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
//