ID A0A0P8WAQ4_9CLOT Unreviewed; 2215 AA.
AC A0A0P8WAQ4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Endo-1,4-beta-xylanase A {ECO:0000313|EMBL:KPU45031.1};
DE EC=3.2.1.8 {ECO:0000313|EMBL:KPU45031.1};
GN Name=xynA1 {ECO:0000313|EMBL:KPU45031.1};
GN ORFNames=OXPF_15090 {ECO:0000313|EMBL:KPU45031.1};
OS Oxobacter pfennigii.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; Oxobacter.
OX NCBI_TaxID=36849 {ECO:0000313|EMBL:KPU45031.1, ECO:0000313|Proteomes:UP000050326};
RN [1] {ECO:0000313|EMBL:KPU45031.1, ECO:0000313|Proteomes:UP000050326}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3222 {ECO:0000313|EMBL:KPU45031.1,
RC ECO:0000313|Proteomes:UP000050326};
RA Poehlein A., Bengelsdorf F.R., Schiel-Bengelsdorf B., Duerre P., Daniel R.;
RT "Genome sequence of Oxobacter pfennigii DSM 3222.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPU45031.1}.
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DR EMBL; LKET01000028; KPU45031.1; -; Genomic_DNA.
DR STRING; 36849.OXPF_15090; -.
DR PATRIC; fig|36849.3.peg.1599; -.
DR OrthoDB; 1703838at2; -.
DR Proteomes; UP000050326; Unassembled WGS sequence.
DR GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR CDD; cd00118; LysM; 1.
DR Gene3D; 2.10.270.10; Cholin Binding; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 6.
DR Gene3D; 2.60.40.4270; Listeria-Bacteroides repeat domain; 1.
DR Gene3D; 3.10.350.10; LysM domain; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013378; InlB-like_B-rpt.
DR InterPro; IPR042229; Listeria/Bacterioides_rpt_sf.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR InterPro; IPR001119; SLH_dom.
DR NCBIfam; NF012200; choice_anch_D; 3.
DR NCBIfam; TIGR02543; List_Bact_rpt; 1.
DR PANTHER; PTHR37833; LIPOPROTEIN-RELATED; 1.
DR PANTHER; PTHR37833:SF1; LIPOPROTEIN-RELATED; 1.
DR Pfam; PF09479; Flg_new; 1.
DR Pfam; PF01476; LysM; 1.
DR Pfam; PF00395; SLH; 3.
DR SMART; SM00257; LysM; 1.
DR SUPFAM; SSF69360; Cell wall binding repeat; 1.
DR SUPFAM; SSF54106; LysM domain; 1.
DR PROSITE; PS51782; LYSM; 1.
DR PROSITE; PS51272; SLH; 3.
PE 4: Predicted;
KW Carbohydrate metabolism {ECO:0000313|EMBL:KPU45031.1};
KW Glycosidase {ECO:0000313|EMBL:KPU45031.1};
KW Hydrolase {ECO:0000313|EMBL:KPU45031.1};
KW Polysaccharide degradation {ECO:0000313|EMBL:KPU45031.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000050326};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000313|EMBL:KPU45031.1}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..2215
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006153270"
FT DOMAIN 1930..1988
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT DOMAIN 1991..2054
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT DOMAIN 2057..2120
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT DOMAIN 2168..2212
