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P13656

- CHIA_ECOLI

UniProt

P13656 - CHIA_ECOLI

Protein

Probable bifunctional chitinase/lysozyme

Gene

chiA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 2 (01 Nov 1995)
      Previous versions | rss
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    Functioni

    Bifunctional enzyme with lysozyme/chitinase activity.1 Publication

    Catalytic activityi

    Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.1 Publication
    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.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei700 – 7001Proton donorBy similarity

    GO - Molecular functioni

    1. carbohydrate binding Source: InterPro
    2. chitin binding Source: UniProtKB-KW
    3. endochitinase activity Source: EcoCyc
    4. lysozyme activity Source: UniProtKB-EC

    GO - Biological processi

    1. chitin catabolic process Source: UniProtKB-KW
    2. polysaccharide catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Chitin degradation, Polysaccharide degradation

    Keywords - Ligandi

    Chitin-binding

    Enzyme and pathway databases

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

    Protein family/group databases

    CAZyiCBM5. Carbohydrate-Binding Module Family 5.
    GH18. Glycoside Hydrolase Family 18.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable bifunctional chitinase/lysozyme
    Including the following 2 domains:
    Chitinase (EC:3.2.1.14)
    Lysozyme (EC:3.2.1.17)
    Gene namesi
    Name:chiA
    Synonyms:yheB
    Ordered Locus Names:b3338, JW3300
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG11237. chiA.

    Subcellular locationi

    Periplasm 1 Publication
    Note: Secreted via the Gsp type II secretion machinery under conditions of derepressed gsp gene expression.

    GO - Cellular componenti

    1. extracellular region Source: InterPro
    2. outer membrane-bounded periplasmic space Source: EcoCyc
    3. periplasmic space Source: EcoCyc

    Keywords - Cellular componenti

    Periplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424Sequence AnalysisAdd
    BLAST
    Chaini25 – 897873Probable bifunctional chitinase/lysozymePRO_0000011907Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi628 ↔ 673By similarity

    Keywords - PTMi

    Disulfide bond

    Expressioni

    Inductioni

    Silenced by the DNA-binding protein H-NS under standard growth conditions.1 Publication

    Gene expression databases

    GenevestigatoriP13656.

    Interactioni

    Protein-protein interaction databases

    DIPiDIP-9276N.
    IntActiP13656. 1 interaction.
    STRINGi511145.b3338.

    Structurei

    3D structure databases

    ProteinModelPortaliP13656.
    SMRiP13656. Positions 457-509, 585-896.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini25 – 9167Chitin-binding type-3 1Add
    BLAST
    Domaini128 – 19467Chitin-binding type-3 2Add
    BLAST
    Domaini229 – 29567Chitin-binding type-3 3Add
    BLAST
    Domaini337 – 40367Chitin-binding type-3 4Add
    BLAST
    Domaini459 – 52971Chitin-binding type-3 5Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni647 – 897251CatalyticBy similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi93 – 1019Poly-Ser

    Sequence similaritiesi

    Contains 5 chitin-binding type-3 domains.Curated

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG12793.
    HOGENOMiHOG000125409.
    KOiK13381.
    OMAiGSIYKNA.
    OrthoDBiEOG6QVRC6.

    Family and domain databases

    Gene3Di2.10.10.20. 1 hit.
    3.20.20.80. 1 hit.
    InterProiIPR003610. CBM_fam5/12.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF02839. CBM_5_12. 1 hit.
    [Graphical view]
    SMARTiSM00495. ChtBD3. 7 hits.
    [Graphical view]
    SUPFAMiSSF51055. SSF51055. 1 hit.
    SSF51445. SSF51445. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P13656-1 [UniParc]FASTAAdd to Basket

