ID   CHIA_ECOLI              Reviewed;         897 AA.
AC   P13656; Q2M703;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   04-NOV-2026, entry version 190.
DE   RecName: Full=Probable bifunctional chitinase/lysozyme;
DE   Includes:
DE     RecName: Full=Chitinase;
DE              EC=3.2.1.14;
DE   Includes:
DE     RecName: Full=Lysozyme;
DE              EC=3.2.1.17;
DE   Flags: Precursor;
GN   Name=chiA; Synonyms=yheB; OrderedLocusNames=b3338, JW3300;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 874-897.
RC   STRAIN=K12;
RX   PubMed=2661540; DOI=10.1128/jb.171.7.3940-3947.1989;
RA   Andrews S.C., Harrison P.M., Guest J.R.;
RT   "Cloning, sequencing, and mapping of the bacterioferritin gene (bfr) of
RT   Escherichia coli K-12.";
RL   J. Bacteriol. 171:3940-3947(1989).
RN   [4]
RP   CHITIN-BINDING PROPERTIES.
RX   PubMed=10419961; DOI=10.1128/jb.181.15.4611-4616.1999;
RA   Simpson H.D., Barras F.;
RT   "Functional analysis of the carbohydrate-binding domains of Erwinia
RT   chrysanthemi Cel5 (Endoglucanase Z) and an Escherichia coli putative
RT   chitinase.";
RL   J. Bacteriol. 181:4611-4616(1999).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TRANSCRIPTIONAL
RP   REGULATION, AND GENE NAME.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=10760150; DOI=10.1046/j.1365-2958.2000.01817.x;
RA   Francetic O., Badaut C., Rimsky S., Pugsley A.P.;
RT   "The ChiA (YheB) protein of Escherichia coli K-12 is an endochitinase whose
RT   gene is negatively controlled by the nucleoid-structuring protein H-NS.";
RL   Mol. Microbiol. 35:1506-1517(2000).
RN   [6]
RP   SECRETION VIA THE GSP SECRETON.
RC   STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX   PubMed=11118204; DOI=10.1093/emboj/19.24.6697;
RA   Francetic O., Belin D., Badaut C., Pugsley A.P.;
RT   "Expression of the endogenous type II secretion pathway in Escherichia coli
RT   leads to chitinase secretion.";
RL   EMBO J. 19:6697-6703(2000).
CC   -!- FUNCTION: Bifunctional enzyme with lysozyme/chitinase activity.
CC       {ECO:0000269|PubMed:10760150}.
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         Evidence={ECO:0000269|PubMed:10760150};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic
CC         acid and N-acetyl-D-glucosamine residues in a peptidoglycan and
CC         between N-acetyl-D-glucosamine residues in chitodextrins.;
CC         EC=3.2.1.17; Evidence={ECO:0000269|PubMed:10760150};
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:10760150}.
CC       Note=Secreted via the Gsp type II secretion machinery under conditions
CC       of derepressed gsp gene expression.
CC   -!- INDUCTION: Silenced by the DNA-binding protein H-NS under standard
CC       growth conditions. {ECO:0000269|PubMed:10760150}.
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; U18997; AAA58135.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76363.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77953.1; -; Genomic_DNA.
DR   EMBL; M27176; AAC13985.1; -; mRNA.
DR   PIR; E65127; E65127.
DR   RefSeq; NP_417797.1; NC_000913.3.
DR   RefSeq; WP_000773156.1; NZ_CP009789.1.
DR   AlphaFoldDB; P13656; -.
DR   SMR; P13656; -.
DR   BioGRID; 4261016; 168.
DR   DIP; DIP-9276N; -.
DR   FunCoup; P13656; 94.
DR   IntAct; P13656; 2.
DR   STRING; 511145.b3338; -.
DR   CAZy; CBM5; Carbohydrate-Binding Module Family 5.
DR   CAZy; GH18; Glycoside Hydrolase Family 18.
DR   PaxDb; 511145-b3338; -.
DR   EnsemblBacteria; AAC76363; AAC76363; b3338.
DR   GeneID; 947837; -.
DR   KEGG; ecj:JW3300; -.
DR   KEGG; eco:b3338; -.
DR   PATRIC; fig|1411691.4.peg.3393; -.
DR   EchoBASE; EB1219; -.
DR   eggNOG; COG3979; Bacteria.
DR   HOGENOM; CLU_019399_2_0_6; -.
DR   InParanoid; P13656; -.
DR   OMA; ADHESIN; -.
DR   OrthoDB; 6018988at2; -.
DR   BioCyc; EcoCyc:EG11237-MONOMER; -.
DR   BioCyc; MetaCyc:EG11237-MONOMER; -.
DR   PRO; PR:P13656; -.
DR   Proteomes; UP000000625; Chromosome.
