Probable bifunctional chitinase/lysozyme precursor

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P13656 (CHIA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 123. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Probable bifunctional chitinase/lysozyme

Including the following 2 domains:

Chitinase
EC=3.2.1.14
Lysozyme
EC=3.2.1.17

Gene names

Name:	chiA
Synonyms:	yheB
Ordered Locus Names:	b3338, JW3300

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	897 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Bifunctional enzyme with lysozyme/chitinase activity. Ref.5
Catalytic activity	Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins. Ref.5 Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins. Ref.5
Subcellular location	Periplasm. Note: Secreted via the Gsp type II secretion machinery under conditions of derepressed gsp gene expression. Ref.5
Induction	Silenced by the DNA-binding protein H-NS under standard growth conditions. Ref.5
Sequence similarities	Belongs to the glycosyl hydrolase 18 family. Chitinase class II subfamily. Contains 5 chitin-binding type-3 domains.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Chitin degradation Polysaccharide degradation
Cellular component	Periplasm
Domain	Repeat Signal
Ligand	Chitin-binding
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond
Technical term	Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological_process	chitin catabolic process Inferred from electronic annotation. Source: UniProtKB-KW polysaccharide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular region Inferred from electronic annotation. Source: InterPro periplasmic space Inferred from direct assay Ref.5. Source: EcoCyc
Molecular_function	carbohydrate binding Inferred from electronic annotation. Source: InterPro chitin binding Inferred from electronic annotation. Source: UniProtKB-KW endochitinase activity Inferred from direct assay Ref.5. Source: EcoCyc lysozyme activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 24

Potential

Chain

25 – 897

873

Probable bifunctional chitinase/lysozyme

PRO_0000011907

Regions

Domain

25 – 91

Chitin-binding type-3 1

Domain

128 – 194

Chitin-binding type-3 2

Domain

229 – 295

Chitin-binding type-3 3

Domain

337 – 403

Chitin-binding type-3 4

Domain

459 – 529

Chitin-binding type-3 5

Region

647 – 897

251

Catalytic By similarity

Compositional bias

93 – 101

Poly-Ser

Sites

Active site

700

Proton donor By similarity

Amino acid modifications

Disulfide bond

628 ↔ 673

By similarity

Experimental info

Sequence conflict

874

F → I in AAC13985. Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

P13656 [UniParc].

Last modified November 1, 1995. Version 2.
Checksum: 968D145BA1F954F3
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FASTA

897

97,058

        10         20         30         40         50         60 
MKLNIFTKSM IGMGLVCSAL PALAMEAWNN QQGGNKYQVI FDGKIYENAW WVSSTNCPGK 

        70         80         90        100        110        120 
AKANDATNPW RLKRTATAAE ISQFGNTLSC EKSGSSSSSN SNTPASNTPA NGGSATPAQG 

       130        140        150        160        170        180 
TVPSNSSVVA WNKQQGGQTW YVVFNGAVYK NAWWVASSNC PGDAKSNDAS NPWRYVRAAT 

       190        200        210        220        230        240 
ATEISETSNP QSCTSAPQPS PDVKPAPDVK PAPDVQPAPA DKSNDNYAVV AWKGQEGSST 

       250        260        270        280        290        300 
WYVIYNGGIY KNAWWVGAAN CPGDAKENDA SNPWRYVRAA TATEISQYGN PGSCSVKPDN 

       310        320        330        340        350        360 
NGGAVTPVDP TPETPVTPTP DNSEPSTPAD SVNDYSLQAW SGQEGSEIYH VIFNGNVYKN 

       370        380        390        400        410        420 
AWWVGSKDCP RGTSAENSNN PWRLERTATA AELSQYGNPT TCEIDNGGVI VADGFQASKA 

       430        440        450        460        470        480 
YSADSIVDYN DAHYKTSVDQ DAWGFVPGGD NPWKKYEPAK AWSASTVYVK GDRVVVDGQA 

       490        500        510        520        530        540 
YEALFWTQSD NPALVANQNA TGSNSRPWKP LGKAQSYSNE ELNNAPQFNP ETLYASDTLI 

       550        560        570        580        590        600 
RFNGVNYISQ SKVQKVSPSD SNPWRVFVDW TGTKERVGTP KKAWPKHVYA PYVDFTLNTI 

       610        620        630        640        650        660 
PDLAALAKNH NVNHFTLAFV VSKDANTCLP TWGTAYGMQN YAQYSKIKAL REAGGDVMLS 

