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   27-MAR-2024, entry version 127.
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; Bacteroidota; 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; 226186-BT_3698; -.
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   OrthoDB; 9805159at2; -.
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   CDD; cd11316; AmyAc_bac2_AmyA; 1.
DR   CDD; cd12961; CBM58_SusG; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 2.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 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   InterPro; IPR048755; SusG_CBM58.
DR   PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR10357:SF179; NEUTRAL AND BASIC AMINO ACID TRANSPORT PROTEIN RBAT; 1.
DR   Pfam; PF00128; Alpha-amylase; 2.
DR   Pfam; PF20756; CBM58; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 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
//