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Database: UniProt
Entry: K6TC06_9CLOT
LinkDB: K6TC06_9CLOT
Original site: K6TC06_9CLOT 
ID   K6TC06_9CLOT            Unreviewed;      1629 AA.
AC   K6TC06;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   SubName: Full=Putative cell wall binding protein {ECO:0000313|EMBL:EKQ57478.1};
GN   ORFNames=A370_00851 {ECO:0000313|EMBL:EKQ57478.1};
OS   Clostridium sp. Maddingley MBC34-26.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1196322 {ECO:0000313|EMBL:EKQ57478.1, ECO:0000313|Proteomes:UP000001325};
RN   [1] {ECO:0000313|EMBL:EKQ57478.1, ECO:0000313|Proteomes:UP000001325}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Maddingley MBC34-26 {ECO:0000313|Proteomes:UP000001325};
RX   PubMed=23405323;
RA   Rosewarne C.P., Greenfield P., Li D., Tran-Dinh N., Bradbury M.I.,
RA   Midgley D.J., Hendry P.;
RT   "Draft Genome Sequence of Clostridium sp. Maddingley, Isolated from Coal-
RT   Seam Gas Formation Water.";
RL   Genome Announc. 1:E00081-12(2013).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC       {ECO:0000256|ARBA:ARBA00008061, ECO:0000256|RuleBase:RU003615}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EKQ57478.1}.
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DR   EMBL; ALXI01000021; EKQ57478.1; -; Genomic_DNA.
DR   STRING; 1196322.A370_00851; -.
DR   PATRIC; fig|1196322.3.peg.831; -.
DR   eggNOG; COG0366; Bacteria.
DR   eggNOG; COG1501; Bacteria.
DR   eggNOG; COG5263; Bacteria.
DR   Proteomes; UP000001325; Unassembled WGS sequence.
DR   GO; GO:0004556; F:alpha-amylase activity; IEA:InterPro.
DR   GO; GO:0043169; F:cation binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd11315; AmyAc_bac1_AmyA; 1.
DR   Gene3D; 2.10.270.10; Cholin Binding; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 6.
DR   InterPro; IPR006046; Alpha_amylase.
DR   InterPro; IPR031965; CBM26.
DR   InterPro; IPR018337; Cell_wall/Cho-bd_repeat.
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   PANTHER; PTHR43447; ALPHA-AMYLASE; 1.
DR   PANTHER; PTHR43447:SF7; ALPHA-AMYLASE 2-RELATED; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF16738; CBM26; 6.
DR   Pfam; PF01473; Choline_bind_1; 1.
DR   Pfam; PF19127; Choline_bind_3; 1.
DR   PRINTS; PR00110; ALPHAAMYLASE.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF69360; Cell wall binding repeat; 1.
DR   PROSITE; PS51170; CW; 3.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001325};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          50..408
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   REPEAT          1550..1569
FT                   /note="Cell wall-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT   REPEAT          1570..1590
FT                   /note="Cell wall-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT   REPEAT          1591..1610
FT                   /note="Cell wall-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT   REGION          1317..1349
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1317..1338
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1629 AA;  175383 MW;  F86AF6FD0679D8AD CRC64;
     MQRNHRSFKS IIAITLVLSI IITCGPNTVI AKAEDNNSVI TRLTTAEKQG VILHAWDWSF
     NNVTANLDAI KAAGYTEIQV SPIQVNKDLN DEYTTSDKWW ILYQPAGFQI GNKQLGTEDE
     FKAMCAAAKA KGIKIIVDTI VNHMGNNGDP DIPAEEVADL DPDLSLANHP DMWHVDSNGK
     LNVISDYNNR YDVTHNGVGL PDLNTANPLL QEKIKLYLQK CLDDGAAGFR FDTAKHVELP
     IDPDNVKSDF WPNVLSGLHT ADGNTPFIYG EVLQGGADNI AGYAKYFNVT ASKYGADIRS
     TVGVGTSGPN LSGNIDKLKS YDVPSGIDNT EIVTWVESHD TYANDSSEST PMTDEQIKNG
     WAIVASRENS TPLFFDRPAG RKKLQGNIGD AGSDTWKDPD VVAINKFHTA MDGQDESLIK
     LSDNVLMIER GTSSGASKKG VVIVNLDSIP YQLPAGQAIN LEDGIYTNCA PVGGTFTVAS
     GQISGTVPSG ITVLYADGIP EQPVITPKVS IDKEDCSFAD KLDLTLHVTS AASATYSIDG
     APQGSYADGQ TITIGESAAA GATIKVVVSA TSSDGKTASE TYTYIKRDPN AKTVVYFTKP
     AGWQLPYAYV YNDLKENYNN EAWPGTKMVK IGDNLYKLEI SGFTNGQVIF NDWFYGSHQT
     SAFTIAPSES VEKKLYDTDG TWKDTTATFD NGTTLPDDGV TNGTAKVYFQ KPSTAEWAYN
     DVNIYFYGKG GPSWPGVPMT KVSDNLYTYT LPAGLEGSNV IFNANAGKIQ VPGSGESGLT
     APANTSMILA DGVWKEYTKG VSKAYFRKPS DWAEPNIYVF NDQGVKVSEW PGVKMDKVAG
     TETLYSYTLP ENFGDAKIIF NDKIAGNDSG NQTADLVLPF ETSKIYDETT KTLRDFTLDD
     LQEPEKPSTD AQGVTKVYFK NTFGWEKVNV YAYNDGSSDK VKDWPGASAV DEGNGLYSYT
     LPKGFESATV IFNNGGKGKQ TNNLPTKVGS TMEFVSDGTE TDGKLNGELV SKSKVYFKNT
     SGWSSVKIYY WVDANNNGWP GSSMVDEGDN LYSFVMPDGF ENANVIFNNN GKGKQSPDKQ
     AQAGKTLILD GDTWREFTEA DIPGANTKPT NPGDNEEVGS TVYVKVPSGW NGIPNIHYWN
     TAGGTTTWPG VAMKDEGNGI YSAAIPKSFG DVSIIINDGS NKLADKDGNT EFTVKLGSTI
     IFEDGAWKDY VKPTPDPGAQ EVSKTPIVDG IIYTGTTTVK GTAGANADVV LGIDEDNVTT
     SAAVQCTTSA GAQYVIGTSK SDENGNWLVQ IPAQSKGTVI KITAKEEGKL EASITVTVQE
     KPSSSSGSSS GSDSGSSYSH SSHRKEKTVT VDGNSTIIKS SDASVIIDGI VNANTSNIVV
     KLSSSQSVAM KSIFEALLSK PDKTLTLVQG NVSLTFKGTD LLANGAADLD TTIQSISSNA
     SAINNLTNGA EIIDLSFAYK GAFPGKATIT TDVNSKYNNK LMYVYSYNAA NNRLTLVSLN
     VPVQNGEVSF TASKGSDYVL SEKPITGAVT EGWNKITDGN WIYVKDENNV AGWIYDGGNW
     YLTNESGIMQ KGWSKDRNGK WYYLNSAGAM QTGWLNDNGT WYYLSTSGDM LSDTTIDGYT
     LGVDGAWIA
//
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