ID Q0ZKA9_AERHY Unreviewed; 640 AA.
AC Q0ZKA9;
DT 22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT 22-AUG-2006, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Basic endochitinase {ECO:0000313|EMBL:ABD59015.1};
OS Aeromonas hydrophila.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=644 {ECO:0000313|EMBL:ABD59015.1};
RN [1] {ECO:0000313|EMBL:ABD59015.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SSU {ECO:0000313|EMBL:ABD59015.1};
RX PubMed=16790746; DOI=10.1128/IAI.00402-06;
RA Pillai L., Sha J., Erova T.E., Fadl A.A., Khajanchi B.K., Chopra A.K.;
RT "Molecular and functional characterization of a ToxR-regulated lipoprotein
RT from a clinical isolate of Aeromonas hydrophila.";
RL Infect. Immun. 74:3742-3755(2006).
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DR EMBL; DQ398103; ABD59015.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0ZKA9; -.
DR CAZy; CBM5; Carbohydrate-Binding Module Family 5.
DR CAZy; CBM73; Carbohydrate-Binding Module Family 73.
DR CAZy; GH19; Glycoside Hydrolase Family 19.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004568; F:chitinase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro.
DR GO; GO:0006032; P:chitin catabolic process; IEA:InterPro.
DR CDD; cd12214; ChiA1_BD; 1.
DR CDD; cd12215; ChiC_BD; 1.
DR CDD; cd00325; chitinase_GH19; 1.
DR Gene3D; 1.10.530.10; -; 1.
DR Gene3D; 2.10.10.20; Carbohydrate-binding module superfamily 5/12; 1.
DR Gene3D; 3.30.20.10; Endochitinase, domain 2; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR003610; CBM_fam5/12.
DR InterPro; IPR036573; CBM_sf_5/12.
DR InterPro; IPR000726; Glyco_hydro_19_cat.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR022409; PKD/Chitinase_dom.
DR InterPro; IPR035986; PKD_dom_sf.
DR PANTHER; PTHR22595:SF208; CHITINASE; 1.
DR PANTHER; PTHR22595; CHITINASE-RELATED; 1.
DR Pfam; PF00182; Glyco_hydro_19; 1.
DR Pfam; PF18911; PKD_4; 1.
DR SMART; SM00495; ChtBD3; 2.
DR SMART; SM00089; PKD; 1.
DR SUPFAM; SSF51055; Carbohydrate binding domain; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
DR SUPFAM; SSF49299; PKD domain; 1.
PE 4: Predicted;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023024};
KW Chitin degradation {ECO:0000256|ARBA:ARBA00023024};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023024};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..640
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004179428"
FT DOMAIN 24..69
FT /note="Chitin-binding type-3"
FT /evidence="ECO:0000259|SMART:SM00495"
FT DOMAIN 487..576
FT /note="PKD/Chitinase"
FT /evidence="ECO:0000259|SMART:SM00089"
FT DOMAIN 585..636
FT /note="Chitin-binding type-3"
FT /evidence="ECO:0000259|SMART:SM00495"
FT REGION 73..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 640 AA; 68987 MW; D844FBD86A486627 CRC64;
MMTRKSSVAT LLAALCLSGQ LWAATPYDIN QGYAGGSQVS FNGQIYEAKW YANPGQSPGV
QVANEWDSPW ALMGEGEVTP PAGGEGVTPP EQGGSGTADG SPVYLSQSEL DAREQALTDF
PAMTAVKASI ATRDNTVVEA VAPGLPLNPA NVKRVEGLLS ESQFNFLFPL RAPEYTYRGF
LQAVAKFPAF CGDYSDGRNA EAICRKSLAT MFAHFAQETG GHENWRPEPE WRQGLVWVRE
MGWTEQMRGG YNAECNPEVW QGQQWPCGKF DNGEFKSYFG RGAKQLSYNY NYGPFSEAMF
GTVRTLLDNP EKVADTWLNL ASAVFFFVYP QPPKPSMLHV IDGTWQPNAH DRQNGLVPGF
GVTTQIINGG VECGGAAEHA QSQNRITYYQ AQAQYLGVPV PADEVLGCKN MKVFDEAGAG
ALPIYWENDW SYVPGNPNGG KSYACKLVGY QTRFSAFKER DYSRCVQHFF PEVVIEDNGG
GTNLPPVASI SGPSEALGGA TVLLSGQGSS DPEGKPLSYA WTLPAGASAS DLTQSTLSAT
LPPTPASDTR YGFVLKVTDD KGLSRSATHE ILIKGSGGTT PPDGNPPYQE GTAYKAGDKV
SNLGGNYQCK PHPYTGWCAG AAWAYEPGKG TAWSDAWIKL
//