ID   ARAFA_BIFL2             Reviewed;        1065 AA.
AC   A0A3R0A696;
DT   25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT   10-APR-2019, sequence version 1.
DT   03-AUG-2022, entry version 10.
DE   RecName: Full=Alpha-L-arabinofuranosidase {ECO:0000303|PubMed:30564851};
DE            EC=3.2.1.55 {ECO:0000269|PubMed:30564851};
DE   AltName: Full=Non-reducing end alpha-L-arabinofuranosidase {ECO:0000305};
DE   Flags: Precursor;
GN   Name=blArafA {ECO:0000303|PubMed:30564851};
GN   OrderedLocusNames=BLLJ_1854 {ECO:0000312|EMBL:BAJ67518.1};
OS   Bifidobacterium longum subsp. longum (strain ATCC 15707 / DSM 20219 / JCM
OS   1217 / NCTC 11818 / E194b).
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=565042;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b;
RX   PubMed=30564851; DOI=10.1007/s00253-018-9566-4;
RA   Fujita K., Sakamoto A., Kaneko S., Kotake T., Tsumuraya Y., Kitahara K.;
RT   "Degradative enzymes for type II arabinogalactan side chains in
RT   Bifidobacterium longum subsp. longum.";
RL   Appl. Microbiol. Biotechnol. 103:1299-1310(2019).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b;
RX   PubMed=21270894; DOI=10.1038/nature09646;
RA   Fukuda S., Toh H., Hase K., Oshima K., Nakanishi Y., Yoshimura K., Tobe T.,
RA   Clarke J.M., Topping D.L., Suzuki T., Taylor T.D., Itoh K., Kikuchi J.,
RA   Morita H., Hattori M., Ohno H.;
RT   "Bifidobacteria can protect from enteropathogenic infection through
RT   production of acetate.";
RL   Nature 469:543-547(2011).
CC   -!- FUNCTION: Involved in the type II arabinogalactan (AG) side chains
CC       degradation (PubMed:30564851). Releases arabinofuranose (Araf) from
CC       alpha-1,3-Araf-substituted beta-1,6-galactooligosaccharides
CC       (PubMed:30564851). Can use radish root AGP, larch AG and arabinan.
CC       Shows weaker activity with gum arabic and arabinoxylan
CC       (PubMed:30564851). {ECO:0000269|PubMed:30564851}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside
CC         residues in alpha-L-arabinosides.; EC=3.2.1.55;
CC         Evidence={ECO:0000269|PubMed:30564851};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=7.86 mg/ml for larch arabinogalactan
CC         {ECO:0000269|PubMed:30564851};
CC         Note=kcat is 220 sec(-1) with larch arabinogalactan as substrate.
CC         {ECO:0000269|PubMed:30564851};
CC       pH dependence:
CC         Optimum pH is 5.5 with larch arabinogalactan as substrate.
CC         {ECO:0000269|PubMed:30564851};
CC       Temperature dependence:
CC         Optimum temperature is 50 degrees Celsius with larch arabinogalactan
CC         as substrate. {ECO:0000269|PubMed:30564851};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family. {ECO:0000305}.
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DR   EMBL; BR001495; FAA01257.1; -; Genomic_DNA.
DR   EMBL; AP010888; BAJ67518.1; -; Genomic_DNA.
DR   RefSeq; WP_013583011.1; NZ_SHRD01000030.1.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.115.10.20; -; 1.
DR   InterPro; IPR003343; Big_2.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR   InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR   Pfam; PF02368; Big_2; 1.
DR   SMART; SM00635; BID_2; 1.
DR   SUPFAM; SSF49373; SSF49373; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   SUPFAM; SSF75005; SSF75005; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cell membrane; Glycosidase; Hydrolase; Membrane;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..1065
FT                   /note="Alpha-L-arabinofuranosidase"
FT                   /id="PRO_5018696848"
FT   TRANSMEM        1040..1060
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          277..346
FT                   /note="BIG2"
FT                   /evidence="ECO:0000255"
FT   REGION          997..1031
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1013..1031
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1065 AA;  113682 MW;  A7901D3673DDD74F CRC64;
     MKHWKKMAAS LIAISTMVAV VPTTYAMESE DSQPQTTDTA TVQTTKAAEP TLLASWDFTG
     KNGTTNSAIA DSTGKYNLTL KDGAKIEQYG DRSNNEALSL RGDGQYAQID DQLFKDAGDS
     FTLEFASKTR HDDSGKFFSF IVGKDGSNDA NTTDQANANK YLMFYNSKTA IKGVISNNNW
     GNEQGSKVTV SGNDNSWADY KIVVDGTNLA VFRNNALIIF KANTGIKMSD LGATTAYIGK
     SFYSVDEYWN GAMDDIKVYR GADLTMPTAV AISGTGVVNN KLTLIEKDST KLTATVTPDD
     AVSKNVTWSS SDESVAKVAA DGTVTGVKAG TATITATTEL GGVKAELPVT VEPMNAQNAA
     AADLDAAIAA LKVPAAENLP LVAKGTKNGS AITWKSSDEK LITSTNEKYE NRTTGADDPY
     RGAGIINRPA YGDGDSKPVT LTATASYNGG EKVTKTIEVT VKEKTRIAPD TGYAAVTFES
     DSNGGEKAWV ASTEKNDFFT FKTRNNGQAV LTNDADTGGL RDMFVLRSHE GDKYYLIATD
     LKVSSMGWSQ NQVNGSRKVE VYESTDMMNW TRTNGDGNGG ITINTPNAGM TWAPEAYWDD
     DLNAYVVFFS SRMFTDDTRT TPVKNDKTGN SSYAQVRYAI TRDFVNFTEP QMWQDTGYSR
     IDSTVRKIGG YYYRFTKNEQ GGAAGDYITT GKSIFLERSK VLTAPTTEAS PGQDPNTGWQ
     LLEQALLPFE GPETIKLNKD DELNTKDDDG YILLSDNFAY RAFMTTGAEL SKTTWDNPMT
     KRYPDFNNEK KPVKAEPGAQ GYITQGANGG LPDKVRHGAF VNVPESVLKV TKSWTAANPT
     HIEAVDSTTK AVYNAGTREL TATVTSADKG TLAGSVKFSA GDWSKTVKLD AEGKATVTLP
     ASVSGTVAVA YDGYTDGLVN PSDTTVDGIE QGKVDLAELN KQIAAAEALK ESDYTADSWA
     KLAAALKTAK AALAAENQGE VDTAAADLKT AIEALQKAPT NPGEGDGDKG DGNKPTTPTT
     GDKTNVNKPG SALSNTGTAV LGLGGAVVAL AIAGISLTLW RKRRA