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   25-OCT-2017, entry version 61.
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}.
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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   PDBsum; 4B9C; -.
DR   ProteinModelPortal; 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; ENOG4105WJF; Bacteria.
DR   eggNOG; ENOG41123G8; LUCA.
DR   OMA; ENRVINS; -.
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; 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.
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
//