CHIA_FLAJ1
ID CHIA_FLAJ1 Reviewed; 1578 AA.
AC A5FB63;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Chitinase ChiA;
DE EC=3.2.1.14;
DE Flags: Precursor;
GN Name=chiA; OrderedLocusNames=Fjoh_4555;
OS Flavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / JCM 8514 / NBRC
OS 14942 / NCIMB 11054 / UW101) (Cytophaga johnsonae).
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=376686;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17061 / DSM 2064 / JCM 8514 / NBRC 14942 / NCIMB 11054 / UW101;
RX PubMed=19717629; DOI=10.1128/aem.01495-09;
RA McBride M.J., Xie G., Martens E.C., Lapidus A., Henrissat B., Rhodes R.G.,
RA Goltsman E., Wang W., Xu J., Hunnicutt D.W., Staroscik A.M., Hoover T.R.,
RA Cheng Y.Q., Stein J.L.;
RT "Novel features of the polysaccharide-digesting gliding bacterium
RT Flavobacterium johnsoniae as revealed by genome sequence analysis.";
RL Appl. Environ. Microbiol. 75:6864-6875(2009).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, DOMAIN, DISRUPTION
RP PHENOTYPE, AND GENE NAME.
RC STRAIN=ATCC 17061 / DSM 2064 / JCM 8514 / NBRC 14942 / NCIMB 11054 / UW101;
RX PubMed=24363341; DOI=10.1128/jb.01170-13;
RA Kharade S.S., McBride M.J.;
RT "Flavobacterium johnsoniae chitinase ChiA is required for chitin
RT utilization and is secreted by the type IX secretion system.";
RL J. Bacteriol. 196:961-970(2014).
CC -!- FUNCTION: Major extracellular chitinase, which is essential for chitin
CC utilization. {ECO:0000269|PubMed:24363341}.
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:24363341};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24363341}.
CC Note=Translocated across the cytoplasmic membrane via the Sec system,
CC and across the outer membrane via the type IX secretion system (T9SS).
CC -!- DOMAIN: The C-terminal region (CTD) is necessary and sufficient for
CC secretion by the T9SS. The CTD may be cleaved during secretion.
CC {ECO:0000269|PubMed:24363341}.
CC -!- DISRUPTION PHENOTYPE: Disruption results in cells that fail to digest
CC chitin. {ECO:0000269|PubMed:24363341}.
CC -!- MISCELLANEOUS: Western blot and liquid chromatography-tandem mass
CC spectrometry (LC-MS/MS) analyses suggest that ChiA could be
CC proteolytically processed into two GH18 domain-containing proteins.
CC However, it could be the result of non-specific digestion
CC (PubMed:24363341). {ECO:0000305|PubMed:24363341}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class II subfamily. {ECO:0000305}.
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DR EMBL; CP000685; ABQ07554.1; -; Genomic_DNA.
DR RefSeq; WP_012026520.1; NZ_MUGZ01000011.1.
DR AlphaFoldDB; A5FB63; -.
DR SASBDB; A5FB63; -.
DR SMR; A5FB63; -.
DR STRING; 376686.Fjoh_4555; -.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR EnsemblBacteria; ABQ07554; ABQ07554; Fjoh_4555.
DR KEGG; fjo:Fjoh_4555; -.
DR eggNOG; COG3325; Bacteria.
DR eggNOG; COG3469; Bacteria.
DR HOGENOM; CLU_245202_0_0_10; -.
DR OrthoDB; 1081028at2; -.
DR Proteomes; UP000006694; Chromosome.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0008061; F:chitin binding; IEA:InterPro.
DR GO; GO:0004568; F:chitinase activity; IDA:UniProtKB.
DR GO; GO:0006032; P:chitin catabolic process; IDA:UniProtKB.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.10; -; 2.
DR Gene3D; 3.10.50.10; -; 1.
DR InterPro; IPR013784; Carb-bd-like_fold.
DR InterPro; IPR008969; CarboxyPept-like_regulatory.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR029070; Chitinase_insertion_sf.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR Pfam; PF00704; Glyco_hydro_18; 2.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF49452; SSF49452; 1.
DR SUPFAM; SSF49464; SSF49464; 1.
DR SUPFAM; SSF51445; SSF51445; 2.
DR SUPFAM; SSF54556; SSF54556; 1.
DR PROSITE; PS01095; GH18_1; 2.