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT REGION 73..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1684..1725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1684..1701
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2215 AA; 227916 MW; DC59C77DB5433643 CRC64;
MNKRLLSMFL ALCMIVTMLP VSAMAEEIHT TIGGSGEIIS FAPLTETQKA VSLGTSIEDL
ELPETLTATV RTAVPADENS TQDSGSPETA TPTTASEPKW KETTGDIPVT WNSPDYDPNT
GGVYAFTPVI EGYTVSAPLP EISVTVGAAM LIDKTQAREK PTLTAQSAET RDFYIVLVGE
RMSPSSLGFL SNDCGLSPIS TADSDDYAPD DDGNAMVKSY LYRAAVGQTI TFHWGLGEDG
FRGLLYAYYA DDEPILDATF GAQWAVLRNS GLIGFATGAK QPIGLQFEVA SPPVLLAPDA
VTNYDIWVGG VQVASTNASN VLDDGTVTYD SDTNTLTLNN AAITTSHMVS AANYGIYAPF
GLNLKLVGAN SIALPHSGSY SVYGIASDES DLQISAEEHG SLTVTAGNNF GIYSNNLTIN
SGAITTVSSV IFVRESVSIS GGTVTSTGGT QGIVGKTITV SGGTMTASGS GKALTNSVGS
PDFTGMQVTA SLNESGTPTV SYDAANLATY KYIKVEPAVT PPVLSEVADL TALQSAIDGA
AGDLNLKLSD SYSGTGTITI PNTCSYDITI DLNGKTLNGG SVSAIKHLGS GTLTITDSAG
GGMVTSGTMG TIFVSGSGTV NLSGGTVRSI GGTEYVAIWI GSNNTLNITD GTVSATGFRG
IAIYSQNGTV NISGGAVSAT GNNGKAILGE TGASGQLNIS GGTVSAAGTG GIAIDHANAT
IQNGTTTIIQ GSSGAIAYAP TLDSGVQGGA STNYDGSGSV AYNTAHWPTY KYLKFGLDVI
SPVLSAGNVS RTSDTEGTID FTTDKAGTAY YLVVNSGVSA PTSAEVKEGA SLGAVSAGAV
TNQSVTLTAG AKDIYVVVED SAGNISTPLK IEAAAYVAPD TTPPVLSAGN VTRTSDTAAT
IGFITDEAGT AYYLVVNSGE STPTSAAVKN TGISLGSVSG TVTDKAVTLA AGAKDIYVVV
EDLANNISAP LKIEAAALTY TITASPISKH FGSLAVGYTA PAAQTVTIRN TGNSSVTLTP
PTSTNYTIGA LSTTTLAANG TATFTVAPKT GLSVGNYAET LTVSTDHSTS TTVSFIFTVT
AAPTYTITAN PTSKDFSSQT IGYSAPAAQT IAITNTGNSS VTLTPPTSTN YTIGALSTTT
LAANGTATFT VAPKAGLAVG NYNETLTVST DHSTNATVDL SFTVTAAPTY TITANPTSKN
FGSLAVGYSA PAAQTVTITN TGNTSVTLTQ PTSTNYTIGA LSTTILAVNG TATFTVTPKT
GLAVGNHDET LTVSTDHSTN ATVDLNFTVT AAPTYTITAN PTSKNFGSLV EGYSAPAAQT
VTITNAGNSS VTLTQPTSTN YTIGTLSTTT LAANGTATFT VAPKAGLAVG AHNETLTVST
DHSTNATVEL SFEVTAAPTY TITADPVTKD FGSLTIGYIA PVAQTVTITN TGNSSVTLTQ
PTSTNYTIGT LSTTTLAANG TATFTITPKT GLAVGNYNET LTVSTNHSTN ATVELSFAVT
TAPTYTITAD PVTKDFGSLT IGYSAPTAQT VTITNTGNSS VTLIQPTSTN YTIGTLSTTT
LAANGTATFT VAPKAGLAVG NYNETLTVST NQSTNATVEL SFSVTVVPNY IVTFNPNGGT
VSETSRSVAS GTAVGALPTP TRSGSYSFDG WYTAASGGTQ ISASTTVSAN VIYYAHWTYT
GGGGSGSGGG SSSNDNSSPV IVTPPAPDKP NSPTQGEIKV PGTVDGKGNV TVSLTDKTVT
DAFNKALAEA KKNGTEQNGI TVVLRVDTGN KTGSNVTVNL PKAVQDTIIA KKIVNTIVVV
DNPDIRVGMD LATIQEINKQ AKSDVNITAT RTNSGKLTGE AKKAIGSRPV FDLKVNYGNG
KAVSSFGAGS VSVTIPYTLG ANEKVGNVQA VYVDSKGKVH WLVNSVYDSV EKVLRFSTDH
FSTYGIGYKQ ANTAFTDIAG HWAKEDIEFV ASRGLFSGTS ETKFSPNTAM TRGMFVTALG
RLANADVSGY AKSSFSDVQD DAYYMGYIEW ASKNNIVNGV GNGKFAPDQS ITREQMAVIM
SNYAKTIGYT LPKVHIENIF TDNAKISTYA KEAVKQMQMA GVISGKNGNL YDPQGTATRA
EVSAVLRRFV ELAISSDTAQ GWSMNDSGKW MYFKDGKPLT GKQDIDGATY TFDQYGVTVD
VPKNLRYTTY TVQKGDSFWS ISHKLCCPMS ELERLNNKSR FSIIYPGDVL RVPEK
//