ID RSGI1_ACET2 Reviewed; 486 AA. AC A3DBH1; DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot. DT 20-MAR-2007, sequence version 1. DT 12-OCT-2022, entry version 85. 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 Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC OS 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Clostridium thermocellum). OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae; OC Acetivibrio. OX NCBI_TaxID=203119; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL RC B-4536 / 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., Pitluck S., RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Wu J.H.D., RA 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 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL RC B-4536 / 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., Bayer E.A., RA 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., Bayer E.A., RA 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:0007744|PDB:4B9C} RP X-RAY CRYSTALLOGRAPHY (1.17 ANGSTROMS) OF 340-485 IN COMPLEX WITH CALCIUM. RC STRAIN=ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL RC B-4536 / 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 anti- RT 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 the CC polysaccharide substrate to the extracellular C-terminal sensing domain CC of RsgI1 may induce a conformational change in its N-terminal CC cytoplasmic region, leading to the release and activation of SigI1 CC (Probable). {ECO:0000269|PubMed:20937888, ECO:0000305|PubMed:20937888}. CC -!- SUBUNIT: Interacts (via RsgI N-terminal anti-sigma domain) with SigI1. CC {ECO:0000255|PROSITE-ProRule:PRU01196, ECO:0000269|PubMed:20937888}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000255}. CC -!- DOMAIN: The CBM3 domain binds to cellulose. CC {ECO:0000269|PubMed:20487018}. 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 PDB; 6IVS; NMR; -; A=1-52. DR PDB; 6IVU; NMR; -; A=1-52. DR PDBsum; 4B9C; -. DR PDBsum; 6IVS; -. DR PDBsum; 6IVU; -. DR AlphaFoldDB; A3DBH1; -. DR BMRB; A3DBH1; -. DR SMR; A3DBH1; -. DR DIP; DIP-59450N; -. DR IntAct; A3DBH1; 1. 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 eggNOG; COG4447; Bacteria. DR HOGENOM; CLU_511640_0_0_9; -. DR OMA; SSATWHW; -. DR OrthoDB; 1808279at2; -. 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; CBM2/CBM3_carb-bd_dom_sf. DR InterPro; IPR001956; CBM3. DR InterPro; IPR036966; CBM3_sf. 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. DR PROSITE; PS51849; RSGI_N; 1. PE 1: Evidence at protein level; KW 3D-structure; Calcium; Cell membrane; Coiled coil; Membrane; Metal-binding; KW Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1..486 FT /note="Anti-sigma-I factor RsgI1" FT /id="PRO_0000436544" FT TOPO_DOM 1..53 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 54..74 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 75..486 FT /note="Extracellular" FT /evidence="ECO:0000305" FT DOMAIN 3..50 FT /note="RsgI N-terminal anti-sigma" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01196" FT DOMAIN 336..486 FT /note="CBM3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00513" FT REGION 265..336 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 161..192 FT /evidence="ECO:0000255" FT COMPBIAS 267..308 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 319..336 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 382 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000269|PubMed:24531486, FT ECO:0007744|PDB:4B9C" FT BINDING 452 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000269|PubMed:24531486, FT ECO:0007744|PDB:4B9C" FT BINDING 455 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000269|PubMed:24531486, FT ECO:0007744|PDB:4B9C" FT BINDING 456 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000269|PubMed:24531486, FT ECO:0007744|PDB:4B9C" FT STRAND 2..11 FT /evidence="ECO:0007829|PDB:6IVS" FT STRAND 14..19 FT /evidence="ECO:0007829|PDB:6IVS" FT STRAND 24..28 FT /evidence="ECO:0007829|PDB:6IVS" FT STRAND 37..42 FT /evidence="ECO:0007829|PDB:6IVS" FT HELIX 43..45 FT /evidence="ECO:0007829|PDB:6IVS" FT STRAND 46..50 FT /evidence="ECO:0007829|PDB:6IVS" FT STRAND 341..344 FT /evidence="ECO:0007829|PDB:4B9C" FT STRAND 351..357 FT /evidence="ECO:0007829|PDB:4B9C" FT STRAND 360..364 FT /evidence="ECO:0007829|PDB:4B9C" FT STRAND 366..368 FT /evidence="ECO:0007829|PDB:4B9C" FT HELIX 372..374 FT /evidence="ECO:0007829|PDB:4B9C" FT STRAND 375..381 FT /evidence="ECO:0007829|PDB:4B9C" FT HELIX 387..389 FT /evidence="ECO:0007829|PDB:4B9C" FT STRAND 390..397 FT /evidence="ECO:0007829|PDB:4B9C" FT HELIX 402..404 FT /evidence="ECO:0007829|PDB:4B9C" FT STRAND 405..411 FT /evidence="ECO:0007829|PDB:4B9C" FT STRAND 419..428 FT /evidence="ECO:0007829|PDB:4B9C" FT STRAND 436..445 FT /evidence="ECO:0007829|PDB:4B9C" FT STRAND 471..475 FT /evidence="ECO:0007829|PDB:4B9C" FT STRAND 478..482 FT /evidence="ECO:0007829|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 //