CHIA_ECOLI
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 03-AUG-2022, entry version 171.
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; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC 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_LN832404.1.
DR AlphaFoldDB; P13656; -.
DR SMR; P13656; -.
DR BioGRID; 4261016; 167.
DR DIP; DIP-9276N; -.
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; P13656; -.
DR PRIDE; P13656; -.
DR EnsemblBacteria; AAC76363; AAC76363; b3338.
DR EnsemblBacteria; BAE77953; BAE77953; BAE77953.
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; CATSAID; -.
DR BioCyc; EcoCyc:EG11237-MON; -.
DR BioCyc; MetaCyc:EG11237-MON; -.
DR PRO; PR:P13656; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0042597; C:periplasmic space; IDA:EcoCyc.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR GO; GO:0008843; F:endochitinase activity; IDA:EcoCyc.
DR GO; GO:0003796; F:lysozyme activity; IEA:UniProtKB-EC.
DR GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR003610; CBM_fam5/12.
DR InterPro; IPR036573; CBM_sf_5/12.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF02839; CBM_5_12; 1.
DR SMART; SM00495; ChtBD3; 7.
DR SUPFAM; SSF51055; SSF51055; 1.
DR SUPFAM; SSF51445; SSF51445; 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 182..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..214
FT /note="Pro 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
