ID R4JYC7_CLOPA Unreviewed; 303 AA.
AC R4JYC7;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE SubName: Full=Putative xylanase/chitin deacetylase {ECO:0000313|EMBL:AGK95298.1};
GN ORFNames=Clopa_0232 {ECO:0000313|EMBL:AGK95298.1};
OS Clostridium pasteurianum BC1.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=86416 {ECO:0000313|EMBL:AGK95298.1, ECO:0000313|Proteomes:UP000013523};
RN [1] {ECO:0000313|EMBL:AGK95298.1, ECO:0000313|Proteomes:UP000013523}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BC1 {ECO:0000313|EMBL:AGK95298.1,
RC ECO:0000313|Proteomes:UP000013523};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Dunn J.,
RA Taghavi S., Francis A., van der Lelie D., Woyke T.;
RT "Complete sequence of chromosome of Clostridium pasteurianum BC1.";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the polysaccharide deacetylase family.
CC {ECO:0000256|ARBA:ARBA00010973}.
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; CP003261; AGK95298.1; -; Genomic_DNA.
DR RefSeq; WP_015613625.1; NC_021182.1.
DR AlphaFoldDB; R4JYC7; -.
DR STRING; 86416.Clopa_0232; -.
DR KEGG; cpas:Clopa_0232; -.
DR PATRIC; fig|86416.3.peg.205; -.
DR eggNOG; COG0726; Bacteria.
DR HOGENOM; CLU_030024_2_0_9; -.
DR OrthoDB; 9778320at2; -.
DR Proteomes; UP000013523; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR CDD; cd10918; CE4_NodB_like_5s_6s; 1.
DR Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR002509; NODB_dom.
DR PANTHER; PTHR34216; -; 1.
DR PANTHER; PTHR34216:SF3; POLY-BETA-1,6-N-ACETYL-D-GLUCOSAMINE N-DEACETYLASE; 1.
DR Pfam; PF01522; Polysacc_deac_1; 1.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR PROSITE; PS51677; NODB; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000313|EMBL:AGK95298.1};
KW Glycosidase {ECO:0000313|EMBL:AGK95298.1};
KW Hydrolase {ECO:0000313|EMBL:AGK95298.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Polysaccharide degradation {ECO:0000313|EMBL:AGK95298.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000013523};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Xylan degradation {ECO:0000313|EMBL:AGK95298.1}.
FT TRANSMEM 7..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 140..303
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
SQ SEQUENCE 303 AA; 34681 MW; 8BCD2971228220D3 CRC64;
MRTFKLRIVG IIVIILVLLC GIVTYNIITN KKNNNSSANN KQEILHKVSE IGVKKDEPKY
NKLREFKGEN LIHNDKQIPV LMYHSIADNS MVTDTASKSI ILPPEAFKQQ MQYLKDNGYT
TLTLDELYNF LKNGKPVPEK SVVLTFDDAY EDNYTNAYPI LKEFGFRATI FVITGGTDKI
GAYLTSAQLK EMDANGIDIQ SHTVNHEELD KLSLKEQQET LVQSKQFLEK LLNKKVDYIA
YPYGKYNNFT EQAAQNAGYT MAFTINNGWA NKDTNILFLN RVFVNALKGF DQFKERLTNP
NYQ
//
