ID B1C5E0_9FIRM Unreviewed; 2169 AA.
AC B1C5E0;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 28-JAN-2026, entry version 82.
DE SubName: Full=LPXTG-motif cell wall anchor domain protein {ECO:0000313|EMBL:EDS73884.1};
GN ORFNames=CLOSPI_02309 {ECO:0000313|EMBL:EDS73884.1};
OS Thomasclavelia spiroformis DSM 1552.
OC Bacteria; Bacillati; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Coprobacillaceae; Thomasclavelia.
OX NCBI_TaxID=428126 {ECO:0000313|EMBL:EDS73884.1, ECO:0000313|Proteomes:UP000004910};
RN [1] {ECO:0000313|EMBL:EDS73884.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1552 {ECO:0000313|EMBL:EDS73884.1};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDS73884.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 1552 {ECO:0000313|EMBL:EDS73884.1};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Clostridium spiroforme (DSM 1552).";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family.
CC {ECO:0000256|ARBA:ARBA00007806}.
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:EDS73884.1}.
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DR EMBL; ABIK02000015; EDS73884.1; -; Genomic_DNA.
DR STRING; 428126.CLOSPI_02309; -.
DR CAZy; GH31; Glycoside Hydrolase Family 31.
DR eggNOG; COG1196; Bacteria.
DR eggNOG; COG1501; Bacteria.
DR eggNOG; COG3250; Bacteria.
DR HOGENOM; CLU_001337_1_1_9; -.
DR OrthoDB; 176168at2; -.
DR Proteomes; UP000004910; Unassembled WGS sequence.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:InterPro.
DR CDD; cd00063; FN3; 1.
DR CDD; cd06596; GH31_CPE1046; 1.
DR CDD; cd14752; GH31_N; 1.
DR CDD; cd08759; Type_III_cohesin_like; 1.
DR Gene3D; 2.60.40.1080; -; 1.
DR Gene3D; 2.60.40.680; -; 1.
DR Gene3D; 1.20.1270.90; AF1782-like; 3.
DR Gene3D; 1.20.1270.70; Designed single chain three-helix bundle; 2.
DR Gene3D; 1.10.1330.10; Dockerin domain; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 3.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1760; glycosyl hydrolase (family 31); 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR003343; Big_2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR036439; Dockerin_dom_sf.
DR InterPro; IPR033403; DUF5110.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR017853; GH.
DR InterPro; IPR048395; Glyco_hydro_31_C.
DR InterPro; IPR025887; Glyco_hydro_31_N_dom.
DR InterPro; IPR000322; Glyco_hydro_31_TIM.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR013783; Ig-like_fold.
DR NCBIfam; TIGR01167; LPXTG_anchor; 1.
DR PANTHER; PTHR22762; ALPHA-GLUCOSIDASE; 1.
DR PANTHER; PTHR22762:SF166; ALPHA-GLUCOSIDASE; 1.
DR Pfam; PF17137; DUF5110; 1.
DR Pfam; PF00754; F5_F8_type_C; 2.
DR Pfam; PF07554; FIVAR; 4.
DR Pfam; PF13802; Gal_mutarotas_2; 1.
DR Pfam; PF01055; Glyco_hydro_31_2nd; 1.
DR Pfam; PF21365; Glyco_hydro_31_3rd; 1.
DR SMART; SM00635; BID_2; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR SUPFAM; SSF63446; Type I dockerin domain; 1.
DR PROSITE; PS50022; FA58C_3; 2.
