RSGI1_ACET2
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 03-AUG-2022, entry version 84.
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}.
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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 PRIDE; A3DBH1; -.
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
