ID   GUNA_XANCP              Reviewed;         484 AA.
AC   P19487;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2002, sequence version 2.
DT   27-MAR-2024, entry version 151.
DE   RecName: Full=Major extracellular endoglucanase;
DE            EC=3.2.1.4;
DE   AltName: Full=Cellulase;
DE   AltName: Full=Endo-1,4-beta-glucanase;
DE   Flags: Precursor;
GN   Name=engXCA; OrderedLocusNames=XCC3521;
OS   Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS   528 / LMG 568 / P 25).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=190485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 26-61.
RX   PubMed=2373365; DOI=10.1016/0378-1119(90)90205-6;
RA   Gough C.L., Dow J.M., Keen J., Henrissat B., Daniels M.J.;
RT   "Nucleotide sequence of the engXCA gene encoding the major endoglucanase of
RT   Xanthomonas campestris pv. campestris.";
RL   Gene 89:53-59(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX   PubMed=12024217; DOI=10.1038/417459a;
RA   da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA   Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA   Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA   Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA   Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA   Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA   Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA   Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA   Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA   Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA   Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA   Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA   Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA   Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT   "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT   specificities.";
RL   Nature 417:459-463(2002).
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   -!- DOMAIN: The C-terminal region of the protein is not crucial for
CC       activity.
CC   -!- DOMAIN: The Thr/Pro-rich region (also termed 'hinge') may be a
CC       potential site for proteolysis.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000305}.
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DR   EMBL; M32700; AAA27612.1; -; Genomic_DNA.
DR   EMBL; AE008922; AAM42791.1; -; Genomic_DNA.
DR   PIR; JH0158; JH0158.
DR   RefSeq; NP_638867.1; NC_003902.1.
DR   RefSeq; WP_011038613.1; NC_003902.1.
DR   PDB; 4TUF; X-ray; 2.70 A; A/B/C/D=26-371.
DR   PDBsum; 4TUF; -.
DR   AlphaFoldDB; P19487; -.
DR   SMR; P19487; -.
DR   STRING; 190485.XCC3521; -.
DR   CAZy; CBM2; Carbohydrate-Binding Module Family 2.
DR   CAZy; GH5; Glycoside Hydrolase Family 5.
DR   EnsemblBacteria; AAM42791; AAM42791; XCC3521.
DR   KEGG; xcc:XCC3521; -.
DR   PATRIC; fig|190485.4.peg.3766; -.
DR   eggNOG; COG2730; Bacteria.
DR   eggNOG; COG5297; Bacteria.
DR   HOGENOM; CLU_020735_1_0_6; -.
DR   OrthoDB; 1153097at2; -.
DR   BRENDA; 3.2.1.4; 9230.
DR   Proteomes; UP000001010; Chromosome.
DR   GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.290; -; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR001919; CBD2.
DR   InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR   InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR   InterPro; IPR001547; Glyco_hydro_5.
DR   InterPro; IPR018087; Glyco_hydro_5_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR35923:SF2; CELLULASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR35923; MAJOR EXTRACELLULAR ENDOGLUCANASE; 1.
DR   Pfam; PF00553; CBM_2; 1.
DR   Pfam; PF00150; Cellulase; 1.
DR   SMART; SM00637; CBD_II; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR   PROSITE; PS51173; CBM2; 1.
