ID Q9ZIX3_9GAMM Unreviewed; 525 AA.
AC Q9ZIX3;
DT 01-MAY-1999, integrated into UniProtKB/TrEMBL.
DT 01-MAY-1999, sequence version 1.
DT 24-JAN-2024, entry version 65.
DE SubName: Full=Chitinase B {ECO:0000313|EMBL:AAC79666.1};
GN Name=chiB {ECO:0000313|EMBL:AAC79666.1};
OS Pseudoalteromonas sp. S9.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=55516 {ECO:0000313|EMBL:AAC79666.1};
RN [1] {ECO:0000313|EMBL:AAC79666.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=9251187;
RA Techkarnjanaruk S., Pongpattanakitshote S., Goodman A.E.;
RT "Use of a promoterless lacZ gene insertion to investigate chitinase gene
RT expression in the marine bacterium Pseudoalteromonas sp. strain S9.";
RL Appl. Environ. Microbiol. 63:2989-2996(1997).
RN [2] {ECO:0000313|EMBL:AAC79666.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=10220172;
RA Techkarnjanaruk S., Goodman A.E.;
RT "Multiple genes involved in chitin degradation from the marine bacterium
RT Pseudoalteromonas sp. strain S91.";
RL Microbiology 145:925-934(1999).
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DR EMBL; AH007017; AAC79666.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9ZIX3; -.
DR CAZy; AA10; Auxiliary Activities 10.
DR CAZy; CBM5; Carbohydrate-Binding Module Family 5.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd12215; ChiC_BD; 2.
DR Gene3D; 3.30.70.2150; -; 1.
DR Gene3D; 2.10.10.20; Carbohydrate-binding module superfamily 5/12; 2.
DR Gene3D; 2.70.50.50; chitin-binding protein cbp21; 1.
DR InterPro; IPR003610; CBM_fam5/12.
DR InterPro; IPR036573; CBM_sf_5/12.
DR InterPro; IPR004302; Cellulose/chitin-bd_N.
DR InterPro; IPR041029; GbpA_2.
DR InterPro; IPR014756; Ig_E-set.
DR PANTHER; PTHR34823:SF1; CHITIN-BINDING TYPE-4 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR34823; GLCNAC-BINDING PROTEIN A; 1.
DR Pfam; PF02839; CBM_5_12; 2.
DR Pfam; PF18416; GbpA_2; 1.
DR Pfam; PF03067; LPMO_10; 1.
DR SMART; SM00495; ChtBD3; 2.
DR SUPFAM; SSF51055; Carbohydrate binding domain; 2.
DR SUPFAM; SSF81296; E set domains; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Chitin-binding {ECO:0000256|ARBA:ARBA00022669};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..525
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004337479"
FT DOMAIN 436..478
FT /note="Chitin-binding type-3"
FT /evidence="ECO:0000259|SMART:SM00495"
FT DOMAIN 483..525
FT /note="Chitin-binding type-3"
FT /evidence="ECO:0000259|SMART:SM00495"
SQ SEQUENCE 525 AA; 57501 MW; E3642585D19B42B6 CRC64;
MNTKFNISVL SGSVLLACIA APFNASAHGY MDSPKARQAF CQAQGGYWWP EDGSNIPNLA
CRAAFLESGH VQFIQEHEFA VNTPDYLNQS AVEANVPDGT LCAAGSHEKR GMNLPSAHWQ
KTVVTPNANG EIQVRYRATT PHNPSFWQFY LTKPGFNPAT DTLTWQNIEL IQSHDNIEFV
KDPDGKRYYE MSVAIPAERV GDAVLYSRWQ RVDVVGEGFY NCSDIIIERD TVTPVDWFPL
GYFVRQGQSA NAGDTVQVRL FDATGLEVVN QLFAVHASNQ ATWQSELAAK LNLDYASELQ
IGVKNASGDI VFDEANLASN QVYATSSDHS FALSVIAASE NTAPNVNPVA DVVMDEGSQT
LVHVHAFDDE NDPLSYQFTV PNEFTYSVDG PNLTLNAPEV SANANFAIQV SVSDGKLSTP
ASFTVTVNDT ATNPDVPAWD ASKAYNAGDK VSYLGTVYKA KWWVQGEKPN SSDAWQSLSQ
STDDAWLSSK AYSAGDIVSH NSQKYQARWW TKGDEPGTAS VWQTL
//
