ID   A6WEP7_KINRD            Unreviewed;       786 AA.
AC   A6WEP7;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   02-SEP-2026, entry version 94.
DE   RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE            EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN   OrderedLocusNames=Krad_3823 {ECO:0000313|EMBL:ABS05286.1};
OS   Kineococcus radiotolerans (strain ATCC BAA-149 / DSM 14245 / SRS30216).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Kineosporiales;
OC   Kineosporiaceae; Kineococcus.
OX   NCBI_TaxID=266940 {ECO:0000313|EMBL:ABS05286.1, ECO:0000313|Proteomes:UP000001116};
RN   [1] {ECO:0000313|Proteomes:UP000001116}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-149 / DSM 14245 / SRS30216
RC   {ECO:0000313|Proteomes:UP000001116};
RX   PubMed=19057647; DOI=10.1371/journal.pone.0003878;
RA   Bagwell C.E., Bhat S., Hawkins G.M., Smith B.W., Biswas T., Hoover T.R.,
RA   Saunders E., Han C.S., Tsodikov O.V., Shimkets L.J.;
RT   "Survival in nuclear waste, extreme resistance, and potential applications
RT   gleaned from the genome sequence of Kineococcus radiotolerans SRS30216.";
RL   PLoS ONE 3:e3878-e3878(2008).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in
CC         cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4;
CC         Evidence={ECO:0000256|RuleBase:RU361166};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 9 (cellulase E) family.
CC       {ECO:0000256|ARBA:ARBA00007072, ECO:0000256|PROSITE-ProRule:PRU10059,
CC       ECO:0000256|RuleBase:RU361166}.
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DR   EMBL; CP000750; ABS05286.1; -; Genomic_DNA.
DR   RefSeq; WP_012086432.1; NC_009664.2.
DR   AlphaFoldDB; A6WEP7; -.
DR   STRING; 266940.Krad_3823; -.
DR   KEGG; kra:Krad_3823; -.
DR   eggNOG; COG5297; Bacteria.
DR   HOGENOM; CLU_006010_0_0_11; -.
DR   OrthoDB; 9808897at2; -.
DR   Proteomes; UP000001116; Chromosome.
DR   GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd02850; E_set_Cellulase_N; 1.
DR   Gene3D; 1.50.10.10; -; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR004197; Cellulase_Ig-like.
DR   InterPro; IPR003305; CenC_carb-bd.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR001701; Glyco_hydro_9.
DR   InterPro; IPR033126; Glyco_hydro_9_Asp/Glu_AS.
DR   InterPro; IPR018221; Glyco_hydro_9_His_AS.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   PANTHER; PTHR22298; ENDO-1,4-BETA-GLUCANASE; 1.
DR   Pfam; PF02018; CBM_4_9; 1.
DR   Pfam; PF02927; CelD_N; 1.
DR   Pfam; PF00759; Glyco_hydro_9; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR   PROSITE; PS00592; GH9_2; 1.
DR   PROSITE; PS00698; GH9_3; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW   ECO:0000256|PROSITE-ProRule:PRU10059};
KW   Cellulose degradation {ECO:0000256|RuleBase:RU361166};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PROSITE-
KW   ProRule:PRU10059};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU10059};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW   ECO:0000256|PROSITE-ProRule:PRU10059};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001116};
KW   Signal {ECO:0000256|RuleBase:RU361166}.
FT   SIGNAL          1..34
FT                   /evidence="ECO:0000256|RuleBase:RU361166"
FT   CHAIN           35..786
FT                   /note="Endoglucanase"
FT                   /evidence="ECO:0000256|RuleBase:RU361166"
FT                   /id="PRO_5005121745"
FT   DOMAIN          36..154
FT                   /note="CBM-cenC"
FT                   /evidence="ECO:0000259|Pfam:PF02018"
FT   DOMAIN          185..268
FT                   /note="Cellulase Ig-like"
FT                   /evidence="ECO:0000259|Pfam:PF02927"
FT   DOMAIN          278..769
FT                   /note="Glycoside hydrolase family 9"
FT                   /evidence="ECO:0000259|Pfam:PF00759"
FT   ACT_SITE        696
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10059"
FT   ACT_SITE        748
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
FT   ACT_SITE        757
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
SQ   SEQUENCE   786 AA;  84232 MW;  8B30E82CBC734AA4 CRC64;
     MPSHPRKSRA RALTAVSALL VPASLLLTPS AAQAADQITN GSFDNGTTGW QVYPTASVQD
     GAGCTTVPAS TGAYGAAIQQ EVPLTEGETY KLSFRARTTP ATTGPVRVVV QGGADVNYQQ
     FLPAEKPAFE SAFGTYEYYF TADRDYPNAQ LAFQQDVVNP VAYTLCVDDV VLEGGAERPP
     YVPETGPRVR VNQEAYLPQG PKGATLVTDS TTALPWELKS AGGTVLARGT TTPRGVDPSA
     GLNVHVIDFS GYQRRSTDLV LTVDGETSHP FDIGEDAYER LRDDSMTFFY TNRSGTPISD
     ELAPGYGRAA GHVGVAPNLG DTAVPCQSLE DDSQELLVKQ GDQPFTCDYT TDVTGGWYDA
     GDHGKYVVNG GIAVGQLLQQ YERSLTAPTA DRGALADGTL SIPESGNRVP DVLDEARWEL
     EWFLKMQVQP GRPYAGMVFH KVADVDWTGL PQDPATDPQP RVLYRPSTAA TLNVAATAAQ
     GARLFARYDR AFSQRLLATA RTAYAAAQAN PAVYAPAPDA ALDPNPGSGP YDDRDVSDEF
     YWAAAELYLT TGEPQFRKDV LGSPVHTADV FPAGGFDWGH VGALARLDLA TVPSELNQRE
     RRAVRRSVTE AADRLLIDQA GQPFGQPYAP EGGQYAWGSN SGILANLQVL GTAFDLTGDD
     AYRDGVVRGM DYLLGRNALN NSYITGYGDV FSKNQHSRMY ANQLDPSLPN PPAGTVAGGP
     YSPTATSGDP ITAPLFPEGC AAQFCYVDDI GSWSTNEITV NWNAPLAWVA SFVADQDGGR
     DERQRR
//