ID NTCA_SYNE7 Reviewed; 222 AA. AC P29283; Q31S10; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-1992, sequence version 1. DT 27-MAR-2024, entry version 132. DE RecName: Full=Global nitrogen regulator; GN Name=ntcA; OrderedLocusNames=Synpcc7942_0127; OS Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805) OS (Anacystis nidulans R2). OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae; OC Synechococcus. OX NCBI_TaxID=1140; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1630321; DOI=10.1111/j.1365-2958.1992.tb01357.x; RA Vega-Palas M.A., Flores E., Herrero A.; RT "NtcA, a global nitrogen regulator from the cyanobacterium Synechococcus RT that belongs to the Crp family of bacterial regulators."; RL Mol. Microbiol. 6:1853-1859(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33912 / 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., Golden S., 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: Required for full expression of proteins subject to ammonium CC repression. Transcriptional activator of genes subject to nitrogen CC control. CC -!- INTERACTION: CC P29283; Q7X386: Synpcc7942_2061; NbExp=3; IntAct=EBI-15870797, EBI-700982; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X60197; CAA42755.1; -; Genomic_DNA. DR EMBL; CP000100; ABB56159.1; -; Genomic_DNA. DR PIR; S25244; S25244. DR PDB; 2XGX; X-ray; 2.85 A; A/B=1-222. DR PDB; 2XHK; X-ray; 2.30 A; A/B=1-222. DR PDB; 2XKO; X-ray; 2.25 A; A/B=1-222. DR PDB; 2XKP; X-ray; 3.05 A; A/B/C/D/E/F=1-222. DR PDBsum; 2XGX; -. DR PDBsum; 2XHK; -. DR PDBsum; 2XKO; -. DR PDBsum; 2XKP; -. DR AlphaFoldDB; P29283; -. DR SMR; P29283; -. DR DIP; DIP-59550N; -. DR IntAct; P29283; 1. DR STRING; 1140.Synpcc7942_0127; -. DR PaxDb; 1140-Synpcc7942_0127; -. DR KEGG; syf:Synpcc7942_0127; -. DR eggNOG; COG0664; Bacteria. DR HOGENOM; CLU_075053_3_2_3; -. DR OrthoDB; 9810708at2; -. DR BioCyc; SYNEL:NTCA; -. DR EvolutionaryTrace; P29283; -. DR Proteomes; UP000889800; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro. DR CDD; cd00038; CAP_ED; 1. DR CDD; cd00092; HTH_CRP; 1. DR Gene3D; 2.60.120.10; Jelly Rolls; 1. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1. DR InterPro; IPR000595; cNMP-bd_dom. DR InterPro; IPR018490; cNMP-bd_dom_sf. DR InterPro; IPR012318; HTH_CRP. DR InterPro; IPR014710; RmlC-like_jellyroll. DR InterPro; IPR018335; Tscrpt_reg_HTH_Crp-type_CS. DR InterPro; IPR022299; Tscrpt_reg_NtcA. DR InterPro; IPR036388; WH-like_DNA-bd_sf. DR InterPro; IPR036390; WH_DNA-bd_sf. DR NCBIfam; TIGR03697; NtcA_cyano; 1. DR PANTHER; PTHR24567; CRP FAMILY TRANSCRIPTIONAL REGULATORY PROTEIN; 1. DR PANTHER; PTHR24567:SF74; REGULATORY PROTEIN CYSR HOMOLOG; 1. 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; SSF51206; cAMP-binding domain-like; 1. DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 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 3D-structure; Activator; DNA-binding; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1..222 FT /note="Global nitrogen regulator" FT /id="PRO_0000100186" FT DOMAIN 142..215 FT /note="HTH crp-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00387" FT DNA_BIND 175..194 FT /note="H-T-H motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00387" FT BINDING 6..128 FT /ligand="a nucleoside 3',5'-cyclic phosphate" FT /ligand_id="ChEBI:CHEBI:58464" FT HELIX 12..15 FT /evidence="ECO:0007829|PDB:2XKO" FT STRAND 18..20 FT /evidence="ECO:0007829|PDB:2XKO" FT STRAND 23..27 FT /evidence="ECO:0007829|PDB:2XKO" FT STRAND 32..34 FT /evidence="ECO:0007829|PDB:2XKO" FT STRAND 42..49 FT /evidence="ECO:0007829|PDB:2XKO" FT STRAND 51..56 FT /evidence="ECO:0007829|PDB:2XKO" FT STRAND 58..60 FT /evidence="ECO:0007829|PDB:2XKP" FT STRAND 62..68 FT /evidence="ECO:0007829|PDB:2XKO" FT STRAND 72..74 FT /evidence="ECO:0007829|PDB:2XKP" FT HELIX 78..81 FT /evidence="ECO:0007829|PDB:2XKO" FT HELIX 82..84 FT /evidence="ECO:0007829|PDB:2XKO" FT STRAND 89..95 FT /evidence="ECO:0007829|PDB:2XKO" FT STRAND 97..103 FT /evidence="ECO:0007829|PDB:2XKO" FT HELIX 104..106 FT /evidence="ECO:0007829|PDB:2XKO" FT HELIX 107..113 FT /evidence="ECO:0007829|PDB:2XKO" FT HELIX 116..140 FT /evidence="ECO:0007829|PDB:2XKO" FT HELIX 144..159 FT /evidence="ECO:0007829|PDB:2XKO" FT STRAND 160..163 FT /evidence="ECO:0007829|PDB:2XKO" FT STRAND 166..171 FT /evidence="ECO:0007829|PDB:2XKO" FT HELIX 175..182 FT /evidence="ECO:0007829|PDB:2XKO" FT HELIX 186..198 FT /evidence="ECO:0007829|PDB:2XKO" FT STRAND 201..205 FT /evidence="ECO:0007829|PDB:2XKO" FT STRAND 208..212 FT /evidence="ECO:0007829|PDB:2XKO" FT HELIX 214..219 FT /evidence="ECO:0007829|PDB:2XKO" SQ SEQUENCE 222 AA; 24833 MW; C6A9DC575D15A69A CRC64; MLANENSLLT MFRELGSGKL PLQIEQFERG KTIFFPGDPA ERVYLLVKGA VKLSRVYESG EEITVALLRE NSVFGVLSLL TGQRSDRFYH AVAFTPVQLF SVPIEFMQKA LIERPELANV MLQGLSSRIL QTEMMIETLA HRDMGSRLVS FLLILCRDFG IPSPDGITID LKLSHQAIAE AIGSTRVTVT RLLGDLRESK LIAIHKKRIT VFNPVALSQQ FS //