ID A0A1C0BV16_9FIRM Unreviewed; 1798 AA.
AC A0A1C0BV16;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OCN04827.1};
GN ORFNames=A4S06_10340 {ECO:0000313|EMBL:OCN04827.1};
OS Erysipelotrichaceae bacterium MTC7.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae.
OX NCBI_TaxID=1768196 {ECO:0000313|EMBL:OCN04827.1, ECO:0000313|Proteomes:UP000093409};
RN [1] {ECO:0000313|EMBL:OCN04827.1, ECO:0000313|Proteomes:UP000093409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MTC7 {ECO:0000313|EMBL:OCN04827.1,
RC ECO:0000313|Proteomes:UP000093409};
RA Whitehead T.R., Haley B.J.;
RT "Genome Sequence of MTC7.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401}.
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:OCN04827.1}.
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DR EMBL; LVZN01000017; OCN04827.1; -; Genomic_DNA.
DR STRING; 1768196.A4S06_10340; -.
DR OrthoDB; 9762066at2; -.
DR Proteomes; UP000093409; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 1.20.1270.90; AF1782-like; 2.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR011081; Big_4.
DR InterPro; IPR032311; DUF4982.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR040605; Glyco_hydro2_dom5.
DR InterPro; IPR006101; Glyco_hydro_2.
DR InterPro; IPR006103; Glyco_hydro_2_cat.
DR InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR InterPro; IPR006104; Glyco_hydro_2_N.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR PANTHER; PTHR42732; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR42732:SF1; BETA-MANNOSIDASE; 1.
DR Pfam; PF07532; Big_4; 1.
DR Pfam; PF16355; DUF4982; 1.
DR Pfam; PF07554; FIVAR; 2.
DR Pfam; PF18565; Glyco_hydro2_C5; 1.
DR Pfam; PF00703; Glyco_hydro_2; 1.
DR Pfam; PF02836; Glyco_hydro_2_C; 1.
DR Pfam; PF02837; Glyco_hydro_2_N; 1.
DR PRINTS; PR00132; GLHYDRLASE2.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000093409};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1798
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038794782"
FT TRANSMEM 1770..1788
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 55..201
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 218..322
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 331..571
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT DOMAIN 685..755
FT /note="DUF4982"
FT /evidence="ECO:0000259|Pfam:PF16355"
FT DOMAIN 773..875
FT /note="Glycoside hydrolase family 2"
FT /evidence="ECO:0000259|Pfam:PF18565"
FT DOMAIN 898..950
FT /note="Bacterial Ig-like"
FT /evidence="ECO:0000259|Pfam:PF07532"
FT REGION 1656..1751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1656..1678
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1690..1704
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1723..1741
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1798 AA; 197439 MW; 4E36DD1D23746EA2 CRC64;
MNIKKLGIVA LVSLLSFTSL PMNTNVMKKN NEQVSFTKPE DIYVDIIGES ERTTNFNENW
KFYRGNKQDA EKQGIDTQEW ESITLPHDYS IDTEFTVAGE AESGFLLGGV GWYRKEFIVP
EKYADKQLTI EFDGAYMNSE IYVNGKKIGT HPYGYTAFAY NLKDHLVIDG KTENVIAVKT
DNKLPSSRWY SGSGIYRDVK LTVADEVHVA NTGVVVTADA ENIIVNGNGE LNVVTTVDND
SEDRQTVDVK TSLVDAKGKI VSTSGKQNKS IEVNGTTEFN TTMDVENVTT WSIENPYLYT
VRVEVSKADK TIDTYDTVYG FRHYNFDANT GFSLNGEKMK LKGVSMHHDQ GSLGAVANRD
AIARQVKILK EMGANAIRVT HNPAATALLE ICDEEGMLVI NEAFDGWTEY KNGNTNDYTK
YFNTLIEEDN EILHGSTGMK WGEFDAKAMV RSGINNPSII MWSIGNEIDE GVSGNTSHYV
ELSRDIIRWI QETDATRPVT IGDNRRGDGN VGKIDQIIHE AGGVVGFNYA TATAFKNKHS
QNPEWKLYGA ETTSAIHSRG IYSTYGTDGT NLQLSEYDND QAKVGWGHSA SNAWSYVIEN
DFNAGQFVWT GFDYLGEPTP WNGVGQGSVS GQGPTPNSSY FGIVDTAGFP KDTYYLYKSL
WDEKNDTLHI MSNWNNDEIV KNGNGKVQVD VYSNAHTVEL YLNDEKVGTQ TATEYTTTTG
YKYQKFGNKF YPSFEVTWAA GALRAVALDK EGNVIEETVG NQSATTTVST AKLVANADKS
EIIANGSSLA YITVDVQDAD GNFVAGANNK IDFSIEGNGK IVGVDNGNAA SIESYKGSSR
KAFSGKALVI VQSTKEEGSF TLKATSDGLE STSVTVQTGK DTSSDDAYLS YYTMSKDVYV
AQGTIPALPS SVTGTNSDGS KVDLSITWNA VSEEDVSEIQ VFDVEGTIDG KSIPVTMKIH
VIGDIVAFEN YATMTTAEVM PKLPQTLRGF YADGTFSEYF PVSWELSSDD YATKGMKNIV
GSLSVLNEVY TANLSLRVLD KLADAKNIAS KNFVGAPVFK NGTLRNGVVS DPSTTAINDS
LLELNDGVKT ESVRESARWT NWGLRNENPT VDTYVQLDWS EPHKMQNVKL WHFTDNAFSV
VPGDDNVRFE YLDTKDNTWK EIESSHITQV SYLAGDTPYG FIHAIETQSL RVWLKSPTVG
KCIGLTEIEV YESVNVPEAN GSINIEEVTL NGTPIESFNG FESYDEQTKT YVVRLEDSNY
PELDITSNNA ATTILPIYEH VQRAYLVAED RSADTMITVV YDVAEPAVDM SELNTLIETV
ETLDEEAYTP ESWTALQEAL ETAKAVVSGD APTQEAIDQA YASLDEAYKG LEQVVPESME
KQILKIFIDL AQVEVDNGNV DKLIDGAKAE YYAALEEAID LYEDANATSE AMSLSIIRLT
EALELLDYIK ADTTKLQALY DECLAVNLDD YMNNEAKENF MAALENAKAV LSIEGGALTY
EVEEAYEQLE STLVQLVLKP SKDALAYMIS LAEAKDANAD RYTKESYGAL LEALAEAKEV
YEDEDATAEQ ISTQVNKLAK AIAQLRLKVD RSYLSAKVEG IKATNFGAYT EASVARLMSV
VSDAEAFLAT PEQSADVEAA QLQALSEKLD EALATLEIKD EKPTEPETPE KPEVKPEPSE
PTIPEQPGKS NETKVEKEED KQGSQVLPSI DIDDDDTNGK DISMVTEGKN ESQTDSQSAS
AGKDKGKVKG SNTGQKAAFG AIMQNGQLSG VIYFMFGLLG SGFIIILIKR RKDEKDKA
//
