SUSG_BACTN
ID SUSG_BACTN Reviewed; 692 AA.
AC Q8A1G3; Q45772;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Alpha-amylase SusG;
DE EC=3.2.1.1 {ECO:0000269|PubMed:20159465};
DE AltName: Full=Starch-utilization system protein G;
DE Flags: Precursor;
GN Name=susG; OrderedLocusNames=BT_3698;
OS Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=226186;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50;
RX PubMed=9006015; DOI=10.1128/jb.179.3.643-649.1997;
RA Reeves A.R., Wang G.R., Salyers A.A.;
RT "Characterization of four outer membrane proteins that play a role in
RT utilization of starch by Bacteroides thetaiotaomicron.";
RL J. Bacteriol. 179:643-649(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50;
RX PubMed=12663928; DOI=10.1126/science.1080029;
RA Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA Hooper L.V., Gordon J.I.;
RT "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL Science 299:2074-2076(2003).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50;
RX PubMed=10572122; DOI=10.1128/jb.181.23.7206-7211.1999;
RA Shipman J.A., Cho K.H., Siegel H.A., Salyers A.A.;
RT "Physiological characterization of SusG, an outer membrane protein
RT essential for starch utilization by Bacteroides thetaiotaomicron.";
RL J. Bacteriol. 181:7206-7211(1999).
RN [4]
RP FUNCTION.
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50;
RX PubMed=11717282; DOI=10.1128/jb.183.24.7224-7230.2001;
RA Cho K.H., Salyers A.A.;
RT "Biochemical analysis of interactions between outer membrane proteins that
RT contribute to starch utilization by Bacteroides thetaiotaomicron.";
RL J. Bacteriol. 183:7224-7230(2001).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 24-692 IN COMPLEXES WITH
RP MALTOOLIGOSACCHARIDE; CALCIUM AND MAGNESIUM, COFACTOR, SUBUNIT, FUNCTION,
RP CATALYTIC ACTIVITY, AND MUTAGENESIS OF TRP-460; TYR-469; ASP-473 AND
RP ASP-498.
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50;
RX PubMed=20159465; DOI=10.1016/j.str.2009.12.010;
RA Koropatkin N.M., Smith T.J.;
RT "SusG: a unique cell-membrane-associated alpha-amylase from a prominent
RT human gut symbiont targets complex starch molecules.";
RL Structure 18:200-215(2010).
CC -!- FUNCTION: Alpha-amylase that cleaves starch into oligosaccharides
CC before internalization for degradation, the first step in starch
CC degradation. {ECO:0000269|PubMed:10572122, ECO:0000269|PubMed:11717282,
CC ECO:0000269|PubMed:20159465}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in
CC polysaccharides containing three or more (1->4)-alpha-linked D-
CC glucose units.; EC=3.2.1.1; Evidence={ECO:0000269|PubMed:20159465};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:20159465};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:20159465};
CC -!- PATHWAY: Glycan degradation; starch degradation.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:20159465}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane
CC {ECO:0000269|PubMed:10572122}; Lipid-anchor {ECO:0000255|PROSITE-
CC ProRule:PRU00303, ECO:0000269|PubMed:10572122}.
CC -!- INDUCTION: By maltose. {ECO:0000269|PubMed:9006015}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR EMBL; L77732; AAB42174.1; -; Genomic_DNA.
DR EMBL; AE015928; AAO78803.1; -; Genomic_DNA.
DR RefSeq; NP_812609.1; NC_004663.1.
DR RefSeq; WP_011108937.1; NC_004663.1.
DR PDB; 3K8K; X-ray; 2.20 A; A/B=24-692.
DR PDB; 3K8L; X-ray; 2.30 A; A/B=24-692.
DR PDB; 3K8M; X-ray; 2.50 A; A/B=24-692.
DR PDB; 6BS6; X-ray; 2.17 A; A/B=24-692.
DR PDBsum; 3K8K; -.
DR PDBsum; 3K8L; -.
DR PDBsum; 3K8M; -.
DR PDBsum; 6BS6; -.
DR AlphaFoldDB; Q8A1G3; -.
DR SMR; Q8A1G3; -.
DR STRING; 226186.BT_3698; -.
