301
FT                   /evidence="ECO:0007829|PDB:5Z49"
SQ   SEQUENCE   323 AA;  35776 MW;  91932129F43FD004 CRC64;
     MKNLTLHQLK VFEAAARHSS FTRAAEELYL TQPTVSIQVK QLTKAVGLPL FEQIGKRLYL
     TEAGRQLYKT TRQVFEQLEQ LDMTIADLQG MKQGQLRLAV ITTAKYFIPR LIGPFCQRYP
     GINVSLKVTN HEGLINRIND NLDDLYVLSR PPSGFDITVQ PFLDNPLVVV GPASHPLANQ
     RGISLERLAQ EPFILRERGS GTREATEQLF AAHNLNLNVK LDLGSNEAIK QAILGGLGLA
     VLSYHTLTSA GATPELKMFE VEGFPIHRQW HAVYPAGKQL STVAATFLDY LLTESQRIAA
     DIQIPESTTT DPELDAPQPV VGV
 
 
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