ID RSGI1_CLOTH Reviewed; 486 AA. AC A3DBH1; DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot. DT 20-MAR-2007, sequence version 1. DT 02-NOV-2016, entry version 57. DE RecName: Full=Anti-sigma-I factor RsgI1 {ECO:0000305}; GN Name=rsgI1 {ECO:0000303|PubMed:20487018}; GN OrderedLocusNames=Cthe_0059 {ECO:0000312|EMBL:ABN51300.1}; OS Clostridium thermocellum (strain ATCC 27405 / DSM 1237 / NBRC 103400 / OS NCIMB 10682 / NRRL B-4536 / VPI 7372) (Ruminiclostridium OS thermocellum). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Ruminiclostridium. OX NCBI_TaxID=203119; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27405 / DSM 1237 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 RC / VPI 7372; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R., RA Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Wu J.H.D., Newcomb M., Richardson P.; RT "Complete sequence of Clostridium thermocellum ATCC 27405."; RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NOMENCLATURE, AND DOMAIN. RC STRAIN=ATCC 27405 / DSM 1237 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 RC / VPI 7372; RX PubMed=20487018; DOI=10.1111/j.1574-6968.2010.01997.x; RA Kahel-Raifer H., Jindou S., Bahari L., Nataf Y., Shoham Y., RA Bayer E.A., Borovok I., Lamed R.; RT "The unique set of putative membrane-associated anti-sigma factors in RT Clostridium thermocellum suggests a novel extracellular carbohydrate- RT sensing mechanism involved in gene regulation."; RL FEMS Microbiol. Lett. 308:84-93(2010). RN [3] RP FUNCTION, AND INTERACTION WITH SIGI1. RX PubMed=20937888; DOI=10.1073/pnas.1012175107; RA Nataf Y., Bahari L., Kahel-Raifer H., Borovok I., Lamed R., RA Bayer E.A., Sonenshein A.L., Shoham Y.; RT "Clostridium thermocellum cellulosomal genes are regulated by RT extracytoplasmic polysaccharides via alternative sigma factors."; RL Proc. Natl. Acad. Sci. U.S.A. 107:18646-18651(2010). RN [4] {ECO:0000244|PDB:4B9C} RP X-RAY CRYSTALLOGRAPHY (1.17 ANGSTROMS) OF 340-485 IN COMPLEX WITH RP CALCIUM. RC STRAIN=ATCC 27405 / DSM 1237 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 RC / VPI 7372; RX PubMed=24531486; DOI=10.1107/S139900471302926X; RA Yaniv O., Fichman G., Borovok I., Shoham Y., Bayer E.A., Lamed R., RA Shimon L.J., Frolow F.; RT "Fine-structural variance of family 3 carbohydrate-binding modules as RT extracellular biomass-sensing components of Clostridium thermocellum RT anti-sigmaI factors."; RL Acta Crystallogr. D 70:522-534(2014). CC -!- FUNCTION: Anti-sigma factor for SigI1. Negatively regulates SigI1 CC activity through direct interaction (PubMed:20937888). Binding of CC the polysaccharide substrate to the extracellular C-terminal CC sensing domain of RsgI1 may induce a conformational change in its CC N-terminal cytoplasmic region, leading to the release and CC activation of SigI1 (Probable). {ECO:0000269|PubMed:20937888, CC ECO:0000305|PubMed:20937888}. CC -!- SUBUNIT: Interacts (via N-terminal region) with SigI1. CC {ECO:0000269|PubMed:20937888}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass CC membrane protein {ECO:0000255}. CC -!- DOMAIN: The CBM3 domain binds to cellulose. CC {ECO:0000269|PubMed:20487018}. CC -!