DR CAZy; CBM58; Carbohydrate-Binding Module Family 58.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR TCDB; 8.A.9.1.3; the rbat transport accessory protein (rbat) family.
DR PaxDb; Q8A1G3; -.
DR PRIDE; Q8A1G3; -.
DR DNASU; 1072061; -.
DR EnsemblBacteria; AAO78803; AAO78803; BT_3698.
DR GeneID; 60924867; -.
DR KEGG; bth:BT_3698; -.
DR PATRIC; fig|226186.12.peg.3758; -.
DR eggNOG; COG0366; Bacteria.
DR HOGENOM; CLU_006462_2_4_10; -.
DR InParanoid; Q8A1G3; -.
DR OMA; YRSDYIE; -.
DR BRENDA; 3.2.1.1; 709.
DR UniPathway; UPA00153; -.
DR EvolutionaryTrace; Q8A1G3; -.
DR Proteomes; UP000001414; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019867; C:outer membrane; IDA:MENGO.
DR GO; GO:0004556; F:alpha-amylase activity; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:2001070; F:starch binding; IDA:UniProtKB.
DR GO; GO:0009313; P:oligosaccharide catabolic process; IBA:GO_Central.
DR GO; GO:0005983; P:starch catabolic process; IDA:UniProtKB.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 2.60.40.1180; -; 1.
DR Gene3D; 3.90.400.10; -; 1.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR045857; O16G_dom_2.
DR Pfam; PF00128; Alpha-amylase; 2.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Carbohydrate metabolism; Cell outer membrane;
KW Glycosidase; Hydrolase; Lipoprotein; Magnesium; Membrane; Metal-binding;
KW Palmitate; Polysaccharide degradation; Reference proteome; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 23..692
FT /note="Alpha-amylase SusG"
FT /id="PRO_0000425887"
FT REGION 154
FT /note="Starch binding"
FT /evidence="ECO:0000305|PubMed:20159465"
FT REGION 260..263
FT /note="Starch binding"
FT /evidence="ECO:0000305|PubMed:20159465"
FT REGION 330..333
FT /note="Starch binding"
FT /evidence="ECO:0000305|PubMed:20159465"
FT REGION 386..392
FT /note="Starch binding"
FT /evidence="ECO:0000305|PubMed:20159465"
FT REGION 437
FT /note="Starch binding"
FT /evidence="ECO:0000305|PubMed:20159465"
FT REGION 457
FT /note="Starch binding"
FT /evidence="ECO:0000305|PubMed:20159465"
FT ACT_SITE 388
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 431
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 73
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:20159465"
FT BINDING 75
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:20159465"
FT BINDING 77
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:20159465"
FT BINDING 79
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:20159465"
FT BINDING 81
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:20159465"
FT BINDING 153
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:20159465"
FT BINDING 352
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:20159465"
FT BINDING 392
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:20159465"
FT SITE 304
FT /note="Starch"
FT /evidence="ECO:0000305|PubMed:20159465"
FT SITE 472..473
FT /note="Starch"
FT /evidence="ECO:0000305|PubMed:20159465"
FT SITE 498
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000305|PubMed:20159465"
FT SITE 545
FT /note="Starch"
FT /evidence="ECO:0000305|PubMed:20159465"
FT SITE 549
FT /note="Starch"
FT /evidence="ECO:0000305|PubMed:20159465"
FT LIPID 23
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 23
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT MUTAGEN 460
FT /note="W->A: Slight reduction in catalytic activity, while
FT it does not affect the catalytic turnover rate; when
FT associated with A-469 and V-473."
FT /evidence="ECO:0000269|PubMed:20159465"
FT MUTAGEN 469
FT /note="Y->A: Slight reduction in catalytic activity, while
FT it does not affect the catalytic turnover rate; when
FT associated with A-460 and V-473."
FT /evidence="ECO:0000269|PubMed:20159465"
FT MUTAGEN 473
FT /note="D->V: Slight reduction in catalytic activity, while
FT it does not affect the catalytic turnover rate; when
FT associated with A-460 and A-469."
FT /evidence="ECO:0000269|PubMed:20159465"
FT MUTAGEN 498
FT /note="D->N: Abolishes alpha-amylase activity."
