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Database: UniProt
Entry: A0A1M4V0G0_9CLOT
LinkDB: A0A1M4V0G0_9CLOT
Original site: A0A1M4V0G0_9CLOT 
ID   A0A1M4V0G0_9CLOT        Unreviewed;      2327 AA.
AC   A0A1M4V0G0;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Beta-xylosidase, GH43 family {ECO:0000313|EMBL:SHE62435.1};
GN   ORFNames=SAMN02745158_01064 {ECO:0000313|EMBL:SHE62435.1};
OS   Lactonifactor longoviformis DSM 17459.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Lactonifactor.
OX   NCBI_TaxID=1122155 {ECO:0000313|EMBL:SHE62435.1, ECO:0000313|Proteomes:UP000184245};
RN   [1] {ECO:0000313|EMBL:SHE62435.1, ECO:0000313|Proteomes:UP000184245}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17459 {ECO:0000313|EMBL:SHE62435.1,
RC   ECO:0000313|Proteomes:UP000184245};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC       {ECO:0000256|ARBA:ARBA00009865}.
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DR   EMBL; FQVI01000003; SHE62435.1; -; Genomic_DNA.
DR   RefSeq; WP_072849609.1; NZ_FQVI01000003.1.
DR   STRING; 1122155.SAMN02745158_01064; -.
DR   OrthoDB; 273314at2; -.
DR   Proteomes; UP000184245; Unassembled WGS sequence.
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; cd18818; GH43_GbtXyl43B-like; 1.
DR   CDD; cd18819; GH43_LbAraf43-like; 1.
DR   Gene3D; 2.60.120.200; -; 2.
DR   Gene3D; 2.60.40.1080; -; 1.
DR   Gene3D; 2.10.270.10; Cholin Binding; 2.
DR   Gene3D; 2.20.120.10; Multimodular pneumococcal cell wall endolysin, domain 3; 1.
DR   InterPro; IPR046780; aBig_2.
DR   InterPro; IPR003343; Big_2.
DR   InterPro; IPR011081; Big_4.
DR   InterPro; IPR018337; Cell_wall/Cho-bd_repeat.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR006710; Glyco_hydro_43.
DR   InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR   InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR   PANTHER; PTHR43817; GLYCOSYL HYDROLASE; 1.
DR   PANTHER; PTHR43817:SF1; HYDROLASE, FAMILY 43, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G01660)-RELATED; 1.
DR   Pfam; PF20578; aBig_2; 4.
DR   Pfam; PF02368; Big_2; 1.
DR   Pfam; PF07532; Big_4; 2.
DR   Pfam; PF01473; Choline_bind_1; 2.
DR   Pfam; PF19127; Choline_bind_3; 3.
DR   Pfam; PF04616; Glyco_hydro_43; 2.
DR   Pfam; PF13385; Laminin_G_3; 2.
DR   SMART; SM00635; BID_2; 1.
DR   SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 2.
DR   SUPFAM; SSF69360; Cell wall binding repeat; 2.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR   SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 1.
DR   PROSITE; PS51170; CW; 9.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184245};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..2327
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012815776"
FT   DOMAIN          2026..2100
FT                   /note="BIG2"
FT                   /evidence="ECO:0000259|SMART:SM00635"
FT   REPEAT          2127..2146
FT                   /note="Cell wall-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT   REPEAT          2147..2166
FT                   /note="Cell wall-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT   REPEAT          2167..2186
FT                   /note="Cell wall-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT   REPEAT          2187..2206
FT                   /note="Cell wall-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT   REPEAT          2207..2226
