CHIB_SERMA
ID CHIB_SERMA Reviewed; 499 AA.
AC P11797;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Chitinase B;
DE EC=3.2.1.14;
DE Flags: Precursor;
GN Name=chiB;
OS Serratia marcescens.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=615;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 990 / QMB1466;
RX PubMed=2668886; DOI=10.1093/nar/17.13.5395;
RA Harpster M.H., Dunsmuir P.;
RT "Nucleotide sequence of the chitinase B gene of Serratia marcescens
RT QMB1466.";
RL Nucleic Acids Res. 17:5395-5395(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=2170;
RX PubMed=9371460; DOI=10.1128/jb.179.22.7111-7117.1997;
RA Watanabe T., Kimura K., Sumiya T., Nikaidou N., Suzuki K., Suzuki M.,
RA Taiyoji M., Ferrer S., Regue M.;
RT "Genetic analysis of the chitinase system of Serratia marcescens 2170.";
RL J. Bacteriol. 179:7111-7117(1997).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide
CC (1->4)-beta-linkages in chitin and chitodextrins.; EC=3.2.1.14;
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class II subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X15208; CAA33278.1; -; Genomic_DNA.
DR EMBL; AB015997; BAA31568.1; -; Genomic_DNA.
DR PIR; S04856; S04856.
DR RefSeq; WP_016926761.1; NZ_VOUW01000021.1.
DR PDB; 1E6N; X-ray; 2.25 A; A/B=1-497.
DR PDB; 1GOI; X-ray; 1.45 A; A/B=1-497.
DR PDB; 1H0G; X-ray; 2.00 A; A/B=1-497.
DR PDB; 1H0I; X-ray; 2.00 A; A/B=1-497.
DR PDB; 1O6I; X-ray; 1.70 A; A/B=1-497.
DR PDB; 1OGB; X-ray; 1.85 A; A/B=1-497.
DR PDB; 1OGG; X-ray; 1.97 A; A/B=1-497.
DR PDB; 3WD0; X-ray; 1.70 A; A=2-499.
DR PDB; 3WD1; X-ray; 2.30 A; A=2-499.
DR PDB; 3WD2; X-ray; 2.20 A; A=2-499.
DR PDB; 3WD3; X-ray; 2.20 A; A=2-499.
DR PDB; 3WD4; X-ray; 2.00 A; A=2-499.
DR PDB; 4Z2G; X-ray; 2.60 A; A=2-499.
DR PDB; 4Z2H; X-ray; 2.35 A; A=2-499.
DR PDB; 4Z2I; X-ray; 2.00 A; A=2-499.
DR PDB; 4Z2J; X-ray; 2.60 A; A=2-499.
DR PDB; 4Z2K; X-ray; 2.30 A; A=2-499.
DR PDB; 4Z2L; X-ray; 2.30 A; A=2-499.
DR PDB; 6JK9; X-ray; 2.31 A; A/B=3-498.
DR PDB; 6JKF; X-ray; 1.99 A; A/B=3-499.
DR PDB; 7C34; X-ray; 1.94 A; A/B=3-498.
DR PDB; 7C92; X-ray; 2.32 A; A/B=2-499.
DR PDB; 7CB1; X-ray; 1.98 A; A/B=2-499.
DR PDBsum; 1E6N; -.
DR PDBsum; 1GOI; -.
DR PDBsum; 1H0G; -.
DR PDBsum; 1H0I; -.
DR PDBsum; 1O6I; -.
DR PDBsum; 1OGB; -.
DR PDBsum; 1OGG; -.
DR PDBsum; 3WD0; -.
DR PDBsum; 3WD1; -.
DR PDBsum; 3WD2; -.
DR PDBsum; 3WD3; -.
DR PDBsum; 3WD4; -.
DR PDBsum; 4Z2G; -.
DR PDBsum; 4Z2H; -.
DR PDBsum; 4Z2I; -.
