Reviewed, UniProtKB/Swiss-Prot P13656 (CHIA_ECOLI)

Names and origin

Protein names

Recommended name:
    Probable bifunctional chitinase/lysozyme
Including the following 2 domains:
    1- Recommended name:
            Chitinase
              EC=3.2.1.14
    2- Recommended name:
            Lysozyme
              EC=3.2.1.17

Gene names

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

Organism

Escherichia coli (strain K12) [Complete 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.
Catalytic activity	Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins. 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.
Subcellular location	Periplasm.
Miscellaneous	In E.coli K12, chiA expression is repressed. The DNA-binding protein H-NS participates in the silencing of chiA.
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
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 electronic annotation. Source: UniProtKB-SubCell
Molecular function	chitin binding Inferred from electronic annotation. Source: UniProtKB-KW chitinase activity Inferred from electronic annotation. Source: EC 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	24	Potential
	Chain	25 – 897	873	Probable bifunctional chitinase/lysozyme		PRO_0000011907
Regions
	Domain	25 – 91	67	Chitin-binding type-3 1
	Domain	128 – 194	67	Chitin-binding type-3 2
	Domain	229 – 295	67	Chitin-binding type-3 3
	Domain	337 – 403	67	Chitin-binding type-3 4
	Domain	459 – 529	71	Chitin-binding type-3 5
	Region	647 – 897	251	Catalytic By similarity
	Compositional bias	93 – 101	9	Poly-Ser
Sites
	Active site	700	1	Proton donor By similarity
Amino acid modifications
	Disulfide bond	628 ↔ 673		By similarity
Experimental info
	Sequence conflict	874	1	F → I in AAC13985. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P13656-1 [UniParc]. Last modified November 1, 1995. Version 2. Checksum: 968D145BA1F954F3	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

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: 9278503] [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: 16738553] [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: 2661540] [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: 10419961] [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: 10760150] [Abstract] Cited for: CHARACTERIZATION. Strain: K12 / MG1655 / ATCC 47076.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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	AP_004452.1. NP_417797.1.
3D structure databases
ModBase	Search...
Protein family/group databases
CAZy	CBM5. Carbohydrate-Binding Module Family 5. GH18. Glycoside Hydrolase Family 18.
Genome annotation databases
GeneID	947837.
GenomeReviews	Gene locus JW3300 in contig AP009048_GR. Gene locus b3338 in contig U00096_GR.
KEGG	ecj:JW3300. eco:b3338.
Organism-specific databases
EchoBASE	EB1219.
EcoGene	EG11237. chiA.
CMR	Search...
Phylogenomic databases
HOGENOM	P13656.
OMA	P13656. YKNAWWV.
Enzyme and pathway databases
BioCyc	EcoCyc:EG11237-MON.
Family and domain databases
InterPro	IPR003610. CBM_5_12. IPR001579. Glyco_hydro_18_chit_AS. [Graphical view]
Pfam	PF02839. CBM_5_12. 1 hit. [Graphical view]
SMART	SM00495. ChtBD3. 7 hits. [Graphical view]
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:	June 16, 2009
This is version 88 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)