DEXT_STRMU
ID DEXT_STRMU Reviewed; 850 AA.
AC Q54443;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Dextranase;
DE EC=3.2.1.11;
DE AltName: Full=Alpha-1,6-glucan-6-glucanohydrolase;
DE Flags: Precursor;
GN Name=dexA; OrderedLocusNames=SMU_2042;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Ingbritt;
RX PubMed=8657012; DOI=10.1111/j.1348-0421.1995.tb03282.x;
RA Igarashi T., Yamamoto A., Goto N.;
RT "Sequence analysis of the Streptococcus mutans Ingbritt dexA gene encoding
RT extracellular dextranase.";
RL Microbiol. Immunol. 39:853-860(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Ingbritt;
RX PubMed=8535521; DOI=10.1099/13500872-141-11-2929;
RA Colby S.M., Whiting G.C., Tao L., Russell R.R.B.;
RT "Insertional inactivation of the Streptococcus mutans dexA (dextranase)
RT gene results in altered adherence and dextran catabolism.";
RL Microbiology 141:2929-2936(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
CC -!- FUNCTION: May play a role in sucrose-independent adherence to the
CC pellicle-coated tooth surface.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->6)-alpha-D-glucosidic linkages in
CC dextran.; EC=3.2.1.11;
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-
CC ProRule:PRU00477}; Peptidoglycan-anchor {ECO:0000255|PROSITE-
CC ProRule:PRU00477}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 66 family. {ECO:0000305}.
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DR EMBL; D49430; BAA08409.1; -; Genomic_DNA.
DR EMBL; AE014133; AAN59642.1; -; Genomic_DNA.
DR RefSeq; NP_722336.1; NC_004350.2.
DR PDB; 3VMN; X-ray; 1.60 A; A=100-732.
DR PDB; 3VMO; X-ray; 1.90 A; A=100-732.
DR PDB; 3VMP; X-ray; 1.88 A; A=100-732.
DR PDBsum; 3VMN; -.
DR PDBsum; 3VMO; -.
DR PDBsum; 3VMP; -.
DR AlphaFoldDB; Q54443; -.
DR SMR; Q54443; -.
DR STRING; 210007.SMU_2042; -.
DR CAZy; GH66; Glycoside Hydrolase Family 66.
DR PRIDE; Q54443; -.
DR EnsemblBacteria; AAN59642; AAN59642; SMU_2042.
DR KEGG; smu:SMU_2042; -.
DR PATRIC; fig|210007.7.peg.1820; -.
DR eggNOG; COG5297; Bacteria.
DR HOGENOM; CLU_321569_0_0_9; -.
DR OMA; KFPRYGF; -.
DR BRENDA; 3.2.1.11; 5941.
DR Proteomes; UP000002512; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0033904; F:dextranase activity; IEA:UniProtKB-EC.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR CDD; cd14745; GH66; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 2.60.40.1180; -; 1.
DR InterPro; IPR025092; Glyco_hydro_66.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR019931; LPXTG_anchor.
DR Pfam; PF13199; Glyco_hydro_66; 1.
DR Pfam; PF00746; Gram_pos_anchor; 1.
DR PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell wall; Glycosidase; Hydrolase; Peptidoglycan-anchor;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..?
FT CHAIN ?..814
FT /note="Dextranase"
FT /id="PRO_0000012238"
FT PROPEP 815..850
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000012239"
FT REGION 1..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 811..815
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 1..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 814
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT CONFLICT 16
FT /note="A -> N (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 22
FT /note="T -> A (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 39
FT /note="V -> A (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 56
FT /note="G -> E (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 67
FT /note="S -> P (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 141
FT /note="A -> V (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 376
FT /note="N -> T (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 504
FT /note="V -> I (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 704
FT /note="A -> T (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 707
FT /note="I -> V (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 776..778
FT /note="VDE -> EDG (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 783
FT /note="I -> L (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 849