DR PDBsum; 4Z2J; -.
DR PDBsum; 4Z2K; -.
DR PDBsum; 4Z2L; -.
DR PDBsum; 6JK9; -.
DR PDBsum; 6JKF; -.
DR PDBsum; 7C34; -.
DR PDBsum; 7C92; -.
DR PDBsum; 7CB1; -.
DR AlphaFoldDB; P11797; -.
DR SMR; P11797; -.
DR STRING; 273526.SMDB11_2875; -.
DR BindingDB; P11797; -.
DR ChEMBL; CHEMBL5348; -.
DR DrugBank; DB04520; (3s,8ar)-3-(4-Hydroxybenzyl)Hexahydropyrrolo[1,2-a]Pyrazine-1,4-Dione.
DR DrugBank; DB02813; 2-Acetamido-2-Deoxy-D-Glucono-1,5-Lactone.
DR DrugBank; DB03109; 2-acetylamino-2-deoxy-b-D-allopyranose.
DR DrugBank; DB04628; Allosamidin.
DR DrugBank; DB04404; Allosamizoline.
DR DrugBank; DB02414; Cyclo(his-pro).
DR DrugBank; DB04541; Cyclo(prolylglycyl).
DR DrugBank; DB04157; N-[(Aminooxy)Carbonyl]Aniline.
DR DrugBank; DB04433; Verpacamide A.
DR CAZy; CBM5; Carbohydrate-Binding Module Family 5.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR BioCyc; MetaCyc:MON-20051; -.
DR BRENDA; 3.2.1.14; 5690.
DR BRENDA; 3.2.1.200; 5690.
DR SABIO-RK; P11797; -.
DR EvolutionaryTrace; P11797; -.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0008061; F:chitin binding; IEA:InterPro.
DR GO; GO:0004568; F:chitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.10.50.10; -; 1.
DR InterPro; IPR003610; CBM_fam5/12.
DR InterPro; IPR036573; CBM_sf_5/12.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR029070; Chitinase_insertion_sf.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00495; ChtBD3; 1.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51055; SSF51055; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF54556; SSF54556; 1.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Chitin degradation; Glycosidase;
KW Hydrolase; Polysaccharide degradation; Signal.
FT SIGNAL 1..41
FT CHAIN 42..499
FT /note="Chitinase B"
FT /id="PRO_0000011909"
FT DOMAIN 42..425
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT DOMAIN 438..498
FT /note="Chitin-binding type-3"
FT ACT_SITE 144
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 68..69
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 95..98
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 145
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 212..215
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 403
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT STRAND 6..12
FT /evidence="ECO:0007829|PDB:1GOI"
FT HELIX 15..19
FT /evidence="ECO:0007829|PDB:1GOI"
FT TURN 26..28
FT /evidence="ECO:0007829|PDB:1GOI"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:1GOI"
FT HELIX 38..43
FT /evidence="ECO:0007829|PDB:1GOI"
FT STRAND 45..54
FT /evidence="ECO:0007829|PDB:1GOI"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:1GOI"
FT HELIX 68..80
FT /evidence="ECO:0007829|PDB:1GOI"
FT HELIX 81..84
FT /evidence="ECO:0007829|PDB:1GOI"
FT STRAND 89..95
FT /evidence="ECO:0007829|PDB:1GOI"
FT HELIX 97..100
