RSGI2_ACET2
ID RSGI2_ACET2 Reviewed; 671 AA.
AC A3DC27;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Anti-sigma-I factor RsgI2 {ECO:0000305};
GN Name=rsgI2 {ECO:0000303|PubMed:20487018};
GN OrderedLocusNames=Cthe_0267 {ECO:0000312|EMBL:ABN51506.1};
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.
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 INTERACTION WITH SIGI2.
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:4B9P}
RP X-RAY CRYSTALLOGRAPHY (1.18 ANGSTROMS) OF 506-671 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 SigI2. Negatively regulates SigI2
CC activity through direct interaction. Binding of the polysaccharide
CC substrate to the extracellular C-terminal sensing domain of RsgI2 may
CC induce a conformational change in its N-terminal cytoplasmic region,
CC leading to the release and activation of SigI2.
CC {ECO:0000250|UniProtKB:A3DBH1}.
CC -!- SUBUNIT: Interacts (via RsgI N-terminal anti-sigma domain) with SigI2.
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 ---------------------------------------------------------------------------
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; ABN51506.1; -; Genomic_DNA.
DR PDB; 4B9P; X-ray; 1.18 A; A=506-671.
DR PDBsum; 4B9P; -.
DR AlphaFoldDB; A3DC27; -.
DR SMR; A3DC27; -.
DR DIP; DIP-59452N; -.
DR IntAct; A3DC27; 1.
DR STRING; 203119.Cthe_0267; -.
DR CAZy; CBM3; Carbohydrate-Binding Module Family 3.
DR EnsemblBacteria; ABN51506; ABN51506; Cthe_0267.
DR KEGG; cth:Cthe_0267; -.
DR eggNOG; COG4447; Bacteria.
DR HOGENOM; CLU_409228_0_0_9; -.
DR OMA; INEIYTC; -.
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; Membrane; Metal-binding;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..671
FT /note="Anti-sigma-I factor RsgI2"
FT /id="PRO_0000436545"
FT TOPO_DOM 1..57
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 79..671
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT DOMAIN 4..51
FT /note="RsgI N-terminal anti-sigma"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01196"
FT DOMAIN 508..671
FT /note="CBM3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00513"
FT REGION 290..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..402
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..454
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..487
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..502
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 554
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:24531486,
FT ECO:0007744|PDB:4B9P"
FT BINDING 556
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:24531486,
FT ECO:0007744|PDB:4B9P"
FT BINDING 637
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:24531486,
FT ECO:0007744|PDB:4B9P"
FT BINDING 640
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:24531486,
FT ECO:0007744|PDB:4B9P"
FT BINDING 641
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:24531486,
FT ECO:0007744|PDB:4B9P"
FT STRAND 512..519
FT /evidence="ECO:0007829|PDB:4B9P"
FT STRAND 523..528
FT /evidence="ECO:0007829|PDB:4B9P"
FT STRAND 530..536
FT /evidence="ECO:0007829|PDB:4B9P"
FT STRAND 538..540
FT /evidence="ECO:0007829|PDB:4B9P"
FT HELIX 544..546
FT /evidence="ECO:0007829|PDB:4B9P"
FT STRAND 547..553
FT /evidence="ECO:0007829|PDB:4B9P"
FT STRAND 560..568
FT /evidence="ECO:0007829|PDB:4B9P"
FT HELIX 572..574
FT /evidence="ECO:0007829|PDB:4B9P"
FT STRAND 575..586
FT /evidence="ECO:0007829|PDB:4B9P"
FT STRAND 589..597
FT /evidence="ECO:0007829|PDB:4B9P"
FT STRAND 609..618
FT /evidence="ECO:0007829|PDB:4B9P"
FT HELIX 619..622
FT /evidence="ECO:0007829|PDB:4B9P"
FT HELIX 631..633
FT /evidence="ECO:0007829|PDB:4B9P"
FT STRAND 636..638
FT /evidence="ECO:0007829|PDB:4B9P"
FT STRAND 657..661
FT /evidence="ECO:0007829|PDB:4B9P"
FT STRAND 664..667
FT /evidence="ECO:0007829|PDB:4B9P"
SQ SEQUENCE 671 AA; 71917 MW; A57F84976CB08FCD CRC64;
MSHYTGIILK LESDRAIVLT DGLDFMELKL KPGMQRGQHV IFDESDLYSA GLITRYKSII
MPFSAFAAAA AVFLVILFSL RFVSISQEYA YIDVDINPSI GLVIDKKEKV IDAKPLNNDA
KPILDEAAPK DMPLYDALSK ILDISKKNGY INSADNIVLF SASINSGRNN VSESDKGIQE
IISTLKDVAK DAGVKFEIIP STEEDRQKAL DQNLSMGRYA IYVKAVEEGV NLNLEDARNL
SVSEILGKVN IGKFAISDTP EDSGIMPAIS VPAEPVPSVT PAYTAVPEKT EAQPVDIPKS
SPTPASFTAH VPTPPKTPSI PHTSGPAIVH TPAADKTTPT FTGSSTPVPT NVVAIASTPV
PVSTPKPVST PAYSSTPTPE STPVPVSTPK PASTPTPAST PKPVSTPTHV STPKPISTPT
STPRPASTPK PTSTPTPEST PKPTSTPAPV STPTSTPIPT YTSTPASTPI PAYTSTPTSI
PTLTPATSPA PTSSPTPIPS PAPTETDLLT KIELQAYNHI RTSETKELQP RIKLINTGNT
PITLSEVKIR YYYTKDQVIN EIYTCDWSNI TSSKITGTVV QMSNPKPNAD SYVEIGFTNS
AGVLNPGEYV EIISRIGNSY ALSLATPPYS EWNYMYDQNS DYSFNNSSSD FVVWDKITVY
ISGTLYWGIE P
