DEXT_STRDO
ID DEXT_STRDO Reviewed; 1337 AA.
AC P39653;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Dextranase;
DE EC=3.2.1.11;
DE AltName: Full=Alpha-1,6-glucan-6-glucanohydrolase;
DE Flags: Precursor;
GN Name=dex;
OS Streptococcus downei (Streptococcus sobrinus).
OG Plasmid pYA902.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1317;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 31-36.
RC STRAIN=6715 / UAB66;
RX PubMed=8021165; DOI=10.1128/jb.176.13.3839-3850.1994;
RA Wanda S.-Y., Curtiss R. III;
RT "Purification and characterization of Streptococcus sobrinus dextranase
RT produced in recombinant Escherichia coli and sequence analysis of the
RT dextranase gene.";
RL J. Bacteriol. 176:3839-3850(1994).
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5.3.;
CC Temperature dependence:
CC Optimum temperature is 39 degrees Celsius.;
CC -!- SUBUNIT: Homodimer.
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}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-5 is the initiator.
CC {ECO:0000305}.
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DR EMBL; M96978; AAA21772.1; -; Genomic_DNA.
DR AlphaFoldDB; P39653; -.
DR SMR; P39653; -.
DR CAZy; GH66; Glycoside Hydrolase Family 66.
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 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 Cell wall; Direct protein sequencing; Glycosidase; Hydrolase;
KW Peptidoglycan-anchor; Plasmid; Repeat; Secreted; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000269|PubMed:8021165"
FT CHAIN 31..1308
FT /note="Dextranase"
FT /id="PRO_0000012236"
FT PROPEP 1309..1337
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000012237"
FT REGION 52..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 806..1310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1305..1309
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 806..829
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 845..865
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 896..1040
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1087..1104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1120..1142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1151..1178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1194..1208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1216..1263
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1274..1304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1308
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ SEQUENCE 1337 AA; 143298 MW; B494275A77A2E3D0 CRC64;
MNNRMLSFPS MLFLLAFGIV LSVSAGTTHA DELANQTAKV ADEASIVVST SQAAVEQTQS
QEKEISPAME EDTSNLSLKP NAQQESQSPD SSTELQDPAE QTPPETSDAS APATTSADSV
EKYAQDATQN QSSTSNGPGV IRATSAQVTA TRSVVSSQSG DAIVDLSADK ASYRQGEDVN
LSVDFKNTTD KEQDVTVYAD VYYIDNKLGT YKFSKHLKAG EGYKMQSGDL KIPASQFENN
HGYLLKVRVR DADNNTLSEV NKAIAVESDW TKFPRYGIVG GSQDTNNSLL SKDADRYRAE
IEKMKNMNIN SYFFYDVYKT ATNPFPSDEA TFKQDWNTWS GSEIDTQAVK DIVNQVHDGG
AVAMLYNMIL AENTNTGEAP VLPETEYAYN SDDRGYGAQG QPMSYTVKIP KDGQEEDVEI
QRYYNPTSKL WQDYIADKMG QAMKNGGFDG WQGDTIGDNE VYSYADKDSN DPSKKFWLTE
GYAEFLRAIK EKLPNYYLTV NDVNGEQIYR LKDGNQDVIY NEIWPFGPAL PSEMAAVKPN
TVTSRPVLTK VRQGDWKISI VGAYMEGSEN GGSKADAEAG KSLQTDAVLL TSASIAAAGG
YHMSLAALAN QQDETDGGQG IGVLQTAYYP TQSLKTSSEL TRKNNDYQQF ITAYENVLRD
GVENDDAQVN TFDSNGQKLS TDAKGITGNQ VWTYGKKGDN FRTVQLLNLM GINSDWKNED
GSAANKTPDE QTNLTVKYAL GDVSMEDAQR MANQTYVTSP DDWSKSNLQK VSASVKTDEN
GKPVLVINVP KLTLWDVVYI SNANQESAPE ADQAQTPAAQ SSDDKVAENE TSQPAAEDAK
EQTSEPAQDQ AAPAEQGQAI NQAESPATEP EAEVTPATAE PAKVDAPEAN QAADQAVSPE
PASQEQAASQ SQPEANQTPA SNETPATQGN SEQPELNEPT AQTQPSSQVS PANTSVTPVA
EQPTNQGQAA DKADQAPTNS TSTPESTSPV EPAATDQSSD TPIVTAGNLS VQPAETETPT
VPDKQGDSKA NQSSTETPVA DQVPAVAEQP QATEPNQAKP SVDKAAAPEA LSLIQLKQQT
PAIQAKEADD PEVDETKSEV TPDSGTDKAP EAGQVDSDKA PTVKPSTPEN NDNQPNNAND
ADKNKTNEAD SNKANQDSTK GSSADQSGKS TTPEDGPDNS SPEDPETKPS DPNTDTSDQE
QVKPSLPVVP NQTVDDPKTD DTDTPANTDS AKSKKVADAD KNKVATDSEG RQKSSEFPKE
ATDLEKVGQP ASPQVAGVKS SVATSPEKKS EPVSKTSTTS SSDKLPKTGD HKTVVLIIVL
GLVFVGMTGL LARHEKK
