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Database: UniProt
Entry: S2ZPI7_BIFBR
LinkDB: S2ZPI7_BIFBR
Original site: S2ZPI7_BIFBR 
ID   S2ZPI7_BIFBR            Unreviewed;       967 AA.
AC   S2ZPI7;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Fibronectin type III-like domain-containing protein {ECO:0000259|SMART:SM01217};
GN   ORFNames=HMPREF1482_00054 {ECO:0000313|EMBL:EPD76285.1};
OS   Bifidobacterium breve HPH0326.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=1203540 {ECO:0000313|EMBL:EPD76285.1, ECO:0000313|Proteomes:UP000014395};
RN   [1] {ECO:0000313|EMBL:EPD76285.1, ECO:0000313|Proteomes:UP000014395}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HPH0326 {ECO:0000313|EMBL:EPD76285.1,
RC   ECO:0000313|Proteomes:UP000014395};
RG   The Broad Institute Genomics Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Schmidt T.M., Dover J., Dai D.,
RA   Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Bifidobacterium breve HPH0326.";
RL   Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC       {ECO:0000256|ARBA:ARBA00005336, ECO:0000256|RuleBase:RU361161}.
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:EPD76285.1}.
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DR   EMBL; ATCB01000001; EPD76285.1; -; Genomic_DNA.
DR   RefSeq; WP_016461981.1; NZ_KE150453.1.
DR   AlphaFoldDB; S2ZPI7; -.
DR   PATRIC; fig|1203540.3.peg.53; -.
DR   HOGENOM; CLU_005235_1_1_11; -.
DR   Proteomes; UP000014395; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR   Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR026891; Fn3-like.
DR   InterPro; IPR019800; Glyco_hydro_3_AS.
DR   InterPro; IPR002772; Glyco_hydro_3_C.
DR   InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR   InterPro; IPR001764; Glyco_hydro_3_N.
DR   InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR42715:SF10; BETA-GLUCOSIDASE F-RELATED; 1.
DR   Pfam; PF14310; Fn3-like; 1.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   Pfam; PF01915; Glyco_hydro_3_C; 1.
DR   PRINTS; PR00133; GLHYDRLASE3.
DR   SMART; SM01217; Fn3_like; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR   PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|RuleBase:RU361161};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        16..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        57..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        929..947
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          448..522
FT                   /note="Fibronectin type III-like"
FT                   /evidence="ECO:0000259|SMART:SM01217"
SQ   SEQUENCE   967 AA;  105852 MW;  DA42F535F902496B CRC64;
     MLDINMSDVI AVLKSLTPYL VVLGVVLVAA IIITFAVNKK TVQNISVRKL VHSESWLVVL
     VVVSVSIALM LTGPMATLLG NATAKKYKLS DETIAAANTQ AQDLYSEAVT MLQNNEDNLP
     ISGTKKLNVF GWGSTQPILG GSGSGSMSNE HPMASILSGL KQAGFETNSE LTDLYTAYRT
     DRPVLNMFQQ DWTLPEVPAD QYSDSLISDA KSFSDEAVVV ITRFGGENAD LPRDMKAESV
     IYNNNSKDYE DYQQGESILE LSQTEKNMLD LISKNFEHVT LIYNGSNPLQ FDFLADYPQI
     KSVLWCPPAG QTGFNALGDI LAGKVNPSGK TSDTFLKNVR STPTLNNIGN FPYDNVEDLA
     VKVNFVGSEY TSSPTFVNYV EGIYVGYKFY ETAADEGLIN YDDTVAFPFG YGLSYTDFSQ
     EMGDVSYKNS KVSFDVTVTN TGDKAGKDVV EVYYNPPYTN GGIEKASVNL AAFEKTKELK
     PGESETVKIE FDDDTMASYD ATDAKAYVLE SGDYEVSLQS DSHTVIDSAT VNVPKTITYD
     SDSNTHNGDQ VAATNQFDDA EGDMTYLSRA DHFANYEEAV AAPVSMSMSD EAKKAFSNND
     TYNPAEHDNA DDEMPTTGAK NGVRLADLRG KDYDDPQWDK LLDQLTFDNM DNMIAMAGYG
     TAAIKNIGKV KLTDLDGPAA LINNFTGVSS IAFPSAVGIA NTWNKDLASE FGKTLGKMAR
     EMHVDGWYAP GMNIHRSPFS GRNFEYFSED GLLSGVMAAG EIAGARSQGV YSFMKHFALN
     DQETNRTAML VTWANEQSIR EIYLKPFEMA VKDGGAQAVM TAYNYIGPTY AGANPALLNT
     VLRDEWGFRG FTLTDYFAGF GYQNADQEIR NGGDAMLATM DVTNHVTSKS ATSLKAMRTA
     AHNILYTAVN SWQYENGEPK TELPIWQTGM WIGIAVVSVL FIGLEVVTIR RFMARRKPAV
     EVIASEK
//
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