DR   AbasyAtlas; P13656; -.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0008843; F:endochitinase activity; IDA:EcoCyc.
DR   GO; GO:0003796; F:lysozyme activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd12215; ChiC_BD; 1.
DR   CDD; cd06543; GH18_PF-ChiA-like; 1.
DR   FunFam; 3.20.20.80:FF:000118; Probable bifunctional chitinase/lysozyme; 1.
DR   Gene3D; 2.10.10.20; Carbohydrate-binding module superfamily 5/12; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR003610; CBM5/12.
DR   InterPro; IPR036573; CBM_sf_5/12.
DR   InterPro; IPR052750; GH18_Chitinase.
DR   InterPro; IPR017853; GH_hydrolase_sf.
DR   InterPro; IPR001223; Glyco_hydro18_cat.
DR   PANTHER; PTHR42976; BIFUNCTIONAL CHITINASE/LYSOZYME-RELATED; 1.
DR   PANTHER; PTHR42976:SF1; GH18 DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   Pfam; PF02839; CBM_5_12; 1.
DR   Pfam; PF00704; Glyco_hydro_18; 1.
DR   SMART; SM00495; ChtBD3; 7.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51055; Carbohydrate binding domain; 1.
DR   PROSITE; PS51910; GH18_2; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Chitin degradation; Chitin-binding;
KW   Disulfide bond; Glycosidase; Hydrolase; Multifunctional enzyme; Periplasm;
KW   Polysaccharide degradation; Reference proteome; Repeat; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..897
FT                   /note="Probable bifunctional chitinase/lysozyme"
FT                   /id="PRO_0000011907"
FT   DOMAIN          25..91
FT                   /note="Chitin-binding type-3 1"
FT   DOMAIN          128..194
FT                   /note="Chitin-binding type-3 2"
FT   DOMAIN          229..295
FT                   /note="Chitin-binding type-3 3"
FT   DOMAIN          337..403
FT                   /note="Chitin-binding type-3 4"
FT   DOMAIN          459..529
FT                   /note="Chitin-binding type-3 5"
FT   DOMAIN          586..877
FT                   /note="GH18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   REGION          90..127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          182..222
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          287..333
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        95..111
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        113..127
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        182..197
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        198..216
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        309..318
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        322..333
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        700
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   DISULFID        628..673
FT                   /evidence="ECO:0000250"
FT   CONFLICT        874
FT                   /note="F -> I (in Ref. 3; AAC13985)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   897 AA;  97058 MW;  968D145BA1F954F3 CRC64;
     MKLNIFTKSM IGMGLVCSAL PALAMEAWNN QQGGNKYQVI FDGKIYENAW WVSSTNCPGK
     AKANDATNPW RLKRTATAAE ISQFGNTLSC EKSGSSSSSN SNTPASNTPA NGGSATPAQG
     TVPSNSSVVA WNKQQGGQTW YVVFNGAVYK NAWWVASSNC PGDAKSNDAS NPWRYVRAAT
     ATEISETSNP QSCTSAPQPS PDVKPAPDVK PAPDVQPAPA DKSNDNYAVV AWKGQEGSST
     WYVIYNGGIY KNAWWVGAAN CPGDAKENDA SNPWRYVRAA TATEISQYGN PGSCSVKPDN
     NGGAVTPVDP TPETPVTPTP DNSEPSTPAD SVNDYSLQAW SGQEGSEIYH VIFNGNVYKN
     AWWVGSKDCP RGTSAENSNN PWRLERTATA AELSQYGNPT TCEIDNGGVI VADGFQASKA
     YSADSIVDYN DAHYKTSVDQ DAWGFVPGGD NPWKKYEPAK AWSASTVYVK GDRVVVDGQA
     YEALFWTQSD NPALVANQNA TGSNSRPWKP LGKAQSYSNE ELNNAPQFNP ETLYASDTLI
     RFNGVNYISQ SKVQKVSPSD SNPWRVFVDW TGTKERVGTP KKAWPKHVYA PYVDFTLNTI
     PDLAALAKNH NVNHFTLAFV VSKDANTCLP TWGTAYGMQN YAQYSKIKAL REAGGDVMLS
     IGGANNAPLA ASCKNVDDLM QHYYDIVDNL NLKVLDFDIE GTWVADQASI ERRNLAVKKV
     QDKWKSEGKD IAIWYTLPIL PTGLTPEGMN VLSDAKAKGV ELAGVNVMTM DYGNAICQSA
     NTEGQNIHGK CATSAIANLH SQLKGLHPNK SDAEIDAMMG TTPMVGVNDV QGEVFYLSDA
     RLVMQDAQKR NLGMVGIWSI ARDLPGGTNL SPEFHGLTKE QAPKYAFSEI FAPFTKQ
//