- SIMILARITY: Contains 1 CBM3 (carbohydrate binding type-3) domain. CC {ECO:0000255|PROSITE-ProRule:PRU00513}. CC -!- SIMILARITY: Contains 1 RsgI_N domain. {ECO:0000305}. 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; CP000568; ABN51300.1; -; Genomic_DNA. DR RefSeq; WP_003518401.1; NC_009012.1. DR PDB; 4B9C; X-ray; 1.17 A; A=340-485. DR PDBsum; 4B9C; -. DR ProteinModelPortal; A3DBH1; -. DR SMR; A3DBH1; -. DR DIP; DIP-59450N; -. DR STRING; 203119.Cthe_0059; -. DR CAZy; CBM3; Carbohydrate-Binding Module Family 3. DR EnsemblBacteria; ABN51300; ABN51300; Cthe_0059. DR KEGG; cth:Cthe_0059; -. DR PATRIC; 19513725; VBICloThe47081_0065. DR eggNOG; ENOG4105WJF; Bacteria. DR eggNOG; ENOG41123G8; LUCA. DR OMA; NINFAVY; -. DR OrthoDB; POG091H0YQ0; -. DR Proteomes; UP000002145; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0030248; F:cellulose binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR Gene3D; 2.60.40.710; -; 1. DR InterPro; IPR024449; Anti-sigma_RsgI_N. DR InterPro; IPR008965; Carb-bd_dom. DR InterPro; IPR001956; CBD_3. DR Pfam; PF00942; CBM_3; 1. DR Pfam; PF12791; RsgI_N; 1. DR SMART; SM01067; CBM_3; 1. DR SUPFAM; SSF49384; SSF49384; 1. DR PROSITE; PS51172; CBM3; 1. PE 1: Evidence at protein level; KW 3D-structure; Calcium; Cell membrane; Coiled coil; Complete proteome; KW Membrane; Metal-binding; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 486 Anti-sigma-I factor RsgI1. FT /FTId=PRO_0000436544. FT TOPO_DOM 1 53 Cytoplasmic. {ECO:0000305}. FT TRANSMEM 54 74 Helical. {ECO:0000255}. FT TOPO_DOM 75 486 Extracellular. {ECO:0000305}. FT DOMAIN 9 59 RsgI_N. {ECO:0000305}. FT DOMAIN 336 486 CBM3. {ECO:0000255|PROSITE- FT ProRule:PRU00513}. FT COILED 161 192 {ECO:0000255}. FT METAL 382 382 Calcium; via carbonyl oxygen. FT {ECO:0000244|PDB:4B9C, FT ECO:0000269|PubMed:24531486}. FT METAL 452 452 Calcium; via carbonyl oxygen. FT {ECO:0000244|PDB:4B9C, FT ECO:0000269|PubMed:24531486}. FT METAL 455 455 Calcium. {ECO:0000244|PDB:4B9C, FT ECO:0000269|PubMed:24531486}. FT METAL 456 456 Calcium. {ECO:0000244|PDB:4B9C, FT ECO:0000269|PubMed:24531486}. FT STRAND 341 344 {ECO:0000244|PDB:4B9C}. FT STRAND 351 357 {ECO:0000244|PDB:4B9C}. FT STRAND 360 364 {ECO:0000244|PDB:4B9C}. FT STRAND 366 368 {ECO:0000244|PDB:4B9C}. FT HELIX 372 374 {ECO:0000244|PDB:4B9C}. FT STRAND 375 381 {ECO:0000244|PDB:4B9C}. FT HELIX 387 389 {ECO:0000244|PDB:4B9C}. FT STRAND 390 397 {ECO:0000244|PDB:4B9C}. FT HELIX 402 404 {ECO:0000244|PDB:4B9C}. FT STRAND 405 411 {ECO:0000244|PDB:4B9C}. FT STRAND 419 428 {ECO:0000244|PDB:4B9C}. FT STRAND 436 445 {ECO:0000244|PDB:4B9C}. FT STRAND 471 475 {ECO:0000244|PDB:4B9C}. FT STRAND 478 482 {ECO:0000244|PDB:4B9C}. SQ SEQUENCE 486 AA; 55308 MW; 909D55B6F51494F0 CRC64; MNRLGIIYEI QGMKAVVLTS EGEFLIIRRR KDMKVGQQVS FENEDIYNVR GKRFLYVAAA VSSVAAVLVV MFLYFQSAFL SNTDNIYGYI CVDINPSVEL VIDETCRVLE VRPQNKDGEQ LISGLELLDK NVEDVVYELI NRSISFGFVK ADDNRKIVLI SGALNDKRNE LKTKKENDEA ELTELLDNIK ARVDRIDNIK VRTITATSRE RKDALKYGLS MGKYCLYLEA QELNGSITID EVHDMSISDM IEKLEQMKLA LKDEASPKLQ TTPTLGGETA QISPESMQHS TVPGLPETPS SSEKTIAPTL HGTPGVPDEK TLQPSTPTES SEYVQDGTKG LKIQYYSRKP HDSAGIDFSF RMFNTGNEAI DLKDVKVRYY FKEDVSIDEM NWAVYFYSLG SEKDVQCRFY ELPGKKEANK YLEITFKSGT LSPNDVMYIT GEFYKNDWTK FEQRDDYSYN PADSYSDWKR MTAYISNKLV WGIEPN //