FT /evidence="ECO:0007829|PDB:1GOI"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:4Z2G"
FT HELIX 107..113
FT /evidence="ECO:0007829|PDB:1GOI"
FT HELIX 117..134
FT /evidence="ECO:0007829|PDB:1GOI"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:1GOI"
FT HELIX 148..171
FT /evidence="ECO:0007829|PDB:1GOI"
FT STRAND 180..188
FT /evidence="ECO:0007829|PDB:1GOI"
FT HELIX 189..192
FT /evidence="ECO:0007829|PDB:1GOI"
FT TURN 193..195
FT /evidence="ECO:0007829|PDB:1GOI"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:1GOI"
FT HELIX 199..203
FT /evidence="ECO:0007829|PDB:1GOI"
FT STRAND 207..212
FT /evidence="ECO:0007829|PDB:1GOI"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:1GOI"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:1GOI"
FT HELIX 242..245
FT /evidence="ECO:0007829|PDB:1GOI"
FT HELIX 252..258
FT /evidence="ECO:0007829|PDB:1GOI"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:1GOI"
FT HELIX 267..275
FT /evidence="ECO:0007829|PDB:1GOI"
FT HELIX 282..284
FT /evidence="ECO:0007829|PDB:1GOI"
FT STRAND 285..298
FT /evidence="ECO:0007829|PDB:1GOI"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:1GOI"
FT TURN 304..307
FT /evidence="ECO:0007829|PDB:1GOI"
FT STRAND 315..317
FT /evidence="ECO:0007829|PDB:1H0G"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:1GOI"
FT HELIX 329..334
FT /evidence="ECO:0007829|PDB:1GOI"
FT STRAND 339..341
FT /evidence="ECO:0007829|PDB:1GOI"
FT HELIX 342..350
FT /evidence="ECO:0007829|PDB:1GOI"
FT STRAND 353..360
FT /evidence="ECO:0007829|PDB:1GOI"
FT TURN 361..364
FT /evidence="ECO:0007829|PDB:1GOI"
FT STRAND 365..370
FT /evidence="ECO:0007829|PDB:1GOI"
FT TURN 371..374
FT /evidence="ECO:0007829|PDB:1GOI"
FT STRAND 375..378
FT /evidence="ECO:0007829|PDB:1GOI"
FT HELIX 382..394
FT /evidence="ECO:0007829|PDB:1GOI"
FT STRAND 399..403
FT /evidence="ECO:0007829|PDB:1GOI"
FT HELIX 405..407
FT /evidence="ECO:0007829|PDB:1GOI"
FT HELIX 413..423
FT /evidence="ECO:0007829|PDB:1GOI"
FT HELIX 445..447
FT /evidence="ECO:0007829|PDB:1O6I"
FT STRAND 467..470
FT /evidence="ECO:0007829|PDB:1GOI"
FT STRAND 473..480
FT /evidence="ECO:0007829|PDB:1GOI"
FT TURN 486..488
FT /evidence="ECO:0007829|PDB:1GOI"
FT STRAND 492..497
FT /evidence="ECO:0007829|PDB:1GOI"
SQ SEQUENCE 499 AA; 55464 MW; FFD674916109D1D8 CRC64;
MSTRKAVIGY YFIPTNQINN YTETDTSVVP FPVSNITPAK AKQLTHINFS FLDINSNLEC
AWDPATNDAK ARDVVNRLTA LKAHNPSLRI MFSIGGWYYS NDLGVSHANY VNAVKTPAAR
TKFAQSCVRI MKDYGFDGVD IDWEYPQAAE VDGFIAALQE IRTLLNQQTI ADGRQALPYQ
LTIAGAGGAF FLSRYYSKLA QIVAPLDYIN LMTYDLAGPW EKITNHQAAL FGDAAGPTFY
NALREANLGW SWEELTRAFP SPFSLTVDAA VQQHLMMEGV PSAKIVMGVP FYGRAFKGVS
GGNGGQYSSH STPGEDPYPN ADYWLVGCDE CVRDKDPRIA SYRQLEQMLQ GNYGYQRLWN
DKTKTPYLYH AQNGLFVTYD DAESFKYKAK YIKQQQLGGV MFWHLGQDNR NGDLLAALDR
YFNAADYDDS QLDMGTGLRY TGVGPGNLPI MTAPAYVPGT TYAQGALVSY QGYVWQTKWG
YITSAPGSDS AWLKVGRLA