DR   PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Carbohydrate metabolism; Cellulose degradation;
KW   Direct protein sequencing; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Reference proteome; Repeat; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000269|PubMed:2373365"
FT   CHAIN           26..484
FT                   /note="Major extracellular endoglucanase"
FT                   /id="PRO_0000007875"
FT   DOMAIN          395..484
FT                   /note="CBM2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01135"
FT   REGION          370..402
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          375..399
FT                   /note="Thr-Pro repeats ('hinge') (Pro-Thr box)"
FT   COMPBIAS        378..398
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        182
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        303
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        410..484
FT                   /note="VDNSWNGGYCNRVQVTNTGTASGTWSIAVPVTGTVNNAWNATWSQSGSTLRA
FT                   SGVDFNRTLAAGATAEFGFCAAS -> ASPVVGSAARKLPAASRLACHWPASSTGWRVW
FT                   VIAAPSVTWKRPHAARAIERRMRVTRLRRATRLNRGPLPAPAHTTQHAPRL (in
FT                   Ref. 1; AAA27612)"
FT                   /evidence="ECO:0000305"
FT   STRAND          45..48
FT                   /evidence="ECO:0007829|PDB:4TUF"
FT   TURN            60..64
FT                   /evidence="ECO:0007829|PDB:4TUF"
FT   HELIX           67..76
FT                   /evidence="ECO:0007829|PDB:4TUF"
FT   STRAND          81..86
FT                   /evidence="ECO:0007829|PDB:4TUF"
FT   HELIX           88..91
FT                   /evidence="ECO:0007829|PDB:4TUF"
FT   TURN            102..104
FT                   /evidence="ECO:0007829|PDB:4TUF"
FT   HELIX           106..108
FT                   /evidence="ECO:0007829|PDB:4TUF"
FT   HELIX           113..127
FT                   /evidence="ECO:0007829|PDB:4TUF"
FT   STRAND          130..135
FT                   /evidence="ECO:0007829|PDB:4TUF"
FT   STRAND          138..142
FT                   /evidence="ECO:0007829|PDB:4TUF"
FT   STRAND          145..147
FT                   /evidence="ECO:0007829|PDB:4TUF"
FT   HELIX           154..168
FT                   /evidence="ECO:0007829|PDB:4TUF"
FT   STRAND          174..178
FT                   /evidence="ECO:0007829|PDB:4TUF"
FT   STRAND          188..192
FT                   /evidence="ECO:0007829|PDB:4TUF"
FT   TURN            194..196
FT                   /evidence="ECO:0007829|PDB:4TUF"
FT   HELIX           198..212
FT                   /evidence="ECO:0007829|PDB:4TUF"
FT   STRAND          216..220
FT                   /evidence="ECO:0007829|PDB:4TUF"
FT   STRAND          227..229
FT                   /evidence="ECO:0007829|PDB:4TUF"
FT   HELIX           242..245
FT                   /evidence="ECO:0007829|PDB:4TUF"
FT   TURN            253..255
FT                   /evidence="ECO:0007829|PDB:4TUF"
FT   STRAND          256..258
FT                   /evidence="ECO:0007829|PDB:4TUF"
FT   STRAND          261..263
FT                   /evidence="ECO:0007829|PDB:4TUF"
FT   TURN            265..267
FT                   /evidence="ECO:0007829|PDB:4TUF"
FT   HELIX           271..274
FT                   /evidence="ECO:0007829|PDB:4TUF"
FT   TURN            278..281
FT                   /evidence="ECO:0007829|PDB:4TUF"
FT   HELIX           282..289
FT                   /evidence="ECO:0007829|PDB:4TUF"
FT   HELIX           291..293
FT                   /evidence="ECO:0007829|PDB:4TUF"
FT   TURN            294..296
FT                   /evidence="ECO:0007829|PDB:4TUF"
FT   STRAND          301..305
FT                   /evidence="ECO:0007829|PDB:4TUF"
FT   HELIX           313..328
FT                   /evidence="ECO:0007829|PDB:4TUF"
FT   STRAND          334..337
FT                   /evidence="ECO:0007829|PDB:4TUF"
FT   STRAND          339..341
FT                   /evidence="ECO:0007829|PDB:4TUF"
FT   TURN            344..346
FT                   /evidence="ECO:0007829|PDB:4TUF"
FT   HELIX           359..369
FT                   /evidence="ECO:0007829|PDB:4TUF"
SQ   SEQUENCE   484 AA;  52242 MW;  6671AE5BF1B7602A CRC64;
     MSIFRTASTL ALATALALAA GPAFSYSINN SRQIVDDSGK VVQLKGVNVF GFETGNHVMH
     GLWARNWKDM IVQMQGLGFN AVRLPFCPAT LRSDTMPASI DYSRNADLQG LTSLQILDKV
     IAEFNARGMY VLLDHHTPDC AGISELWYTG SYTEAQWLAD LRFVANRYKN VPYVLGLDLK
     NEPHGAATWG TGNAATDWNK AAERGSAAVL AVAPKWLIAV EGITDNPVCS TNGGIFWGGN
     LQPLACTPLN IPANRLLLAP HVYGPDVFVQ SYFNDSNFPN NMPAIWERHF GQFAGTHALL
     LGEFGGKYGE GDARDKTWQD ALVKYLRSKG INQGFYWSWN PNSGDTGGIL RDDWTSVRQD
     KMTLLRTLWG TAGNTTPTPT PTPTPTPTPT PTPTPTPTPG TSTFSTKVIV DNSWNGGYCN
     RVQVTNTGTA SGTWSIAVPV TGTVNNAWNA TWSQSGSTLR ASGVDFNRTL AAGATAEFGF
     CAAS
//