ANCA_ACET2
ID ANCA_ACET2 Reviewed; 447 AA.
AC Q06848; A3DJZ7;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Cellulosome-anchoring protein;
DE Flags: Precursor;
GN Name=ancA; OrderedLocusNames=Cthe_3080;
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 [GENOMIC DNA].
RX PubMed=8458832; DOI=10.1128/jb.175.7.1891-1899.1993;
RA Fujino T., Beguin P., Aubert J.-P.;
RT "Organization of a Clostridium thermocellum gene cluster encoding the
RT cellulosomal scaffolding protein CipA and a protein possibly involved in
RT attachment of the cellulosome to the cell surface.";
RL J. Bacteriol. 175:1891-1899(1993).
RN [2]
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.
CC -!- FUNCTION: Anchors the cellulosome to the cell surface by binding the
CC duplicated segment that is present at the C-terminal end of CipA.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall, S-layer.
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DR EMBL; X67506; CAA47843.1; -; Genomic_DNA.
DR EMBL; CP000568; ABN54276.1; -; Genomic_DNA.
DR PIR; T18264; T18264.
DR RefSeq; WP_003511554.1; NC_009012.1.
DR PDB; 3UL4; X-ray; 1.95 A; A=30-175.
DR PDBsum; 3UL4; -.
DR AlphaFoldDB; Q06848; -.
DR SMR; Q06848; -.
DR STRING; 203119.Cthe_3080; -.
DR EnsemblBacteria; ABN54276; ABN54276; Cthe_3080.
DR KEGG; cth:Cthe_3080; -.
DR eggNOG; COG1361; Bacteria.
DR HOGENOM; CLU_623622_0_0_9; -.
DR OMA; TINAFTF; -.
DR OrthoDB; 309336at2; -.
DR Proteomes; UP000002145; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0030115; C:S-layer; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR002102; Cohesin_dom.
DR InterPro; IPR001119; SLH_dom.
DR Pfam; PF00963; Cohesin; 1.
DR Pfam; PF00395; SLH; 3.
DR SUPFAM; SSF49384; SSF49384; 1.
DR PROSITE; PS51272; SLH; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cell wall; Cellulose degradation;
KW Polysaccharide degradation; Reference proteome; Repeat; S-layer; Secreted;
KW Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..447
FT /note="Cellulosome-anchoring protein"
FT /id="PRO_0000032636"
FT DOMAIN 30..180
FT /note="Cohesin"
FT DOMAIN 216..280
FT /note="SLH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00777"
FT DOMAIN 281..344
FT /note="SLH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00777"
FT DOMAIN 345..408
FT /note="SLH 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00777"
FT DOMAIN 409..429
FT /note="SLH 4; truncated"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00777"
FT REGION 30..180
FT /note="Receptor binding site for duplicated segment of
FT CipA"
FT /evidence="ECO:0000255"
FT REGION 177..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:3UL4"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:3UL4"
FT STRAND 48..57
FT /evidence="ECO:0007829|PDB:3UL4"
FT STRAND 63..71
FT /evidence="ECO:0007829|PDB:3UL4"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:3UL4"
FT STRAND 77..84
FT /evidence="ECO:0007829|PDB:3UL4"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:3UL4"
FT HELIX 91..94
FT /evidence="ECO:0007829|PDB:3UL4"
FT STRAND 95..100
FT /evidence="ECO:0007829|PDB:3UL4"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:3UL4"
FT STRAND 105..111
FT /evidence="ECO:0007829|PDB:3UL4"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:3UL4"
FT STRAND 125..134
FT /evidence="ECO:0007829|PDB:3UL4"
FT STRAND 140..155
FT /evidence="ECO:0007829|PDB:3UL4"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:3UL4"
FT STRAND 168..172
FT /evidence="ECO:0007829|PDB:3UL4"
SQ SEQUENCE 447 AA; 48530 MW; 0FD674134ABB8FE1 CRC64;
MKRIKRILAV LTIFALLATI NAFTFVSLAQ TNTIEIIIGN VKARPGDRIE VPVSLKNVPD
KGIVSSDFVI EYDSKLFKVI ELKAGDIVEN PSESFSYNVV EKDEIIAVLY LEETGLGIEA
IRTDGVFFTI VMEVSKDVKP GISPIKFESF GATADNDMNE MTPKLVEGKV EIIEASAPEA
TPTPGSTAGS GAGGGTGSSG SGQPSATPTP TATEKPSTTP KTTEQPHEDI PQSGGTGEHA
PFLKGYPGGL FKPENNITRA EAAVIFAKLL GADENSAGKN SSITFKDLKD SHWAAWAIKY
VTEQNLFGGY PDGTFMPDKS ITRAEFATVT YKFLEKLGKI EQGTDVKTQL KDIEGHWAQK
YIETLVAKGY IKGYPDETFR PQASIKRAES VALINRSLER GPLNGAVLEF TDVPVNYWAY
KDIAEGVIYH SYKIDENGQE VMVEKLD
