ID B5RK45_KLEP3 Unreviewed; 779 AA.
AC B5RK45;
DT 04-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 04-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Endoglucanase {ECO:0000256|RuleBase:RU361166};
DE EC=3.2.1.4 {ECO:0000256|RuleBase:RU361166};
GN Name=celK {ECO:0000313|EMBL:ACI12123.1};
GN OrderedLocusNames=KPK_A0121 {ECO:0000313|EMBL:ACI12123.1};
OS Klebsiella pneumoniae (strain 342).
OG Plasmid pKP187 {ECO:0000313|EMBL:ACI12123.1,
OG ECO:0000313|Proteomes:UP000001734}.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=507522 {ECO:0000313|EMBL:ACI12123.1, ECO:0000313|Proteomes:UP000001734};
RN [1] {ECO:0000313|EMBL:ACI12123.1, ECO:0000313|Proteomes:UP000001734}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=342 {ECO:0000313|EMBL:ACI12123.1,
RC ECO:0000313|Proteomes:UP000001734};
RC PLASMID=Plasmid pKP187 {ECO:0000313|Proteomes:UP000001734};
RX PubMed=18654632; DOI=10.1371/journal.pgen.1000141;
RA Fouts D.E., Tyler H.L., DeBoy R.T., Daugherty S., Ren Q., Badger J.H.,
RA Durkin A.S., Huot H., Shrivastava S., Kothari S., Dodson R.J., Mohamoud Y.,
RA Khouri H., Roesch L.F., Krogfelt K.A., Struve C., Triplett E.W.,
RA Methe B.A.;
RT "Complete genome sequence of the N2-fixing broad host range endophyte
RT Klebsiella pneumoniae 342 and virulence predictions verified in mice.";
RL PLoS Genet. 4:E1000141-E1000141(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|PROSITE-ProRule:PRU10059, ECO:0000256|RuleBase:RU361166}.
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DR EMBL; CP000965; ACI12123.1; -; Genomic_DNA.
DR AlphaFoldDB; B5RK45; -.
DR CAZy; CBM4; Carbohydrate-Binding Module Family 4.
DR CAZy; GH9; Glycoside Hydrolase Family 9.
DR KEGG; kpe:KPK_A0121; -.
DR HOGENOM; CLU_006010_0_0_6; -.
DR Proteomes; UP000001734; Plasmid pKP187.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
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 PANTHER; PTHR22298:SF29; ENDOGLUCANASE; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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}; Plasmid {ECO:0000313|EMBL:ACI12123.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|PROSITE-ProRule:PRU10059};
KW Signal {ECO:0000256|RuleBase:RU361166}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|RuleBase:RU361166"
FT CHAIN 21..779
FT /note="Endoglucanase"
FT /evidence="ECO:0000256|RuleBase:RU361166"
FT /id="PRO_5005123494"
FT DOMAIN 39..161
FT /note="CBM-cenC"
FT /evidence="ECO:0000259|Pfam:PF02018"
FT DOMAIN 184..264
FT /note="Cellulase Ig-like"
FT /evidence="ECO:0000259|Pfam:PF02927"
FT DOMAIN 275..768
FT /note="Glycoside hydrolase family 9"
FT /evidence="ECO:0000259|Pfam:PF00759"
FT ACT_SITE 698
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10059"
FT ACT_SITE 747
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
FT ACT_SITE 756
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10060"
SQ SEQUENCE 779 AA; 86149 MW; C52171D9C109E114 CRC64;
MNTRRTVKFS LIFSSLFALQ GCINGDGSST QQSASLAEEL VNNGSFAAGT DGWWAAGGQL
DRVDNMGCFT FTNSGANPWD VIFAQSGIPL AEGQSYNLSF TAVTKKPINA KILVQQDGAP
YTNYFAQDVE LNETRKDFNF KFTPKSADEK AQFQLQLGTQ SPTTVCLSNV SLKGPRLKVA
SNFASIRVNQ VGYLPHALKR ATMVSDSTQP LSWTLLNSMG TKVAEGQTKP FGINRASNEN
VHIIDFSQYT EETDKLTLVV GDKKSHPFNI SSKLYQQLKY DALSFFYQQR SGIPIEKQYV
QRPDLARPAG HPSERVTCFN KTDAKGNQWP GCDYKLDVTG GWYDAGDQGK YVVNGGISTW
TLMNFFEHEK YSRNVKESAF SDGKVKIPEN NNRKNDLLDE ARWMMDFMLA MQVPDGKKAW
VPVGDQSGHL EALKLTEIDA SGMAFHKVAD EAWTGMPLPP HKDPQPRYLS QPSTAATLNL
AATAAQCARV WKDTDAAYAK RCLAAAEKAW KSANKHPNVF AYDNFVGSGP YDDTKVDDEF
YWAAAELFTT TGKAEYLDAI KNSRYYLTSP KGDKDATGDL FWQDVSAAGT ITLALVPNDL
PAEDVKKAKQ TIINTANAYA QSVQTEGYLI PYSAVEYPWG SNSNLMNRSI FLGLAHDFTG
DRKYVQAMSD AMDYVLGRNP LDQSYVSGYG SRPLKNPHHR FWAQQLDPSS PLVPPGVMSG
GPNSISFSDP IAASLKGHCT GQTCWKDEIG AWTLNEVTIN WNAPFFWTTS YIDEGYLNK
//
