GenomeNet

Database: UniProt
Entry: F3BBR4_9FIRM
LinkDB: F3BBR4_9FIRM
Original site: F3BBR4_9FIRM 
ID   F3BBR4_9FIRM            Unreviewed;      1856 AA.
AC   F3BBR4;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=F5/8 type C domain-containing protein {ECO:0000259|PROSITE:PS50022};
GN   ORFNames=HMPREF9477_01384 {ECO:0000313|EMBL:EGG82375.1};
OS   Lachnospiraceae bacterium 2_1_46FAA.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=742723 {ECO:0000313|EMBL:EGG82375.1, ECO:0000313|Proteomes:UP000018451};
RN   [1] {ECO:0000313|EMBL:EGG82375.1, ECO:0000313|Proteomes:UP000018451}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2_1_46FAA {ECO:0000313|EMBL:EGG82375.1,
RC   ECO:0000313|Proteomes:UP000018451};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J.,
RA   Ambrose C., Allen-Vercoe E., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA   Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A., Gujja S.,
RA   Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C., Murphy C.,
RA   Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Lachnospiraceae bacterium 2_1_46FAA.";
RL   Submitted (DEC-2012) 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:EGG82375.1}.
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DR   EMBL; ADLB02000009; EGG82375.1; -; Genomic_DNA.
DR   STRING; 742723.HMPREF9477_01384; -.
DR   eggNOG; COG3250; Bacteria.
DR   HOGENOM; CLU_001607_1_0_9; -.
DR   OrthoDB; 9762066at2; -.
DR   Proteomes; UP000018451; 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; 2.60.40.3630; -; 1.
DR   Gene3D; 1.20.1270.90; AF1782-like; 1.
DR   Gene3D; 1.20.1270.70; Designed single chain three-helix bundle; 1.
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; IPR000421; FA58C.
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   PANTHER; PTHR42732; BETA-GALACTOSIDASE; 1.
DR   PANTHER; PTHR42732:SF1; BETA-MANNOSIDASE; 1.
DR   Pfam; PF07532; Big_4; 2.
DR   Pfam; PF16355; DUF4982; 1.
DR   Pfam; PF00754; F5_F8_type_C; 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; 2.
DR   PROSITE; PS50022; FA58C_3; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018451};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           32..1856
FT                   /note="F5/8 type C domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5039710932"
FT   TRANSMEM        1831..1851
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1310..1471
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|PROSITE:PS50022"
FT   REGION          1091..1113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1716..1739
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1805..1826
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1680..1707
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1098..1113
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1856 AA;  204648 MW;  38082AC16BF48C47 CRC64;
     MNKFTKGTAR FGATLLTAVL TMSCFSPLAT ANASIDVRTQ SQTQMSSDKE VVYVNTVNNA
     TERTQNFDAN WKFYLGDAGN AQTSNFDDSK WRNISLPHDY SIEQEYSKQM EAESGYLPGG
     TGWYRKHFTV GNELKGKEIR LDFDGVYMNS TVYINGEELG THPYGYTPFS FDLTDHIKFG
     EENVIAVKVD HKTPSSRWYS GSGIYRSVNL TVTDAVNVAL NGTKVETPEL ATNQTTVKTT
     VKTTVENDGK EAKDVVLTHK VFEKGNSKNV IGETTTQKTT IQPNGKADIN AEFTVSNPKL
     WDIESPNLYT VRTEVKVGDK VVDTYDTEYG FRYTKFDKDT GFYLNGKPVK LKGVCMHHDQ
     GALGAVANRR AIERQVEILQ EMGCNSIRVT HNPAAQHLID ICNEKGILVV EEIFDGWHHA
     KNGNTEDFAK YFEKQVGENN KLIGATPTMT WAEFSLKATL KRDCNAPSVI MWSLGNEIQE
     GNYKSGFLER TPNMIKWAQA VDKTRELTIG SNAVKNEGVN GEHSKIADKI TEAGGVSGTN
     YSDGNSYDRL RNLHPNWKIY GSETASSVNS RGVYHTKDRD NNTQELSSYD TSKVNWGAFA
     SDAWYDVITR DFVAGTYVWT GFDYIGEPTH WNGTNPGVVG KWPSPKNSFF GIVDTAGMPK
     DSYYLYQSQW NDDVNTLHVL PTWNRDEIIL DNQNKAEVVV YSDAPKVELW LTPAGSKEAK
     KVGEAQELET RTTEKAKHSY QVVKGSNKLY RTWKVPYEAG TLEARAFDAN GKPITDTKGR
     SSVTTAEKEA KLQVKADRNE IKANGTDLSY LQIDVVDAKG NIVPNADDKV KVEVTGNGTL
     VGLDNGWQTD HDSYKGKERR VYNGSGIAIV QSTKNAGEIK VKVSAEGLGE KTVTLNTTAD
     TTGGEQQVVV DSFFMEKNYY VKVGNKPSLP KTIEVRYSNG TKEQKPVKWN TISDEQTNKA
     GAFTVKGTVE NAGEVSVRVN MIDEVGGLLN YSTAVPVGTT PTLPESRTAY LSNGEVLDVS
     FPVKWEEKDA SAYNKVGTVI VNGTANVLGK EVTVTATVRV AKEDVALGDS ISGAAVVLEQ
     DIPENMQSDH LPAIKDGNTG KNANNEGGTN KSVWTNYKNS NEGNDNKAEI IMGYDTQVVL
     GEIVIHFFED SYSARFPDAN KTKIYVAETK NGPWTQVQAK EQIGTAKDGI KPYTYKLDAP
     VSATFIKFEL TNKDEQLDGR KPCTGITEIE LKKATTSFKT NTTAELGKLT VNGVELTKQQ
     LASGKYTTSA LVADVTPEAK DNAAVTVLPK NENNQIKIII ESEDHKTTNT FTIFLNDKDP
     DVYYPNKDIT PSAPFSLPSP DAHEGDVRYV LDGDVNTHWH TNWRNGATAS DIAKREITLT
     LKEAATIDAM NYHPRVYGGG NGRVTKYKVL YSVDGTTFNE SDVCAEGTIS QDKADWTLIE
     FTKPVKAKAF KLIGVHTYTD QGADKHMAVA ELRLRMNRET TDISDEANKV TIDPIAKQKV
     DVVDEKHPVE PQVTVKQNGK ALTYGIDYKV SYADNTKEGT AKAIVTGIGK YSGTLETTFA
     IEKNPVVLTS IAVKTSPKTD YHVGDTFNPE GLVLSVFYSD NTSSEVAYTA EIKDKFTFAP
     SLETALKETD EVVTVTYEGK TTEVKVNVTE KQESTVRKAL EERVKFAQTI TSNGYTADSY
     SAFKAALKAA EETLANENAT DAQLQSALDN LNTGINGLKE ESVTPNPNPN PNPDENGDRD
     ELRAKLQKFY DECLAYYKEG NYSKDNWKVY EDAMAQAKAV LDNENATEKE LKDALSDLIN
     ATKRLNDEGK AEEQNPPTPP TSIETGDQAP ITMIVVLMVV AVVAIVGIVV YKRKKR
//
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