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    MKLNIFTKSM IGMGLVCSAL PALAMEAWNN QQGGNKYQVI FDGKIYENAW    50
    WVSSTNCPGK AKANDATNPW RLKRTATAAE ISQFGNTLSC EKSGSSSSSN 100
    SNTPASNTPA NGGSATPAQG TVPSNSSVVA WNKQQGGQTW YVVFNGAVYK 150
    NAWWVASSNC PGDAKSNDAS NPWRYVRAAT ATEISETSNP QSCTSAPQPS 200
    PDVKPAPDVK PAPDVQPAPA DKSNDNYAVV AWKGQEGSST WYVIYNGGIY 250
    KNAWWVGAAN CPGDAKENDA SNPWRYVRAA TATEISQYGN PGSCSVKPDN 300
    NGGAVTPVDP TPETPVTPTP DNSEPSTPAD SVNDYSLQAW SGQEGSEIYH 350
    VIFNGNVYKN AWWVGSKDCP RGTSAENSNN PWRLERTATA AELSQYGNPT 400
    TCEIDNGGVI VADGFQASKA YSADSIVDYN DAHYKTSVDQ DAWGFVPGGD 450
    NPWKKYEPAK AWSASTVYVK GDRVVVDGQA YEALFWTQSD NPALVANQNA 500
    TGSNSRPWKP LGKAQSYSNE ELNNAPQFNP ETLYASDTLI RFNGVNYISQ 550
    SKVQKVSPSD SNPWRVFVDW TGTKERVGTP KKAWPKHVYA PYVDFTLNTI 600
    PDLAALAKNH NVNHFTLAFV VSKDANTCLP TWGTAYGMQN YAQYSKIKAL 650
    REAGGDVMLS IGGANNAPLA ASCKNVDDLM QHYYDIVDNL NLKVLDFDIE 700
    GTWVADQASI ERRNLAVKKV QDKWKSEGKD IAIWYTLPIL PTGLTPEGMN 750
    VLSDAKAKGV ELAGVNVMTM DYGNAICQSA NTEGQNIHGK CATSAIANLH 800
    SQLKGLHPNK SDAEIDAMMG TTPMVGVNDV QGEVFYLSDA RLVMQDAQKR 850
    NLGMVGIWSI ARDLPGGTNL SPEFHGLTKE QAPKYAFSEI FAPFTKQ 897
    Length:897
    Mass (Da):97,058
    Last modified:November 1, 1995 - v2
    Checksum:i968D145BA1F954F3
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti874 – 8741F → I in AAC13985. (PubMed:2661540)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U18997 Genomic DNA. Translation: AAA58135.1.
    U00096 Genomic DNA. Translation: AAC76363.1.
    AP009048 Genomic DNA. Translation: BAE77953.1.
    M27176 mRNA. Translation: AAC13985.1.
    PIRiE65127.
    RefSeqiNP_417797.1. NC_000913.3.
    YP_492094.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76363; AAC76363; b3338.
    BAE77953; BAE77953; BAE77953.
    GeneIDi12932022.
    947837.
    KEGGiecj:Y75_p3838.
    eco:b3338.
    PATRICi32122108. VBIEscCol129921_3431.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U18997 Genomic DNA. Translation: AAA58135.1 .
    U00096 Genomic DNA. Translation: AAC76363.1 .
    AP009048 Genomic DNA. Translation: BAE77953.1 .
    M27176 mRNA. Translation: AAC13985.1 .
    PIRi E65127.
    RefSeqi NP_417797.1. NC_000913.3.
    YP_492094.1. NC_007779.1.

    3D structure databases

    ProteinModelPortali P13656.
    SMRi P13656. Positions 457-509, 585-896.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-9276N.
    IntActi P13656. 1 interaction.
    STRINGi 511145.b3338.

    Protein family/group databases

    CAZyi CBM5. Carbohydrate-Binding Module Family 5.
    GH18. Glycoside Hydrolase Family 18.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76363 ; AAC76363 ; b3338 .
    BAE77953 ; BAE77953 ; BAE77953 .
    GeneIDi 12932022.
    947837.
    KEGGi ecj:Y75_p3838.
    eco:b3338.
    PATRICi 32122108. VBIEscCol129921_3431.

    Organism-specific databases

    EchoBASEi EB1219.
    EcoGenei EG11237. chiA.

    Phylogenomic databases

    eggNOGi NOG12793.
    HOGENOMi HOG000125409.
    KOi K13381.
    OMAi GSIYKNA.
    OrthoDBi EOG6QVRC6.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG11237-MONOMER.
    ECOL316407:JW3300-MONOMER.
    MetaCyc:EG11237-MONOMER.

    Miscellaneous databases

    PROi P13656.

    Gene expression databases

    Genevestigatori P13656.

    Family and domain databases

    Gene3Di 2.10.10.20. 1 hit.
    3.20.20.80. 1 hit.
    InterProi IPR003610. CBM_fam5/12.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF02839. CBM_5_12. 1 hit.
    [Graphical view ]
    SMARTi SM00495. ChtBD3. 7 hits.
    [Graphical view ]
    SUPFAMi SSF51055. SSF51055. 1 hit.
    SSF51445. SSF51445. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. 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.

    Entry informationi

    Entry nameiCHIA_ECOLI
    AccessioniPrimary (citable) accession number: P13656
    Secondary accession number(s): Q2M703
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 131 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3