DR PROSITE; PS51910; GH18_2; 2.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Chitin degradation; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Repeat; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1578
FT /note="Chitinase ChiA"
FT /id="PRO_5000243200"
FT DOMAIN 25..466
FT /note="GH18 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT DOMAIN 485..536
FT /note="CNA-B"
FT DOMAIN 1142..1483
FT /note="GH18 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT REGION 26..446
FT /note="GH18N"
FT REGION 1142..1462
FT /note="GH18C"
FT REGION 1473..1578
FT /note="CTD"
FT ACT_SITE 162
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT ACT_SITE 1264
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 92..93
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 119..122
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 163
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 249..252
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 441
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
SQ SEQUENCE 1578 AA; 168921 MW; B721E73B4FCCF3A2 CRC64;
MKHYYRLLFL LLFPLLASAQ PAHGKKVVGY YAQWSIYARD FNVPKIDGSK LTHLNYSFYG
TTYDPAHPEN TKLKCLDTYA DFEHMEGGIP WDAPVKGNFY DLMKLKQKYP HLKILISVGG
WTKGQDLSPI AASPVARAAL AADMANFIVT YPFIDGFDID WEYPLSGGTD GTEIVNGMPV
PPQKYSPDDN KNLVLLLKAM RQAMPNKLVT IAAGNNVRNV SKQYLGPNNR AQYGMTEDIS
TYCDYITYFG YDFGGNWYDK TCYNAPLYAS GNPNDPLYGA TQSESLDELT NQYLNVIGFP
ANKLIMGLPF YGKKFDNVAA NSTNGLFVAA PRYIVPGCTN PQNPTGTWDG SGACEKSGSI
EICDLVGNPV TNSHAYLDPN TMMVTPSAAS AGWVRYFDNT TKVPYLYNST LKQFISYEDK
QSMDLKVQYI KSRNLAGGMI WELSQDTRGS IPNSLLNQVD TSFGSVVPGT VSISGSVKNG
SALVTDVTVE LRNASNAVIQ TVVSANGNFA FNNLTSGQNY SLTALKATYT FTPVTLVNVT
VNQTAVVING TQPTYTVSGT VLDGSTPVSG VTVTAVSGST TLTAVSNASG VYSIAGLTAG
LNFTVTAAKS GFSYAPASTV YNAIDSNKTL NFTQGAPVVN YTVSGTVLNS TTPVSGVTVT
ASFTGGSYAA VTNASGTYSL SLPSGGNYTV TAALTGQTFT PASTVYSNLN ANKTLNFTQD
VVVSTSKISG TVKNGTNPVA GAKVELVLPW TDNTHNWKSV IATTDAQGKY SFDNSVVDGY
TQVLSLKLNS WQNGEVAYYP NNLANFAVPA NPTVYNFNTS STAKSALAAA ANLISGTVKN
GTTPVAGAKV EIVLPWTDNT HNWKSVLATT DASGNYSFDN SVVAGYTQIL SLKLNGWENG
DVTYYPNNLA NFAVPTTPTI YNFNRQAVVA TKPVVTITAP TASAIAINLG SAINFVASVG
LSAVDATTIS SVVFSLDGQS LSTANSSGTY TAAWTPAANQ FSLSHTLTVT ATASNGTTDS
KTYSFTLTCS GANCPNALPV ITWNSPSNTT VYQNTFQVVP ISVTAVDSDG TVSGVTITIN
GGTFNMTAGT NNTYTYNFTP SAYQDYPVVI KATDNKSGVT TLNNTIKIAT VSTNRFIPLP
SKIILGYAHS WENAGAPFLY FSQMVGSKFN VVDYSFVETV NRDGYTPILT TNDTRYLTNG
VFNKQLLKND IKSLRDSGVP VIVSIGGQNG HVVLDNVTQK NIFVNGLKAI IDEYQFDGVD
IDFEGGSMNF NAGGLRDISY AGISAYPRLK NVVDAFKELK AYYGPGFLLT AAPETQYVQG
GYTTYTDTFG SFLPIIQNLR NELDLLAVQL YNTGGENGLD GQYYGTAKKS NMVTALTDMV
IKGYNIASTG MRFDGLPASK VLIALPACPS AAGSGYLTPT EGINAMHYLR TGTTFSGRTY
TMQPGGPYPS LRGLMTWSVN WDASSCGNSS ELSKAYAAYF ASQTAAKTLV LDDISAKSNA
TIAYFKNNAL SVTNENEDIA QVDVFNVLGQ NLVSHRNVQN NKEVLLHNQS FSSKQLFLVV
VTDKAGNKKS FKVMNFLN
