ID A0A1M7PWV8_9BACI Unreviewed; 1723 AA.
AC A0A1M7PWV8;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Concanavalin A-like lectin/glucanases superfamily protein {ECO:0000313|EMBL:SHN22076.1};
GN ORFNames=SAMN05216179_2510 {ECO:0000313|EMBL:SHN22076.1};
OS Gracilibacillus kekensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Gracilibacillus.
OX NCBI_TaxID=1027249 {ECO:0000313|EMBL:SHN22076.1, ECO:0000313|Proteomes:UP000184184};
RN [1] {ECO:0000313|EMBL:SHN22076.1, ECO:0000313|Proteomes:UP000184184}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10681 {ECO:0000313|EMBL:SHN22076.1,
RC ECO:0000313|Proteomes:UP000184184};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865}.
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DR EMBL; FRCZ01000005; SHN22076.1; -; Genomic_DNA.
DR RefSeq; WP_073202193.1; NZ_FRCZ01000005.1.
DR STRING; 1027249.SAMN05216179_2510; -.
DR OrthoDB; 9758923at2; -.
DR Proteomes; UP000184184; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd08983; GH43_Bt3655-like; 1.
DR CDD; cd09004; GH43_bXyl-like; 1.
DR Gene3D; 2.60.120.200; -; 3.
DR Gene3D; 2.60.40.2340; -; 1.
DR InterPro; IPR046780; aBig_2.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR43772:SF2; BETA-1,4-XYLOSIDASE (EUROFUNG); 1.
DR PANTHER; PTHR43772; ENDO-1,4-BETA-XYLANASE; 1.
DR Pfam; PF20578; aBig_2; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR Pfam; PF13385; Laminin_G_3; 3.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 2.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 3.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lectin {ECO:0000313|EMBL:SHN22076.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00022651};
KW Reference proteome {ECO:0000313|Proteomes:UP000184184};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT TRANSMEM 1698..1717
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 477..568
FT /note="Atrophied bacterial Ig"
FT /evidence="ECO:0000259|Pfam:PF20578"
FT REGION 1624..1689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1654..1670
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1194
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 1353
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 1307
FT /note="Important for catalytic activity, responsible for
FT pKa modulation of the active site Glu and correct
FT orientation of both the proton donor and substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-2"
SQ SEQUENCE 1723 AA; 192161 MW; FA946D1944B5E4D0 CRC64;
MLGKKYLALF MIFLIFLSLF PVPATVKANN HSATELIAHY DMTNLENQLI DKTNNGNDAT
IVGFESEDFK EEDNRSILDF TGDKDKYIEL PQGLIIDETF TIETTFSTST AANHWLYTIG
TIEAEWPNVN NYIFLNPKQG NDSIRFGIKD AEDELLFQDG SITSGEYQTV TATFEDELIT
IYINGELAGE LPHTYSVQEI LENGVESGSD IIGYIGKSLY TPDPAFTGKL ADFKVYNDTL
TADEVKHIYL SSTDQLIAHY DMSQEEGNLL DVTNNGNDAP IVGFDQSDFT EENDNAILNF
TGDKSEYVKL PKGLVTDETF TVETTFSTST AANHWLYTLG TMEAEWPNVN NYVFFNPKQG
NDTVRFGIKD AESEELFQEA SIESGEYQTV TATFEDELIT IYINGEEVGN LPHTFSVMDI
LANGVDAETD FIGYIGKSLY TPAPAFTGKL ADFKVYNYTL TAEEIKEMAG LTDQEIVDKA
KNELVIPNAS DIRGNITLPS SSTEGASITW ETDNSDVISV TEEINEGYDN IPPGVVTRQS
TDTFVTLTAT ISYGEIVETK ELEVTVKAAT EIDDYQAYLM THFTGEHDIG EQIYFANSED
GFNWEDLNDG DPVLTSDIGE KGVRDPYIIR SPEGDRFYLN ATDLRIASGK GWGQASTNGS
KSLIIWESSD LVNWSEERIV EVAPSNAGNA WAPEAVYDEA TGEYIVFWAS TTRNENGEYS
EADIYYAKTR DFYSFTEPEV YIDRPGDQHI IDTTIIKDHD MYYRYSADGQ ITIEESQQIL
GDWSAVGNLE PLGLTNDDVE GPLIFKMNDE DKWNLMVDQY ATGQGYLPLL TTDLSSGDFT
RVDSADYSLG SNRKRHGSVL PITMEEYQAI QEKWNQESEI PDEDEQQAPV LSYSFEESMT
EDVIQDNSGN ERNGTLHGNA TYQHDQEKDS QVLYLDGTDN TFAEFPTGFF DGRDTVTISM
DIKPETVTGN FFTFAIGKDN QRYMFLRTRD TEIRNAITSN SWSNEQEVKA NTASVKDNWM
TVDLVITPTS MKMYKDGILL AENNNITVSM SDLGNDLFAY LGKSFYPDDP YFRGAFDNVE
VYNRALSTDE ILDKSLSSTG IAAFQLPGQQ GVTEIDAVNH QITVPFKGKE IDLSNVTPEI
VIASDAEISP ATDQAQDFTN PITYTVTDKD GNKQEWTVSV EIYPSATLPG LYADPQIFVH
DDTFYLYPTT DGFEGWSGTQ FKAFSSKDLI NWEDHGVILD LATDDVEWAT GNAWAPGFAE
KDGKFYHYFS ANQQIGVASS SSPKEGFEDA LGEPLIPRDE YSGQAIDPYV FTDDDGKSYF
YWGNGSLWGA ALNEDMISLA EEPVNMTPDN FREGVVVFKR DGKYYLMWSE NDTRDENYQV
AYAIGETPMG PWTKQDVILS KDLAQGIKAT GHHSVLNIPD TDDYYIVYHR FSIPDGNGFN
REVMIDKMEF NQDGTIKEVV PTLEGITEPV YIDKEGTEPD EDDETPEEDL ELDFHEKQEV
TAATTYIISG SNAQITTPSD LPKGTTIIVE PMDIEGTNYE GLKIAGEAFN ITVEYPEGAD
EPASDFILSL GYQADANPDK IGIYYYNEES NVWEQRGGEV DSENQTIQLA VSHFSSYGVF
SKIEEDDTTD PDNNGNDGNG SNGSNDDNDQ DSDDDNNNSN HKDDTDDNNE IPSGNQHTNG
KEGEKQAGDE LPNTATSIYN YFLISLILLA LGIALLVSRR LKR
//
