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P13656 (CHIA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable bifunctional chitinase/lysozyme

Including the following 2 domains:

  1. Chitinase
    EC=3.2.1.14
  2. Lysozyme
    EC=3.2.1.17
Gene names
Name:chiA
Synonyms:yheB
Ordered Locus Names:b3338, JW3300
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length897 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 897873Probable bifunctional chitinase/lysozyme
PRO_0000011907

Regions

Domain25 – 9167Chitin-binding type-3 1
Domain128 – 19467Chitin-binding type-3 2
Domain229 – 29567Chitin-binding type-3 3
Domain337 – 40367Chitin-binding type-3 4
Domain459 – 52971Chitin-binding type-3 5
Region647 – 897251Catalytic By similarity
Compositional bias93 – 1019Poly-Ser

Sites

Active site7001Proton donor By similarity

Amino acid modifications

Disulfide bond628 ↔ 673 By similarity

Experimental info

Sequence conflict8741F → I in AAC13985. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P13656 [UniParc].

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

FASTA89797,058
        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' 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 277:1453-1462(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.
PIRE65127.
RefSeqNP_417797.1. NC_000913.3.
YP_492094.1. NC_007779.1.

3D structure databases

ProteinModelPortalP13656.
SMRP13656. Positions 457-509, 585-896.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-9276N.
IntActP13656. 1 interaction.
STRING511145.b3338.

Protein family/group databases

CAZyCBM5. Carbohydrate-Binding Module Family 5.
GH18. Glycoside Hydrolase Family 18.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76363; AAC76363; b3338.
BAE77953; BAE77953; BAE77953.
GeneID12932022.
947837.
KEGGecj:Y75_p3838.
eco:b3338.
PATRIC32122108. VBIEscCol129921_3431.

Organism-specific databases

EchoBASEEB1219.
EcoGeneEG11237. chiA.

Phylogenomic databases

eggNOGNOG12793.
HOGENOMHOG000125409.
KOK13381.
OMAGSIYKNA.
OrthoDBEOG6QVRC6.

Enzyme and pathway databases

BioCycEcoCyc:EG11237-MONOMER.
ECOL316407:JW3300-MONOMER.
MetaCyc:EG11237-MONOMER.

Gene expression databases

GenevestigatorP13656.

Family and domain databases

Gene3D2.10.10.20. 1 hit.
3.20.20.80. 1 hit.
InterProIPR003610. CBM_fam5/12.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF02839. CBM_5_12. 1 hit.
[Graphical view]
SMARTSM00495. ChtBD3. 7 hits.
[Graphical view]
SUPFAMSSF51055. SSF51055. 1 hit.
SSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Other

PROP13656.

Entry information

Entry nameCHIA_ECOLI
AccessionPrimary (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 14, 2014
This is version 130 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Escherichia coli

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