DR PROSITE; PS50853; FN3; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000004910};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 899..981
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 971..1128
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 1677..1836
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
SQ SEQUENCE 2169 AA; 238398 MW; F45DB1B091F93B26 CRC64;
MGFRERGYKM NKKTFHKISV WSLAAMMSLS TISTTTIGLS AKNALNDQIS TLEVDEAGYN
VLGAVTSAVV DGNKVDLTIR TGEKIRFTFL EQNVFRMYMA PEGEEFQEYP TPNGSDHTAT
ITNKTDDQYK AEYDVVPELT DDGDKYTIST DKIKLEIVKE TSLMKLMKAD GTVVWEEAAP
LKYKSGSTVQ TLKTNEKEYF FGGGTQNGYF SHKGKSIKIV ATNTWVDGSV ASPNPFYWST
DGYGVVRNTW KPGQYDFDSK GDGTVTTTHN EKRFDAYYFV DDSAEDILGD YYELTGTPAE
LPEYASYLGH LNCYNRDYWL EVPEGTSGAV KLGDKWYKES QSDNGGVKET LLGGNTTAQQ
VIEDHKANDM PLGWFAPNDG YGCGYGQADT QAGDIDNLKN FADFAKANGV ETGLWTQSNL
WPADPSNPQK GERDIYKEVE AGVHATKTDV AWVGPAYSFA LNGVSVAYDA IASRSGLKPA
IVTLDGWAGT QRYGGIWTGD QSGGNWEYIR FHIPTYIGTA LSGQPNVGSD MDGIFGGSNK
IINTRDFQWK AFSTYMLDMD GWGSNQKTPW ALGEDVTSIN RTYLKLKAQL MPYINTISHE
ATAEGGLPMI RAMFLEEENA YTLGTATQYQ YMWGDNFLVA PIYQNTAADA EGNDVRNDIY
LPGTSDVWID YFTGKQYRGG QVLNNFDAPI WKLPLFVKNG SIIPMYAENN NPEAVSETNT
DGLDRSQRIV EFYPYGSTQF EAYEDDGKTL GGASSKTLLT SDVKDGIATL KAEKSVGSYS
GMVKERSTEF VVNASKAPTK VTGNVAGKDV VFTAVSTQEE YDAAKGNVYF YNENPSVIVK
DYATEGTKYA NIEETTTPKL YVKSAEKVDI TEYDFTVNVE GFENTQDLGE DIEDSSVAVP
TNFVEQSKTD SEIILDWDDM EDAVSYDIEV DGTVYRNILD STYTHSGLKY LTDHTYRVRA
VRADGHYSAW SQPLNIQTDD NPYRNVPNFT ADWSYGDSWG DLEDAFDHNT NTMFHSTKAV
TPDQMMTLDL GAAYQLDKLT YQPRMDNKGN GTVTRMDVYA SLDGINYTKV WDGKENAAWT
YSSSMEDPDI KEVTLNGVKA RYLKLSVLES KGGFFSASEI TPYKLDGTNA WVVGDVNNSG
KVDNNDLTFY ENYVGLKPVD NDWEYSTLGN IDNNQIIDAY DISFVSRMLG DEPVNPSQAA
KGVEGKIEIV PSKTDIKAGD EVTLDFYGIG LKNVNAFSVE MPVDTDLFEV TNFGSASLST
VFMRNFSKTR FHNDGSVDNY VCFANEGTQE LINGTGSLAK VTIRATQDFN WDTKATQAIV
VGQDLSKADA LIDITQEPTA PETKDVLGLN DIKAITFDND KKQGMDGSEL WQQSNWKELL
FDGDKSGTLA EFKWYLNTYP EAGDIAEEVK LPTDMNFTFN EAEPLKTIKV YNRVGGNGSV
TSIKATAYAG DTEYDLGTIN ENREVFEFTV PKEATNIDRV VITPLTSTGT ATGTTTGSET
NRMLSLREIE FETDSAVKAT GIEFTKDSAD SVYTGAIAEV SAVVTPDNAS NPFYEITSSD
ETIAKVIKIP MEDKYIYAVQ GIKEGTVTLT ATSEDGQFTA TKEFKVVEGV DTSVLQGQID
KFEDLYENLY TVESYAKVKG LVTSAKELIS SKDVTQAAVD KITIDIVNAM KELEFKGSNT
DQPSSQNLIP QNTLKRYDES SMSAAEKEDA SYTIDGKTDT IWHSNYNSSY KLPQYVTIDL
GAVYDLEQVN MLPRQNSRNG HITHYRIEVS TDGTAFTPVV EGYLENDGNS LTDPGKEKEI
KFDTTKAQYV RFIAIESLGD RNNAYASIAE LNFYGTTESG EVETVNKAAL EAAVTTANAL
KEQGALNNVI PAVVAEFNAA LAEAEGILAD SNADQVTVDA SFFRLATAIQ MVDFVKGDKT
ELIKLVEEYS KLEENNYTTA SWEVFKGALD AAIAVRDDEN ALEYEVKEAL NNLKDGYAQL
VVVADKTALQ AMVDKVNGLD EKLYTEASWA KLADPMAKAN EVLANKDATQ DEVNAAYEAL
VRAYLELRLI PNKDLLEDLI NKAQSFEAAN YTADSYANLR SALLVAQSTL ANESADEAAV
KAAVEGLQAS IDALVPVSAD NNVASGDKVN AGDKTAIATG DSTSMLSSIA GLALASIAMF
GAKRRKKSK
//