       670        680        690        700        710        720 
IGGANNAPLA ASCKNVDDLM QHYYDIVDNL NLKVLDFDIE GTWVADQASI ERRNLAVKKV 

       730        740        750        760        770        780 
QDKWKSEGKD IAIWYTLPIL PTGLTPEGMN VLSDAKAKGV ELAGVNVMTM DYGNAICQSA 

       790        800        810        820        830        840 
NTEGQNIHGK CATSAIANLH SQLKGLHPNK SDAEIDAMMG TTPMVGVNDV QGEVFYLSDA 

       850        860        870        880        890 
RLVMQDAQKR NLGMVGIWSI ARDLPGGTNL SPEFHGLTKE QAPKYAFSEI FAPFTKQ

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[2]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"Cloning, sequencing, and mapping of the bacterioferritin gene (bfr) of Escherichia coli K-12." Andrews S.C., Harrison P.M., Guest J.R. J. Bacteriol. 171:3940-3947(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 874-897. Strain: K12.
[4]	"Functional analysis of the carbohydrate-binding domains of Erwinia chrysanthemi Cel5 (Endoglucanase Z) and an Escherichia coli putative chitinase." Simpson H.D., Barras F. J. Bacteriol. 181:4611-4616(1999) [PubMed] [Europe PMC] [Abstract] Cited for: CHITIN-BINDING PROPERTIES.
[5]	"The ChiA (YheB) protein of Escherichia coli K-12 is an endochitinase whose gene is negatively controlled by the nucleoid-structuring protein H-NS." Francetic O., Badaut C., Rimsky S., Pugsley A.P. Mol. Microbiol. 35:1506-1517(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TRANSCRIPTIONAL REGULATION, GENE NAME. Strain: K12 / MG1655 / ATCC 47076.
[6]	"Expression of the endogenous type II secretion pathway in Escherichia coli leads to chitinase secretion." Francetic O., Belin D., Badaut C., Pugsley A.P. EMBO J. 19:6697-6703(2000) [PubMed] [Europe PMC] [Abstract] Cited for: SECRETION VIA THE GSP SECRETON. Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U18997 Genomic DNA. Translation: AAA58135.1. U00096 Genomic DNA. Translation: AAC76363.1. AP009048 Genomic DNA. Translation: BAE77953.1. M27176 mRNA. Translation: AAC13985.1.
PIR	E65127.
RefSeq	NP_417797.1. NC_000913.2. YP_492094.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P13656.
SMR	P13656. Positions 585-896.
ModBase	Search...
Protein-protein interaction databases
IntAct	P13656. 1 interaction.
STRING	511145.b3338.
Protein family/group databases
CAZy	CBM5. Carbohydrate-Binding Module Family 5. GH18. Glycoside Hydrolase Family 18.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC76363; AAC76363; b3338. BAE77953; BAE77953; BAE77953.
GeneID	12932022. 947837.
KEGG	ecj:Y75_p3838. eco:b3338.
PATRIC	32122108. VBIEscCol129921_3431.
Organism-specific databases
EchoBASE	EB1219.
EcoGene	EG11237. chiA.
Phylogenomic databases
eggNOG	NOG12793.
HOGENOM	HOG000125409.
KO	K13381.
OMA	GSIYKNA.
ProtClustDB	CLSK891810.
Enzyme and pathway databases
BioCyc	EcoCyc:EG11237-MONOMER. ECOL316407:JW3300-MONOMER. MetaCyc:EG11237-MONOMER.
Gene expression databases
Genevestigator	P13656.
Family and domain databases
Gene3D	2.10.10.20. 1 hit. 3.20.20.80. 1 hit.
InterPro	IPR003610. CBM_fam5/12. IPR013781. Glyco_hydro_catalytic_dom. IPR017853. Glycoside_hydrolase_SF. [Graphical view]
Pfam	PF02839. CBM_5_12. 1 hit. [Graphical view]
SMART	SM00495. ChtBD3. 7 hits. [Graphical view]
SUPFAM	SSF51055. CBM_5_12. 1 hit. SSF51445. Glyco_hydro_cat. 1 hit.
PROSITE	PS01095. CHITINASE_18. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CHIA_ECOLI

Accession

Primary (citable) accession number: P13656
Secondary accession number(s): Q2M703

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	November 1, 1995
Last modified:	May 1, 2013
This is version 123 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Including the following 2 domains:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents