RSGI3_ACET2
ID RSGI3_ACET2 Reviewed; 644 AA.
AC A3DC75;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Anti-sigma-I factor RsgI3 {ECO:0000305};
GN Name=rsgI3 {ECO:0000303|PubMed:20487018};
GN OrderedLocusNames=Cthe_0316 {ECO:0000312|EMBL:ABN51554.1};
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Borovok I.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP INDUCTION.
RC STRAIN=ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL
RC B-4536 / VPI 7372;
RX PubMed=24782837; DOI=10.3389/fmicb.2014.00142;
RA Wei H., Fu Y., Magnusson L., Baker J.O., Maness P.C., Xu Q., Yang S.,
RA Bowersox A., Bogorad I., Wang W., Tucker M.P., Himmel M.E., Ding S.Y.;
RT "Comparison of transcriptional profiles of Clostridium thermocellum grown
RT on cellobiose and pretreated yellow poplar using RNA-Seq.";
RL Front. Microbiol. 5:142-142(2014).
CC -!- FUNCTION: Anti-sigma factor for SigI3. Negatively regulates SigI3
CC activity through direct interaction. Binding of the polysaccharide
CC substrate to the extracellular C-terminal sensing domain of RsgI3 may
CC induce a conformational change in its N-terminal cytoplasmic region,
CC leading to the release and activation of SigI3.
CC {ECO:0000250|UniProtKB:A3DBH1}.
CC -!- SUBUNIT: Interacts (via RsgI N-terminal anti-sigma domain) with SigI3.
CC {ECO:0000255|PROSITE-ProRule:PRU01196}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Up-regulated in pretreated yellow poplar (PYP)-grown cells.
CC {ECO:0000269|PubMed:24782837}.
CC -!- DOMAIN: The PA14 dyad binds strongly to pectin as well as to
CC polygalacturonic acid and alfalfa cell walls, but to a lesser extent.
CC {ECO:0000269|PubMed:20487018}.
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DR EMBL; CP000568; ABN51554.1; -; Genomic_DNA.
DR EMBL; KM504391; AIY67765.1; -; Genomic_DNA.
DR RefSeq; WP_003512516.1; NC_009012.1.
DR PDB; 6QE7; X-ray; 2.06 A; A/B/C=358-644.
DR PDBsum; 6QE7; -.
DR AlphaFoldDB; A3DC75; -.
DR SMR; A3DC75; -.
DR STRING; 203119.Cthe_0316; -.
DR EnsemblBacteria; ABN51554; ABN51554; Cthe_0316.
DR KEGG; cth:Cthe_0316; -.
DR eggNOG; COG2133; Bacteria.
DR eggNOG; COG5183; Bacteria.
DR HOGENOM; CLU_424960_0_0_9; -.
DR OMA; SIRLEWE; -.
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 InterPro; IPR024449; Anti-sigma_RsgI_N.
DR InterPro; IPR037524; PA14/GLEYA.
DR InterPro; IPR011658; PA14_dom.
DR Pfam; PF07691; PA14; 2.
DR Pfam; PF12791; RsgI_N; 1.
DR SMART; SM00758; PA14; 2.
DR PROSITE; PS51820; PA14; 2.
DR PROSITE; PS51849; RSGI_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..644
FT /note="Anti-sigma-I factor RsgI3"
FT /id="PRO_0000436546"
FT TOPO_DOM 1..56
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 78..644
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 354..491
FT /note="PA14 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01164"
FT DOMAIN 502..640
FT /note="PA14 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01164"
FT REGION 302..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 358..366
FT /evidence="ECO:0007829|PDB:6QE7"
FT STRAND 371..380
FT /evidence="ECO:0007829|PDB:6QE7"
FT STRAND 382..384
FT /evidence="ECO:0007829|PDB:6QE7"
FT STRAND 396..407
FT /evidence="ECO:0007829|PDB:6QE7"
FT STRAND 410..423
FT /evidence="ECO:0007829|PDB:6QE7"
FT STRAND 425..429
FT /evidence="ECO:0007829|PDB:6QE7"
FT STRAND 432..437
FT /evidence="ECO:0007829|PDB:6QE7"
FT STRAND 442..452
FT /evidence="ECO:0007829|PDB:6QE7"
FT STRAND 458..466
FT /evidence="ECO:0007829|PDB:6QE7"
FT STRAND 472..478
FT /evidence="ECO:0007829|PDB:6QE7"
FT STRAND 480..482
FT /evidence="ECO:0007829|PDB:6QE7"
FT STRAND 484..486
FT /evidence="ECO:0007829|PDB:6QE7"
FT HELIX 489..491
FT /evidence="ECO:0007829|PDB:6QE7"
FT STRAND 492..494
FT /evidence="ECO:0007829|PDB:6QE7"
FT STRAND 505..514
FT /evidence="ECO:0007829|PDB:6QE7"
FT STRAND 519..532
FT /evidence="ECO:0007829|PDB:6QE7"
FT STRAND 538..541
FT /evidence="ECO:0007829|PDB:6QE7"
FT STRAND 546..555
FT /evidence="ECO:0007829|PDB:6QE7"
FT STRAND 558..577
FT /evidence="ECO:0007829|PDB:6QE7"
FT STRAND 580..585
FT /evidence="ECO:0007829|PDB:6QE7"
FT STRAND 593..601
FT /evidence="ECO:0007829|PDB:6QE7"
FT STRAND 607..618
FT /evidence="ECO:0007829|PDB:6QE7"
FT STRAND 621..627
FT /evidence="ECO:0007829|PDB:6QE7"
FT STRAND 629..631
FT /evidence="ECO:0007829|PDB:6QE7"
FT STRAND 633..635
FT /evidence="ECO:0007829|PDB:6QE7"
FT HELIX 638..640
FT /evidence="ECO:0007829|PDB:6QE7"
SQ SEQUENCE 644 AA; 72680 MW; 85DCCAB4EAA965D1 CRC64;
MDNIGVIIKI EGNEAIVMTD DCSFKKVPIK DGMHPGQKIL VPNNEVIQKE NKSIKRISAV
ATGIAAVFLM VLSLIWINKP GRPDGIYAYI DVDINPSLNF LIDREGKVKA LNPLNDDAQE
IIRGVEFEDM FFSEALTQII KISKAKGIID ENKTNYVLIC AALDDNYNLQ SDDKSRAQTE
FEEFLDGIRE SIEKACGNTV IPQTVKVPFE YLKMAKQNDV SMGRYLVYQK LEDIGVNLSI
EELKSLDIDE ILKKYGVGFD ELFKSEYTEL PYGTLQTGED SVVSTEDVPV SPKNAFETMA
VPTNTPSIST KPSATPAENP TPKLTQKPTP VPAKTGERTS TTPTPTPAPT VRNGTGSGLR
GEYYNNMDFS RFQFVRIDPC IDFDWGEGTP DQSIGKDTYS VRWTGKVEPR YSETYTFYTV
TDDGVRLWVD GVLLIDKWKS QSATEHSEQI YLEAGKKYDI KMEYYQHVRA ASAKLMWSSK
SQQKEIIPSS QLYPSDGPLP QKDVNGLSAE YYGDAELKDK RFTRIDDAIN FNWDKDFPVG
ELKDGKFSVR WVGKIDTRYT EEYTFHTVAN GGVRVWINNV LIIDNWQNQG KEAENSGKIE
LKAGRQYDIK VEYCNYGEPA FIKLLWSSQR QKKEVVPSKN LFAD
