ID A0A2A8CWK3_9BACT Unreviewed; 858 AA.
AC A0A2A8CWK3;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Beta-glucanase {ECO:0008006|Google:ProtNLM};
GN ORFNames=CRI94_12160 {ECO:0000313|EMBL:PEN12768.1};
OS Longibacter salinarum.
OC Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Salisaetaceae;
OC Longibacter.
OX NCBI_TaxID=1850348 {ECO:0000313|EMBL:PEN12768.1, ECO:0000313|Proteomes:UP000220102};
RN [1] {ECO:0000313|EMBL:PEN12768.1, ECO:0000313|Proteomes:UP000220102}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 52045 {ECO:0000313|EMBL:PEN12768.1,
RC ECO:0000313|Proteomes:UP000220102};
RA Goh K.M., Shamsir M.S., Lim S.W.;
RT "Draft genome of Longibacter Salinarum.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family.
CC {ECO:0000256|ARBA:ARBA00006865}.
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:PEN12768.1}.
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DR EMBL; PDEQ01000006; PEN12768.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A8CWK3; -.
DR OrthoDB; 610585at2; -.
DR Proteomes; UP000220102; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; 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:InterPro.
DR CDD; cd00146; PKD; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.60.120.430; Galactose-binding lectin; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000757; GH16.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR022409; PKD/Chitinase_dom.
DR InterPro; IPR000601; PKD_dom.
DR InterPro; IPR035986; PKD_dom_sf.
DR PANTHER; PTHR10963:SF55; GH16 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR10963; GLYCOSYL HYDROLASE-RELATED; 1.
DR Pfam; PF00722; Glyco_hydro_16; 1.
DR Pfam; PF18911; PKD_4; 1.
DR SMART; SM00089; PKD; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF49299; PKD domain; 1.
DR PROSITE; PS51762; GH16_2; 1.
DR PROSITE; PS50093; PKD; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000220102};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 327..406
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 554..858
FT /note="GH16"
FT /evidence="ECO:0000259|PROSITE:PS51762"
FT REGION 396..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 858 AA; 91756 MW; 35D9D122B810F9E0 CRC64;
MYIDRSTTTS PLWTLLLGLL LSVLTVSTVS LLSGCDQGGM NDDGDNFIAP STSRVGFEVR
PGATDTTQQL TLTYTSLDVR PEPGDVPTPF TVELVEETGD PSNGTSVFDV TFSPPQDKAT
FTEKLIFSAG GRYVTIQLFG FVGFNDELIT DYAGSGIVDD FFGFNGLEGA SSIDGQLSVP
GSGAGGPGVF PGVSHALSET VDFGQTPVLV ARMRVSADSP GPAIVRAALN QEGDLPDANS
SAAPLIKEVP ADGEYADYYF DFRDLFVQFD GQPVDATNIT EVVLLVNDGG SLDFLGRSDT
FTGTLEIDRL ARRPDIPGEE GGGNAAPNAN FIFAPSQPAV GETVNFTDRS SDDGMIVSRD
WDFGDGTTAT GETPSHAYGA QGDYTVTLTV TDDEGVTSTS TQTVSVSDGS NGGSTFRDDG
DGDGLILYDD FEDGIQADEY VTFQGQGATI GLSESSDAAM DAGGMAAIAA NVDGGGGGGF
AGFGKEYGSG QDGVDVSDLG SDPYFTMYVK SDAASTYTLE INLQEDQDGN DQYDGSGATD
DEFQYDYVVE PSASGYTRIS VPLSAFQDDN DVNNGGDGQL SSRIANVIFA IGNLPAESFT
LTIDDIIFSD QDLGAGGGTV QSACGNDYEL FFEDNFDAPN DTFWDRGNAT FNGNLATFRP
DNITYEDGKM VLNLKKEQFN GKPYTGAELR TDNQTGFYSY GCYEVRMKSA GPSGTVSSFF
GYRYNPWQEI DIEIVGKNNR SMLTNIYYND GPEGAANNDA YQVPPFPEGV GLSYDASQEF
HNYAFEWTPG EIKWYRDGQL VKQATVEGAS SSEIPNLDMQ IMMNLWVSNS PSFAGEIDDS
NFPVRAEYDW VRFYRPAN
//
