ID CRL_ECOLI Reviewed; 133 AA. AC P24251; P77629; Q47242; Q47585; DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 5. DT 02-SEP-2026, entry version 163. DE RecName: Full=Sigma factor-binding protein Crl; DE AltName: Full=Curlin genes transcriptional activatory protein; GN Name=crl; OrderedLocusNames=b0240, JW0230; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=K12; RX PubMed=6341601; DOI=10.1016/0022-2836(83)90110-9; RA Overbeeke N., Bergmans H., van Mansfeld F., Lugtenberg B.; RT "Complete nucleotide sequence of phoE, the structural gene for the RT phosphate limitation inducible outer membrane pore protein of Escherichia RT coli K12."; RL J. Mol. Biol. 163:513-532(1983). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-6, AND RP CHARACTERIZATION. RC STRAIN=AO12; RX PubMed=2649795; DOI=10.1038/338652a0; RA Olsen A., Jonsson A., Normark S.; RT "Fibronectin binding mediated by a novel class of surface organelles on RT Escherichia coli."; RL Nature 338:652-655(1989). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION. RC STRAIN=AO12; RX PubMed=1357528; DOI=10.1111/j.1365-2958.1992.tb01420.x; RA Arnqvist A., Olsen A., Pfeifer J., Russell D.G., Normark S.; RT "The Crl protein activates cryptic genes for curli formation and RT fibronectin binding in Escherichia coli HB101."; RL Mol. Microbiol. 6:2443-2452(1992). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RA Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T., RA Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S., RA Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.; RT "Systematic sequencing of the Escherichia coli genome: analysis of the 4.0 RT - 6.0 min (189,987 - 281,416bp) region."; RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.; RT "Sequence of minutes 4-25 of Escherichia coli."; RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., RA Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1462(1997). RN [7] RP SEQUENCE REVISION. RC STRAIN=K12 / MG1655 / ATCC 700926; RX PubMed=22081388; DOI=10.1128/jb.06087-11; RA Freddolino P.L., Amini S., Tavazoie S.; RT "Newly identified genetic variations in common Escherichia coli MG1655 RT stock cultures."; RL J. Bacteriol. 194:303-306(2012). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO 28. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 RT and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-32. RX PubMed=6397401; DOI=10.1016/0378-1119(84)90052-0; RA Nueesch J., Schuemperli D.; RT "Structural and functional organization of the gpt gene region of RT Escherichia coli."; RL Gene 32:243-249(1984). RN [10] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-32. RC STRAIN=O9:K30:H12; RX PubMed=1729226; DOI=10.1128/jb.174.1.8-16.1992; RA Keenleyside W.J., Jayaratne P., MacLachlan P.R., Whitfield C.; RT "The rcsA gene of Escherichia coli 09:K30:H12 is involved in the expression RT of the serotype-specific group I K (capsular) antigen."; RL J. Bacteriol. 174:8-16(1992). RN [11] RP ACTIVATION OF RPOS ACTIVITY. RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574; RX PubMed=9767590; DOI=10.1046/j.1365-2958.1998.01007.x; RA Pratt L.A., Silhavy T.J.; RT "Crl stimulates RpoS activity during stationary phase."; RL Mol. Microbiol. 29:1225-1236(1998). RN [12] RP BINDING TO SIGMA-SUBUNIT OF RNA POLYMERASE. