ID A0AEF5_RUMFL Unreviewed; 803 AA. AC A0AEF5; DT 28-NOV-2006, integrated into UniProtKB/TrEMBL. DT 28-NOV-2006, sequence version 1. DT 27-MAR-2024, entry version 52. DE SubName: Full=Putative cellulose-binding protein {ECO:0000313|EMBL:CAK18897.1}; DE Flags: Precursor; GN Name=cttA {ECO:0000313|EMBL:CAK18897.1}; OS Ruminococcus flavefaciens. OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae; OC Ruminococcus. OX NCBI_TaxID=1265 {ECO:0000313|EMBL:CAK18897.1}; RN [1] {ECO:0000313|EMBL:CAK18897.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=FD-1 {ECO:0000313|EMBL:CAK18897.1}; RX PubMed=16997963; DOI=10.1128/JB.00973-06; RA Sadanari J., Borovok I., Rincon M.T., Flint H.J., Antonopoulos D.A., RA Berg M.E., White B.A., Bayer E.A., Lamed R.; RT "Conservation and divergence in cellulosome architecture between two RT strains of Ruminococcus flavefaciens."; RL J. Bacteriol. 188:7971-7976(2006). RN [2] {ECO:0007829|PDB:4IU2, ECO:0007829|PDB:4IU3} RP X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS) OF 565-803 IN COMPLEX WITH CALCIUM. RX PubMed=23580648; DOI=10.1074/jbc.M113.466672; RA Salama-Alber O., Jobby M.K., Chitayat S., Smith S.P., White B.A., RA Shimon L.J., Lamed R., Frolow F., Bayer E.A.; RT "Atypical cohesin-dockerin complex responsible for cell surface attachment RT of cellulosomal components: binding fidelity, promiscuity, and structural RT buttresses."; RL J. Biol. Chem. 288:16827-16838(2013). RN [3] {ECO:0007829|PDB:4WKZ} RP X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF 565-803 IN COMPLEX WITH CALCIUM. RA Voronov-Goldman M., Lamed R., Bayer E.A., Yaniv O., Shimon L.J.W.; RT "Complex of autonomous ScaG cohesin CohG and X-doc domains."; RL Submitted (OCT-2014) to the PDB data bank. CC -!- INTERACTION: CC A0AEF5; W5IDC3; NbExp=2; IntAct=EBI-11178202, EBI-11178209; 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; AM262974; CAK18897.1; -; Genomic_DNA. DR PDB; 4IU2; X-ray; 2.00 A; B=565-803. DR PDB; 4IU3; X-ray; 1.97 A; B=565-803. DR PDB; 4WKZ; X-ray; 1.79 A; A=565-803. DR PDBsum; 4IU2; -. DR PDBsum; 4IU3; -. DR PDBsum; 4WKZ; -. DR AlphaFoldDB; A0AEF5; -. DR SMR; A0AEF5; -. DR IntAct; A0AEF5; 2. DR MINT; A0AEF5; -. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:InterPro. DR CDD; cd14257; CttA_X; 1. DR CDD; cd14255; Dockerin_III; 1. DR Gene3D; 2.60.40.3810; -; 1. DR Gene3D; 1.10.1330.10; Dockerin domain; 1. DR InterPro; IPR040959; CttA_N. DR InterPro; IPR033802; CttA_X. DR InterPro; IPR036439; Dockerin_dom_sf. DR Pfam; PF18244; CttA_N; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:4IU2, ECO:0007829|PDB:4IU3}; KW Calcium {ECO:0007829|PDB:4IU2, ECO:0007829|PDB:4IU3}; KW Metal-binding {ECO:0007829|PDB:4IU2, ECO:0007829|PDB:4IU3}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..30 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 31..803 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5002622278" FT DOMAIN 583..662 FT /note="Cellulose-binding protein CttA N-terminal" FT /evidence="ECO:0000259|Pfam:PF18244" FT REGION 430..562 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 684 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4IU2, ECO:0007829|PDB:4IU3" FT BINDING 686 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4IU2, ECO:0007829|PDB:4IU3" FT BINDING 688 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4IU2, ECO:0007829|PDB:4IU3" FT BINDING 690 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4IU2, ECO:0007829|PDB:4IU3" FT BINDING 695 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4IU2, ECO:0007829|PDB:4IU3" FT BINDING 741 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4IU2, ECO:0007829|PDB:4IU3" FT BINDING 743 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4IU2, ECO:0007829|PDB:4IU3" FT BINDING 745 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4WKZ" FT BINDING 760 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4IU2, ECO:0007829|PDB:4IU3" FT BINDING 765 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4IU2, ECO:0007829|PDB:4IU3" SQ SEQUENCE 803 AA; 84775 MW; D61E1EE6F98E1766 CRC64; MKNSLFKRVA AAAAAVPLAL TQCLTFSSVA AENDAVQIVG NTVQDGAAQT VSLESLLYIP ANKTESTWNV TGSAALAKMV GTKGSINNAK ILDLVKYVPA NYREAAKAAL EEYVLVNPVT YEVTADKNIV LKATVSQPNF NGNWANTPGK ALSDLAKAYN APELNAVDFS SVKVGGDLVV TIKTSKLDEG TTVPVEVVYK TADGDIYAGD FAKFANDKLT ELENIAKKAI ENDVAAQYAK EATDKFLAKT ALIRDKINKA EKALDQALTK TADYKSISEA ADAANKFLAK KNINKKVPSS AAEVAAKETV KKYYDAAVKK ASAKADIQIT VEQLGAFVDS LTSKTLTDSE GNEFATAFDI NLNNGKATLV GAFEDAEAAD VQKWVESKGY AYVGSYKKLT GTVDFTGIKT ADTASVDVQI ERILVTETTT TTTTTTDDGS TTTTTTDDGS TTTTTTDDGS TTTTTSTTDD GSTTSTTSTT DDGSTTSTTS TTDDGSTTST TSTTDDGSTT STTSTTDDGS TTSTTSTTDD GSTTSTTSTT DDGSTTSTTS TTGDGSTTTT TTTTNTVTSA VKTQYVEIES VDGFYFNTED KFDTAQIKKA VLHTVYNEGY TGDDGVAVVL REYESEPVDI TAELTFGDAT PANTYKAVEN KFDYEIPVYY NNATLKDAEG NDATVTVYIG LKGDTDLNNI VDGRDATATL TYYAATSTDG KDATTVALSP STLVGGNPES VYDDFSAFLS DVKVDAGKEL TRFAKKAERL IDGRDASSIL TFYTKSSVDQ YKDMAANEPN KLWDIVTGDA EEE //