FT /evidence="ECO:0000269|PubMed:20159465"
FT CONFLICT 456
FT /note="Y -> N (in Ref. 1; AAB42174)"
FT /evidence="ECO:0000305"
FT CONFLICT 465
FT /note="S -> R (in Ref. 1; AAB42174)"
FT /evidence="ECO:0000305"
FT CONFLICT 579
FT /note="D -> H (in Ref. 1; AAB42174)"
FT /evidence="ECO:0000305"
FT CONFLICT 607
FT /note="G -> A (in Ref. 1; AAB42174)"
FT /evidence="ECO:0000305"
FT CONFLICT 685
FT /note="S -> C (in Ref. 1; AAB42174)"
FT /evidence="ECO:0000305"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:6BS6"
FT HELIX 68..71
FT /evidence="ECO:0007829|PDB:6BS6"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:6BS6"
FT HELIX 82..87
FT /evidence="ECO:0007829|PDB:6BS6"
FT HELIX 89..94
FT /evidence="ECO:0007829|PDB:6BS6"
FT STRAND 98..102
FT /evidence="ECO:0007829|PDB:6BS6"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:6BS6"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:6BS6"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:6BS6"
FT HELIX 129..141
FT /evidence="ECO:0007829|PDB:6BS6"
FT STRAND 145..150
FT /evidence="ECO:0007829|PDB:6BS6"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:6BS6"
FT HELIX 160..165
FT /evidence="ECO:0007829|PDB:6BS6"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:6BS6"
FT STRAND 179..182
FT /evidence="ECO:0007829|PDB:6BS6"
FT HELIX 183..188
FT /evidence="ECO:0007829|PDB:6BS6"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:3K8M"
FT HELIX 199..202
FT /evidence="ECO:0007829|PDB:6BS6"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:6BS6"
FT STRAND 208..211
FT /evidence="ECO:0007829|PDB:6BS6"
FT STRAND 218..227
FT /evidence="ECO:0007829|PDB:6BS6"
FT TURN 229..232
FT /evidence="ECO:0007829|PDB:3K8K"
FT STRAND 235..240
FT /evidence="ECO:0007829|PDB:6BS6"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:6BS6"
FT TURN 262..264
FT /evidence="ECO:0007829|PDB:6BS6"
FT STRAND 265..268
FT /evidence="ECO:0007829|PDB:6BS6"
FT STRAND 270..273
FT /evidence="ECO:0007829|PDB:3K8K"
FT STRAND 276..287
FT /evidence="ECO:0007829|PDB:6BS6"
FT STRAND 289..293
FT /evidence="ECO:0007829|PDB:6BS6"
FT STRAND 296..298
FT /evidence="ECO:0007829|PDB:6BS6"
FT STRAND 304..309
FT /evidence="ECO:0007829|PDB:6BS6"
FT STRAND 325..327
FT /evidence="ECO:0007829|PDB:6BS6"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:6BS6"
FT STRAND 340..342
FT /evidence="ECO:0007829|PDB:6BS6"
FT STRAND 350..353
FT /evidence="ECO:0007829|PDB:6BS6"
FT HELIX 358..363
FT /evidence="ECO:0007829|PDB:6BS6"
FT HELIX 365..378
FT /evidence="ECO:0007829|PDB:6BS6"
FT TURN 379..381
FT /evidence="ECO:0007829|PDB:6BS6"
FT STRAND 384..387
FT /evidence="ECO:0007829|PDB:6BS6"
FT HELIX 390..392