FT                   /note="Cell wall-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT   REPEAT          2227..2246
FT                   /note="Cell wall-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT   REPEAT          2247..2266
FT                   /note="Cell wall-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT   REPEAT          2267..2286
FT                   /note="Cell wall-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT   REPEAT          2287..2306
FT                   /note="Cell wall-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
SQ   SEQUENCE   2327 AA;  253166 MW;  4F84AB1908C59F7A CRC64;
     MKKAKRAIAW MLSVIMTVGC CIPAGAAPNE TEGGTNPAPL AWYPLTEDVS DYSGNDFNGE
     LVGGAAVGAD GLYLPGGGKQ RDYVKLPGEI FQGEENLTIS VWLKSNTAKG NYAALFFGTP
     ANASRVPTNY WLFNPTNPNN LFKSVFTDSD NESKPWETEA GVAAHDTSVY QNKWVHYTTV
     LTPDSVEGYV NGRLVGTAEK TKTVAEFGDV LEAYIGRSNY LDDPDYSGTF QDLRVYGEAL
     DAQGVADVYE DTETVTEPII DSLLEDAKSQ LDLGDLSAVT GNLKLPTEGA NGTAVTWETS
     DPTVISTAGE VFLGDEAKDA VLTATLSIGE QSVQREFAVH TLPQSEVSGY VLGKLNLPYT
     ISEHTVLPES IEGRAITWSS DNPAILGDDG VLHGPEAGFE KVTLTAQIDL GADGLQSKQF
     QVQVAESGAS LAAGYTRSTS NKEIGKSMHL ALSADGSAYE ALHNNMGLLF AKTYNVDAEG
     DESKILSEPY IFRMPDGTFG IVAVRAQTSG TDAEDAGKVL FCTSEDLIDY QEIGMIDLKT
     EGIIKAPACE YDGANEQYRI TWKGEDGNTY SNTIADLNSL SCDDTPKEGV AADKASAELG
     IPNAESGNVI PVTKAEAERL QNRLGEIVNT GVSLNQEQVT TSTGEAADLS GIKASLTYSD
     GQTFQRSVDW DTTDVNWKQP GTYTVKGTIR QSDMDFPVIQ NRADPNILYY NGMYYFIATD
     ENGQGKLYIR SGKTVSELKN AQDHLILNKT SSGDMSGSLW APELHVVNGE LYIFFAASTN
     GAWNAVQCRL MKLKTPDADP TNADNWEAPV RVVRKDGSAL YSEGITLDMT YIEENGVSYV
     VWAERRINPT WSSNIMIATI DPEKPYQLTS DPVRLCAPDY GWDRNTTPVD EGPFVIRNKE
     GQLFITFSGA GVNPSYCVGM LTCTNADDML NPDSWQKSNY PILLSESVPG EYGPGHNSYY
     VNEDGNYVNV YHALPQNSGG KRHTGIREVY WSVDGTPILD MTADEAVLPE NKEVSVEVVV
     EGDPIVDEKE LILNYDFSSV EGNIVKDMSG KGNDGEIKGK GASVQNGTLT LPGGAAGSSA
     GYVQLPTGMF DNQDTLTISV WLKNQTGKGN YAAMFFGTTE SLPLQYWLLN PCNPGGRMKS
     VVTNSVNAGQ PYMTEYGFSP TDGKNGVDGP VTDDSWGLYT TVIQPGFITA YFNGEKVGSV
     KTARNVSDFG EDLAAYIGRS SYNDMFYKGQ VRNVKVSADT WTQDDVSKEY GKGLAELDAL
     ALQMDKTTVV DDITLITEGA YGSTIAWASS DENVIAPDGT VTRPAKGKGD AEITLTATVT
     NMEQSVTKEF VITVLENDPS KDLMLKAQEI DLNTYFVTSN LKLPADIDGI SITWSSSSEL
     IKKDGTVTRP EAGKGNQEVT LTATLTQNQA SASRDFKLVV VEKYSSLLTY VTTGNTQRSD
     ALFLAALKDG TYEALNNGKA ILYGNGGTQM GSPSLFRKAD GTYGLIASVN NDSSSVLLYE
     SEDLISFTNE KQAELAPGKK VKNPVCIYDG STETYKIYWD GNDGKSYVTG TKDFTVFGET
     KEAAKPDSLF GITQTLPGNA VKEESNAFEV TKAEYDAVTN KYSRIKNTGI SSVDGVTVEK
     GGEIELPSKV TASYSDGSSK DMAVEWDTDG VNLNIPGTYE VTGEVAQTEY FNPLIEERAD
     PCVTYDEEND CYYFTASYPT RKVNDPEGYD RIVLRTAKTI NGLKDAEEIV IWDEKDHPQG
     RYIWAPEIHK IGDTWCVLFT ASLVENNVWN LKPHIITCEG TAEGGVMNPD NWGEAQRVDL
     VEGDLDYQGL SIDMTYFEAN GQSYYAWSEK PGSANIYIAT VDPSNPSKLT SKKVMLSSPD
     FAWEWNAGQY INEGPAVIQN DGKVYLCFSG ATVDDKYCVG MLSADAGADL LDQESWTKNP
     YPIFTTTDCE VFGNDELGNT QVGPGHNSFT VDQAGNPVIV YHARTKGQKL GPGDGGLDDP
     GRHARAKSVN FAADGTPVLY MTAEEELAPE NRTITTTVTV SGDVEEPVEI KITPAEAVIP
     AESSLPLTAA GSYEGELTWR SSNTRIAVVD QNGVVTGVRV GTATVTAEDS KGNQGTAKIT
     VTKKLQPHWV AENGKWKYSN GDGTYAENCW RQIRGQWYHF NEDGYMQTGW ILDGGQWYYL
     NRDGIMETGW ILDGGQWYYL RDNGVMATGW LSEGKTWYYL KANGAMATGW LLDGKTWYYL
     KASGAMATGW LLDGKTWYYL KSSGAMATGW LLDGKTWYYL KGNGAMATGW LLDGKTWYYL
     KSSGAMATGW IQVSGKWYYL KDNGAMASNT WIGKYYVNGS GVWTKTR
//
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