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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//