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=14978043; DOI=10.1074/jbc.m314145200; RA Bougdour A., Lelong C., Geiselmann J.; RT "Crl, a low temperature-induced protein in Escherichia coli that binds RT directly to the stationary phase sigma subunit of RNA polymerase."; RL J. Biol. Chem. 279:19540-19550(2004). RN [13] RP ROLE IN RNA POLYMERASE HOLOENZYME FORMATION. RX PubMed=16980472; DOI=10.1128/jb.01266-06; RA Gaal T., Mandel M.J., Silhavy T.J., Gourse R.L.; RT "Crl facilitates RNA polymerase holoenzyme formation."; RL J. Bacteriol. 188:7966-7970(2006). CC -!- FUNCTION: Binds to the sigma-S subunit of RNA polymerase, activating CC expression of sigma-S-regulated genes, such as the csgBAC operon CC encoding the subunits of curli proteins. Stimulates RNA polymerase CC holoenzyme formation and may bind to several other sigma factors, such CC as sigma-70 (rpoD) and sigma-32 (rpoH). {ECO:0000269|PubMed:1357528, CC ECO:0000269|PubMed:16980472}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- INDUCTION: Induced at stationary phase, and by low temperatures. CC -!- SIMILARITY: Belongs to the Crl family. {ECO:0000305}. CC -!- CAUTION: A pseudogene in strain MG1655 / ATCC 700926, but not its CC parent MG1655 / ATCC 47076. In ATCC 700926 IS1I has recently inserted CC into the gene (PubMed:22081388). {ECO:0000305|PubMed:22081388}. 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; V00316; CAA23606.1; -; Genomic_DNA. DR EMBL; X67207; CAA47646.1; -; Genomic_DNA. DR EMBL; U70214; AAB08660.1; -; Genomic_DNA. DR EMBL; U00096; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP009048; BAA77909.2; -; Genomic_DNA. DR EMBL; M13422; AAA23930.1; -; Genomic_DNA. DR PIR; A64749; A64749. DR RefSeq; WP_000174689.1; NZ_CP009789.1. DR PDB; 6KJ6; EM; 3.80 A; J=1-133. DR AlphaFoldDB; P24251; -. DR SMR; P24251; -. DR BioGRID; 4260821; 142. DR FunCoup; P24251; 145. DR IntAct; P24251; 11. DR jPOST; P24251; -. DR KEGG; ecj:JW0230; -. DR KEGG; ecoc:C3026_01140; -. DR KEGG; ecoc:C3026_23875; -. DR PATRIC; fig|1411691.4.peg.2043; -. DR EchoBASE; EB1084; -. DR eggNOG; ENOG502ZQ8E; Bacteria. DR HOGENOM; CLU_136773_0_0_6; -. DR InParanoid; P24251; -. DR OMA; FWGWWLE; -. DR OrthoDB; 6428303at2; -. DR PhylomeDB; P24251; -. DR PRO; PR:P24251; -. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0005829; C:cytosol; IDA:EcoCyc. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:EcoCyc. DR GO; GO:2000144; P:positive regulation of DNA-templated transcription initiation; IDA:EcoCyc. DR GO; GO:0065003; P:protein-containing complex assembly; IDA:EcoCyc. DR FunFam; 3.30.310.230:FF:000001; Sigma factor-binding protein Crl; 1. DR Gene3D; 3.30.310.230; Sigma factor-binding protein Crl monomer; 1. DR HAMAP; MF_01178; Crl; 1. DR InterPro; IPR009986; Tscrpt_reg_Crl. DR InterPro; IPR038208; Tscrpt_reg_Crl_sf. DR NCBIfam; NF008217; PRK10984.1; 1. DR Pfam; PF07417; Crl; 1. DR PDBsum; 6KJ6; -. PE 1: Evidence at protein level; KW 3D-structure; Activator; Coiled coil; Cytoplasm; Direct protein sequencing; KW Reference proteome; Transcription; Transcription regulation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:2649795" FT CHAIN 2..133 FT /note="Sigma factor-binding protein Crl" FT /id="PRO_0000079355" FT REGION 99..122 FT /note="Essential for activity" FT COILED 90..116 FT /evidence="ECO:0000255" FT CONFLICT 8 FT /note="P -> L (in Ref. 1; CAA23606)" FT /evidence="ECO:0000305" FT CONFLICT 13 FT /note="I -> N (in Ref. 1; CAA23606)" FT /evidence="ECO:0000305" FT CONFLICT 29 FT /note="K -> E (in Ref. 2 and 3; CAA47646)" FT /evidence="ECO:0000305" SQ SEQUENCE 133 AA; 15655 MW; EA66172EF19586AA CRC64; MTLPSGHPKS RLIKKFTALG PYIREGKCKD NRFFFDCLAV CVNVKPAPEV REFWGWWMEL EAQESRFTYS YQFGLFDKAG DWKSVPVKDT EVVERLEHTL REFHEKLREL LTTLNLKLEP ADDFRDEPVK LTA //