RSGI6_ACET2
ID RSGI6_ACET2 Reviewed; 760 AA.
AC A3DH97;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Anti-sigma-I factor RsgI6 {ECO:0000305};
DE AltName: Full=Endo-1,4-beta-xylanase {ECO:0000305};
DE EC=3.2.1.8 {ECO:0000269|PubMed:20820855};
GN Name=rsgI6 {ECO:0000303|PubMed:20487018};
GN OrderedLocusNames=Cthe_2119 {ECO:0000312|EMBL:ABN53326.1};
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 SIGI6.
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]
RP FUNCTION AS AN HYDROLASE, CATALYTIC ACTIVITY, AND DOMAIN.
RC STRAIN=ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL
RC B-4536 / VPI 7372;
RX PubMed=20820855; DOI=10.1007/s10295-010-0848-9;
RA Bahari L., Gilad Y., Borovok I., Kahel-Raifer H., Dassa B., Nataf Y.,
RA Shoham Y., Lamed R., Bayer E.A.;
RT "Glycoside hydrolases as components of putative carbohydrate biosensor
RT proteins in Clostridium thermocellum.";
RL J. Ind. Microbiol. Biotechnol. 38:825-832(2011).
CC -!- FUNCTION: Anti-sigma factor for SigI6. Negatively regulates SigI6
CC activity through direct interaction. Binding of the polysaccharide
CC substrate to the extracellular C-terminal sensing domain of RsgI6 may
CC induce a conformational change in its N-terminal cytoplasmic region,
CC leading to the release and activation of SigI6 (By similarity). Binds
CC to and hydrolyzes insoluble and soluble xylan substrates. Has low
CC enzymatic activity (PubMed:20820855). {ECO:0000250|UniProtKB:A3DBH1,
CC ECO:0000269|PubMed:20820855}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC EC=3.2.1.8; Evidence={ECO:0000269|PubMed:20820855};
CC -!- PATHWAY: Glycan degradation; xylan degradation. {ECO:0000255|PROSITE-
CC ProRule:PRU01096}.
CC -!- SUBUNIT: Interacts (via RsgI N-terminal anti-sigma domain) with SigI6.
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 GH10 domain binds to xylan. {ECO:0000269|PubMed:20820855}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the glycosyl
CC hydrolase 10 (cellulase F) family. {ECO:0000255|PROSITE-
CC ProRule:PRU01096}.
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; ABN53326.1; -; Genomic_DNA.
DR RefSeq; WP_003514230.1; NC_009012.1.
DR AlphaFoldDB; A3DH97; -.
DR SMR; A3DH97; -.
DR DIP; DIP-59454N; -.
DR IntAct; A3DH97; 1.
DR STRING; 203119.Cthe_2119; -.
DR CAZy; GH10; Glycoside Hydrolase Family 10.
DR EnsemblBacteria; ABN53326; ABN53326; Cthe_2119.
DR KEGG; cth:Cthe_2119; -.
DR eggNOG; COG3693; Bacteria.
DR HOGENOM; CLU_366698_0_0_9; -.
DR OrthoDB; 1808279at2; -.
DR UniPathway; UPA00114; -.
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:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR024449; Anti-sigma_RsgI_N.
DR InterPro; IPR044846; GH10.
DR InterPro; IPR001000; GH10_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31490; PTHR31490; 1.
DR Pfam; PF00331; Glyco_hydro_10; 1.
DR Pfam; PF12791; RsgI_N; 1.
DR SMART; SM00633; Glyco_10; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS51760; GH10_2; 1.
DR PROSITE; PS51849; RSGI_N; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cell membrane; Glycosidase; Hydrolase; Membrane;
KW Polysaccharide degradation; Reference proteome; Transmembrane;
KW Transmembrane helix; Xylan degradation.
FT CHAIN 1..760
FT /note="Anti-sigma-I factor RsgI6"
FT /id="PRO_0000436549"
FT TOPO_DOM 1..55
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 56..76
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 77..760
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT DOMAIN 2..49
FT /note="RsgI N-terminal anti-sigma"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01196"
FT DOMAIN 402..701
FT /note="GH10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT REGION 274..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 538
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT ACT_SITE 635
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
SQ SEQUENCE 760 AA; 85123 MW; EB46E76C5D786B1D CRC64;
MIVGKVLDMD EKTAIIMTDD FAFLNVVRTS EMAVGKKVKV LDSDIIKPKN SLRRYLPVAA
VAACFVIVLS FVLMFINGNT ARKNIYAYVG IDINPSIELW INYNNKIAEA KALNGDAETV
LEGLELKEKT VAEAVNEIVQ KSMELGFISR EKENIILIST ACDLKAGEGS ENKDVQNKIG
QLFDDVNKAV SDLKNSGITT RILNLTLEER ESSKEENISM GRYAVYLKAK EQNVNLTIDE
IKDADLLELI AKVGIDNENV PEDIVTEDKD NLDAINTGPA ESAVPEVTET LPATSTPGRT
EGNTATGSVD STPALSKNET PGKTETPGRT FNTPAKSSLG QSSTPKPVSP VQTATATKGI
GTLTPRNSPT PVIPSTGIQW IDQANERINE IRKRNVQIKV VDSSNKPIEN AYVEAVLTNH
AFGFGTAITR RAMYDSNYTK FIKDHFNWAV FENESKWYTN EPSMGIITYD DADYLYEFCR
SNGIKVRGHC IFWEAEEWQP AWVRSLDPFT LRFAVDNRLN SAVGHFKGKF EHWDVNNEMI
HGNFFKSRLG ESIWPYMFNR AREIDPNAKY FVNNNITTLK EADDCVALVN WLRSQGVRVD
GVGVHGHFGD SVDRNLLKGI LDKLSVLNLP IWITEYDSVT PDEYRRADNL ENLYRTAFSH
PSVEGIVMWG FWERVHWRGR DASIVNDNWT LNEAGRRFES LMNEWTTRAY GSTDGSGSFG
FRGFYGTYRI TVTVPGKGKY NYTLNLNRGS GTLQTTYRIP