FT /note="K -> N (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:3VMN"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:3VMN"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:3VMN"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:3VMN"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:3VMN"
FT STRAND 135..145
FT /evidence="ECO:0007829|PDB:3VMN"
FT STRAND 148..159
FT /evidence="ECO:0007829|PDB:3VMN"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:3VMN"
FT STRAND 171..174
FT /evidence="ECO:0007829|PDB:3VMN"
FT STRAND 181..192
FT /evidence="ECO:0007829|PDB:3VMN"
FT STRAND 198..208
FT /evidence="ECO:0007829|PDB:3VMN"
FT STRAND 218..221
FT /evidence="ECO:0007829|PDB:3VMN"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:3VMN"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:3VMN"
FT HELIX 236..248
FT /evidence="ECO:0007829|PDB:3VMN"
FT STRAND 253..256
FT /evidence="ECO:0007829|PDB:3VMN"
FT STRAND 269..274
FT /evidence="ECO:0007829|PDB:3VMN"
FT TURN 279..281
FT /evidence="ECO:0007829|PDB:3VMN"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:3VMN"
FT HELIX 287..299
FT /evidence="ECO:0007829|PDB:3VMN"
FT STRAND 303..314
FT /evidence="ECO:0007829|PDB:3VMN"
FT HELIX 323..325
FT /evidence="ECO:0007829|PDB:3VMN"
FT STRAND 328..333
FT /evidence="ECO:0007829|PDB:3VMN"
FT STRAND 343..346
FT /evidence="ECO:0007829|PDB:3VMN"
FT STRAND 349..355
FT /evidence="ECO:0007829|PDB:3VMN"
FT HELIX 360..377
FT /evidence="ECO:0007829|PDB:3VMN"
FT STRAND 381..385
FT /evidence="ECO:0007829|PDB:3VMN"
FT STRAND 391..393
FT /evidence="ECO:0007829|PDB:3VMN"
FT HELIX 395..397
FT /evidence="ECO:0007829|PDB:3VMN"
FT HELIX 403..405
FT /evidence="ECO:0007829|PDB:3VMN"
FT HELIX 409..411
FT /evidence="ECO:0007829|PDB:3VMN"
FT HELIX 413..423
FT /evidence="ECO:0007829|PDB:3VMN"
FT STRAND 427..431
FT /evidence="ECO:0007829|PDB:3VMN"
FT HELIX 434..436
FT /evidence="ECO:0007829|PDB:3VMN"
FT HELIX 439..442
FT /evidence="ECO:0007829|PDB:3VMN"
FT STRAND 448..453
FT /evidence="ECO:0007829|PDB:3VMN"
FT STRAND 458..460
FT /evidence="ECO:0007829|PDB:3VMO"
FT STRAND 463..467
FT /evidence="ECO:0007829|PDB:3VMN"
FT HELIX 470..484
FT /evidence="ECO:0007829|PDB:3VMN"
FT STRAND 488..491
FT /evidence="ECO:0007829|PDB:3VMN"
FT STRAND 505..507
FT /evidence="ECO:0007829|PDB:3VMN"
FT HELIX 508..514
FT /evidence="ECO:0007829|PDB:3VMN"
FT HELIX 521..534
FT /evidence="ECO:0007829|PDB:3VMN"
FT STRAND 537..539
FT /evidence="ECO:0007829|PDB:3VMN"
FT STRAND 541..543
FT /evidence="ECO:0007829|PDB:3VMN"
FT HELIX 547..549
FT /evidence="ECO:0007829|PDB:3VMN"
FT STRAND 558..560
FT /evidence="ECO:0007829|PDB:3VMN"
FT HELIX 570..585
FT /evidence="ECO:0007829|PDB:3VMN"
FT HELIX 587..591
FT /evidence="ECO:0007829|PDB:3VMN"
FT STRAND 602..604
FT /evidence="ECO:0007829|PDB:3VMN"
FT STRAND 621..629
FT /evidence="ECO:0007829|PDB:3VMN"
FT STRAND 631..640
FT /evidence="ECO:0007829|PDB:3VMN"
FT STRAND 647..649
FT /evidence="ECO:0007829|PDB:3VMN"
FT HELIX 653..655
FT /evidence="ECO:0007829|PDB:3VMN"
FT STRAND 663..671
FT /evidence="ECO:0007829|PDB:3VMN"
FT HELIX 677..684
FT /evidence="ECO:0007829|PDB:3VMN"
FT STRAND 686..690
FT /evidence="ECO:0007829|PDB:3VMN"
FT TURN 694..698
FT /evidence="ECO:0007829|PDB:3VMN"
FT STRAND 700..702
FT /evidence="ECO:0007829|PDB:3VMN"
FT STRAND 705..709
FT /evidence="ECO:0007829|PDB:3VMN"
FT STRAND 715..732
FT /evidence="ECO:0007829|PDB:3VMN"
SQ SEQUENCE 850 AA; 94482 MW; FCF3E7DF7B4EA178 CRC64;
MEQSNRQTAE PAIRSAETVD STINSFQETD LKVQEKEDVA AAVQTESASI DSNEQGQSVS
ANTNTQSQAK KLSNNSHQEP MQMVSAANKE RAVLETAQNQ KNGNMINLTT DKAVYQAGEA
VHLNLTLNNT TSLAQNITAT AEVYSLENKL KTLQYTKYLL PNESYTTQKG EFVIPANSLA
NNRGYLLKVN ISDSQNNILE QGNRAIAVED DWRTFPRYAA IGGSQKDNNS VLTKNLPDYY
RELEQMKNMN INSYFFYDVY KSATNPFPNV PKFDQSWNWW SHSQVETDAV KALVNRVHQT
GAVAMLYNMI LAQNANETAV LPDTEYIYNY ETGGYGQNGQ VMTYSIDDKP LQYYYNPLSK
SWQNYISNAM AQAMKNGGFD GWQGDTIGDN RVLSHNQKDS RDIAHSFMLS DVYAEFLNKM
KEKLPQYYLT LNDVNGENIS KLANSKQDVI YNELWPFGTS ALGNRPQESY GDLKARVDQV
RQATGKSLIV GAYMEEPKFD DNRVPLNGAA RDVLASATYQ TDAVLLTTAA IAAAGGYHMS
LAALANPNDG GGVGVLETAY YPTQSLKVSK ELNRKNYHYQ QFITAYENLL RDKVENDSAE
PQTFTANGRQ LSQDALGING DQVWTYAKKG NDFRTIQLLN LMGITSDWKN EDGYENNKTP
DEQTNLLVTY PLTGVSMAEA DRIAKQVYLT SPDDWLQSSM ISLATQIKTN ENGDPVLYIQ
VPRLTLWDMI YINETIKPET PKVPEQPQHP ARTLEPAIPQ TPEAVSPLPV ANKQAVDENK
NEIVSALTGE ENDLQLPTLS KRSLSISQAE LPQTGDNNET RSNLLKVIGA GALLIGAAGL
LSLIKGRKKD
