ID A0A1Q9PGE0_9BACI Unreviewed; 1979 AA.
AC A0A1Q9PGE0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=BIG2 domain-containing protein {ECO:0000259|SMART:SM00635};
GN ORFNames=BTR25_26055 {ECO:0000313|EMBL:OLS33402.1};
OS Bacillus sp. MRMR6.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1928617 {ECO:0000313|EMBL:OLS33402.1, ECO:0000313|Proteomes:UP000185615};
RN [1] {ECO:0000313|EMBL:OLS33402.1, ECO:0000313|Proteomes:UP000185615}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRMR6 {ECO:0000313|EMBL:OLS33402.1,
RC ECO:0000313|Proteomes:UP000185615};
RA Thomas J.M., Ghebrendrias N., Rawat M.;
RT "Mendota Genome Annoucement.";
RL Submitted (DEC-2016) 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:OLS33402.1}.
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DR EMBL; MSLS01000058; OLS33402.1; -; Genomic_DNA.
DR RefSeq; WP_075690870.1; NZ_MSLS01000058.1.
DR STRING; 1928617.BTR25_26055; -.
DR Proteomes; UP000185615; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR CDD; cd08983; GH43_Bt3655-like; 2.
DR Gene3D; 2.60.120.200; -; 3.
DR Gene3D; 2.60.40.1080; -; 1.
DR InterPro; IPR046780; aBig_2.
DR InterPro; IPR003343; Big_2.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR InterPro; IPR019931; LPXTG_anchor.
DR NCBIfam; TIGR01167; LPXTG_anchor; 1.
DR PANTHER; PTHR43301; ARABINAN ENDO-1,5-ALPHA-L-ARABINOSIDASE; 1.
DR PANTHER; PTHR43301:SF3; ARABINOSIDASE-RELATED; 1.
DR Pfam; PF20578; aBig_2; 4.
DR Pfam; PF02368; Big_2; 1.
DR Pfam; PF00746; Gram_pos_anchor; 1.
DR Pfam; PF13385; Laminin_G_3; 3.
DR SMART; SM00635; BID_2; 2.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 2.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 3.
DR SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 1.
PE 4: Predicted;
KW Cell wall {ECO:0000256|ARBA:ARBA00022512};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Peptidoglycan-anchor {ECO:0000256|ARBA:ARBA00023088};
KW Reference proteome {ECO:0000313|Proteomes:UP000185615};
KW Secreted {ECO:0000256|ARBA:ARBA00022512};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1951..1972
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1378..1457
FT /note="BIG2"
FT /evidence="ECO:0000259|SMART:SM00635"
FT DOMAIN 1793..1870
FT /note="BIG2"
FT /evidence="ECO:0000259|SMART:SM00635"
FT REGION 1876..1946
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1884..1932
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1979 AA; 217635 MW; 387CED28284BBAF6 CRC64;
MKLRKRFSIF LITLMIFNTL SGIFPQSFLA EEPATPELIL HYDMKSNVKN GNQTIIKDVS
GSDKAFDGEF KNPDNGQLMH NNEVGYVSFN GGSSTSNSGY IEIPKAEDGT DLLNGLQDVT
VSALVNWNND GVNRWIFGLG TVTNDAEYGN KYFFVTPRHG ARNVAATGIS SAGWRNESLI
SGTATMKADS WEVATVVFSG TNNTITLYVN GNQAATGSAG GKKLSEIIDP AAGFSGLIGK
SIFKNDDSFK GMVGDFRVYN GAMSNAQVTA LYTETSNKIE NINQLVINDA QESLDVSHYL
NSEDKSTEEV TKDIALPTTG KHGAAITWTS SNTNVITNDG KVTRTDLTEE NVEVELTANL
SYGGSTAQKI FTVTVLKEFT DEDKVAQDAA NLILENTDNV KGNISLPVTG KNGSTITWES
SNPEIIKGSA QAAQDPKKLG WITRPEADTN VTLTATIANG NAETTKEFNL TVKKDPGELE
YDAYFFSYFT GEYEGGEEIS FATAEDPLKW RALNNGKSII QSNMGEKGLR DPFIIRSPEG
DKFYMLATDL KMGESTNFDQ VQITGSHYMM IWESDDLVNW SEQRMVEVAP KTGGNTWAPE
AIYNEKTGEY VVFWASSMKD SETYGSFPNG RPAGQYNVMY YATTRDFITF SEPKVFIDEG
FPTIDTSFVE DNGTFYRFTK SEVNYRVYYE KTTDIFYDKD GIAENGFQYD VIPRTKSGNS
GLIGHLGNNE GQTIFKDIHE DKWYMFLDSW PYHVRWSTNL EDGTQFVNNL LPTNEYALPP
GPRHGTVIPI TRAEYNALQE KYGIVAPEPS EAPVVHYTFD DNDMDGTTVK DVSNNGFDAK
LVGGSTINTE DTIANSTGSV ELDGSTGYVE LPENLIKDLN LESMTMSTWV NVGQNQANQR
IFDFASDTGR IVNRNTMYLS TQGDSGNLEF AIVTPFTEKF GNQTTPLGSG YKYAVRAPRL
STSSWQHVAV TIEGYDAVVY VNGEEVARSS TYNVEPRMLL ETTMNYLGKS INSSHSLFKG
KFDDFRIYNR ALNADEVSAL ADEETTVPPV EEPEGTNLIL DYDMNKIDGT KVVDNTGNFE
GKLVNPENAV LIMGEEAGVI NFKGGSTSSY IEMPQGVLND LESVTVSSLV NWNGTNEAEW
IYALGQDSNK YLFTTPKRNS GDRSARVGLG ITSWSNEASA NATTGSLKAN EWKLVTTVMS
GEDQTLKLYI DGVEVASGST KGYTLAEINN VNGRSGFIGR SFYSGDPYFG GMIADFEIYD
GALSAEEVSE LKEKADEKIA GMEDLLLQDA SKQLNYDAFI KNNVNKDEIT SDLSFPEVGP
NGTSITWESQ NQDIITNEGK VSRPSFEDGD KTVTITATIT DGTNSVTKEF IVTVLKKPHD
SVSVKLDAAE LKVHNIRDVR GNLTLPVTGE NGSTITWKSS DPAMITPTGE VTRPAQGEGD
KTVRLTATIT LNDATVTKAF LAHVKEMPKE EEYEGYVFSY FTGEGTANGE QIYFSLSEGN
DPLNWQELNN GQPAITSELG EKGLRDPFII RSPEGDKFYL IATDLKINGN WNWDRAQRQG
SRSIMVWESN DLVNWSEQRM AEVAPPEAGN TWAPEIFYDD TTGEYIVFWA SKLYDNEEHT
GGTYNKMMYS KTRDFYTFTE PEVYIDLGYS VIDTTMIQHD GKVYRLSKDE RNNTTSSPNG
KFIFQEVGDS VLDPNFELIK EGIGKGSIGA GEGPTIFKSN TEEKWYMFID EFGGRGYVPF
ETTDLDSGEW TMVTEYDLPA HPRHGTILPV TQSEYEALFA NVPAVKEPAA EQKATNVTLN
QETLELEVGK EGQLAATVTP DDAVNKEVVW SSSNEEIATV DETGKVTALK EGNATISVST
VTGGYMAFAE VVVTKATDNE TPGEDNETPG EDNETPGEDN ETPGEDNETP GEDNETPGED
NETPGEDNET PGEDNETSGK GKELPNTATN LYNYLMIGMI LLAVGGVSLL VAKRRKMNL
//