FT /evidence="ECO:0007829|PDB:6BS6"
FT STRAND 393..395
FT /evidence="ECO:0007829|PDB:6BS6"
FT STRAND 397..400
FT /evidence="ECO:0007829|PDB:6BS6"
FT HELIX 401..419
FT /evidence="ECO:0007829|PDB:6BS6"
FT STRAND 427..430
FT /evidence="ECO:0007829|PDB:6BS6"
FT HELIX 436..439
FT /evidence="ECO:0007829|PDB:6BS6"
FT HELIX 440..444
FT /evidence="ECO:0007829|PDB:6BS6"
FT STRAND 447..450
FT /evidence="ECO:0007829|PDB:6BS6"
FT HELIX 452..463
FT /evidence="ECO:0007829|PDB:6BS6"
FT HELIX 470..484
FT /evidence="ECO:0007829|PDB:6BS6"
FT STRAND 489..491
FT /evidence="ECO:0007829|PDB:6BS6"
FT HELIX 502..505
FT /evidence="ECO:0007829|PDB:6BS6"
FT TURN 506..508
FT /evidence="ECO:0007829|PDB:6BS6"
FT HELIX 510..522
FT /evidence="ECO:0007829|PDB:6BS6"
FT STRAND 523..525
FT /evidence="ECO:0007829|PDB:6BS6"
FT STRAND 528..530
FT /evidence="ECO:0007829|PDB:6BS6"
FT TURN 531..536
FT /evidence="ECO:0007829|PDB:6BS6"
FT HELIX 545..548
FT /evidence="ECO:0007829|PDB:6BS6"
FT HELIX 570..573
FT /evidence="ECO:0007829|PDB:6BS6"
FT HELIX 577..582
FT /evidence="ECO:0007829|PDB:6BS6"
FT HELIX 587..600
FT /evidence="ECO:0007829|PDB:6BS6"
FT HELIX 602..605
FT /evidence="ECO:0007829|PDB:6BS6"
FT STRAND 608..611
FT /evidence="ECO:0007829|PDB:6BS6"
FT STRAND 613..616
FT /evidence="ECO:0007829|PDB:6BS6"
FT HELIX 617..619
FT /evidence="ECO:0007829|PDB:6BS6"
FT TURN 620..622
FT /evidence="ECO:0007829|PDB:6BS6"
FT STRAND 626..633
FT /evidence="ECO:0007829|PDB:6BS6"
FT STRAND 636..643
FT /evidence="ECO:0007829|PDB:6BS6"
FT STRAND 645..647
FT /evidence="ECO:0007829|PDB:6BS6"
FT STRAND 649..653
FT /evidence="ECO:0007829|PDB:6BS6"
FT STRAND 657..670
FT /evidence="ECO:0007829|PDB:6BS6"
FT HELIX 672..674
FT /evidence="ECO:0007829|PDB:3K8K"
FT STRAND 676..680
FT /evidence="ECO:0007829|PDB:6BS6"
FT STRAND 685..690
FT /evidence="ECO:0007829|PDB:6BS6"
SQ SEQUENCE 692 AA; 77959 MW; EB7EC2281844B0F9 CRC64;
MNKHLHFLSL LWLSMLMAFM TACSDDKNIT DPAPEPEPPV EGQWTALTAS PDTWDETKRA
DISYQLLLYS FADSDGDGYG DLNGVTQKLD YLNQLGVKAL WLSPIHPCMS YHGYDVTDYT
KVNPQLGTES DFDRLVTEAH NRGIKIYLDY VMNHTGTAHP WFTEASSSSE SPYRNYYSFS
EDPKTDIAAG KIAMITQEGA AGYNAAEWFQ VSDETAAVKG LLKFTLDWSN APSPILVVST
GTKADEDNPD TGTDNAKYLY YGEDICKKFY DKGNNIYELT VDFESTWGLL IRTSNASFWP
SGTKYGASSS SEKLALNKDF KLTNAGNPAN IMFDSQQITY FHSHFCTDWF ADLNYGPVDQ
AGESPAYQAI ADAAKGWIAR GVDGLRLDAV KHIYHSETSE ENPRFLKMFY EDMNAYYKQK
GHTDDFYMIG EVLSEYDKVA PYYKGLPALF EFSFWYRLEW GINNSTGCYF AKDILSYQQK
YANYRSDYIE ATKLSNHDED RTSSKLGKSA DKCKLAAAVL LTSAGHPYIY YGEELGLYGT
KDNGDEYVRS PMLWGDSYTT NYTDKTDATV SKNVKTVADQ QADTHSLLNI YFSLTRLRNT
YPALAEGNMT KHSVYNESQE KDYKPIAAWY MTKDNEKLLV IHNFGGTAMQ LPLTDKIEKV
LFVNGETQQN TDSDSYTLKL GGYASVVFKL GN
