ID V4PUI6_9CAUL Unreviewed; 560 AA.
AC V4PUI6;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Beta-xylosidase C-terminal Concanavalin A-like domain-containing protein {ECO:0000259|Pfam:PF17851};
GN ORFNames=ABAC460_03735 {ECO:0000313|EMBL:ESQ92021.1};
OS Asticcacaulis sp. AC460.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Asticcacaulis.
OX NCBI_TaxID=1282360 {ECO:0000313|EMBL:ESQ92021.1, ECO:0000313|Proteomes:UP000017839};
RN [1] {ECO:0000313|EMBL:ESQ92021.1, ECO:0000313|Proteomes:UP000017839}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AC460 {ECO:0000313|EMBL:ESQ92021.1,
RC ECO:0000313|Proteomes:UP000017839};
RX PubMed=24463524; DOI=10.1038/nature12900;
RA Jiang C., Brown P.J., Ducret A., Brun Y.V.;
RT "Sequential evolution of bacterial morphology by co-option of a
RT developmental regulator.";
RL Nature 506:489-493(2014).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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:ESQ92021.1}.
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DR EMBL; AWGD01000008; ESQ92021.1; -; Genomic_DNA.
DR RefSeq; WP_023452112.1; NZ_AWGD01000008.1.
DR AlphaFoldDB; V4PUI6; -.
DR STRING; 1282360.ABAC460_03735; -.
DR PATRIC; fig|1282360.3.peg.733; -.
DR eggNOG; COG3507; Bacteria.
DR OrthoDB; 9801455at2; -.
DR Proteomes; UP000017839; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd18617; GH43_XynB-like; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR041542; GH43_C2.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR42812; BETA-XYLOSIDASE; 1.
DR PANTHER; PTHR42812:SF12; BETA-XYLOSIDASE-RELATED; 1.
DR Pfam; PF17851; GH43_C2; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361187};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361187};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..560
FT /note="Beta-xylosidase C-terminal Concanavalin A-like
FT domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004725074"
FT DOMAIN 381..558
FT /note="Beta-xylosidase C-terminal Concanavalin A-like"
FT /evidence="ECO:0000259|Pfam:PF17851"
FT ACT_SITE 63
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 234
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 169
FT /note="Important for catalytic activity, responsible for
FT pKa modulation of the active site Glu and correct
FT orientation of both the proton donor and substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-2"
SQ SEQUENCE 560 AA; 61885 MW; 6EECEF0319F403AE CRC64;
MRRIAALTAL ALSLAAPALA QPEARFDGIW LRGGHLADES YGQNVPDQPG HYQNPILPGF
YPDPSIERVG DTYYMVNSTF AFWPGIPVWK SKDLVNWTQI GNAIDRPGQL AFSNLGTSRG
VFAPTISHHN GLFYIVNTCV DCKGNFVITA KNPAGPWSDP TWLPFGGIDP SLFFDTDGKA
YIAWNDGPQG EPLYSGHRAI WMQEFDPKTL AMTGEKKLVI NGGVDLAKKP VWVEGPHIYH
VKDWYYLMAA EGGTSTDHSE VIFRSKNVWG PYEPWDQNPI LTQRDLDPNR DQPITSSGHA
DLVQTKSGEW WSVFLATRPY TGDLYNTGRE TFLLPVTWKD GWPVILEHGQ PIPLSVKRPK
GLGDKPQPDP RYQNLHGYNP LTWLSIRGSS KDFLTASKDG QTVTLKARNA ALGDVNAIPS
FAGPRQQGNT TAFDTWVHFT PDEGDRAGVA AVQSDDSYIF CGLTKRNGVT EIILTVRAGA
NDPRDGVVLK SAPVDVKDGV FVTLEARRDK LICMYSEAKD YMKTDLKRLM WDGDATVLST
NKAGGFVGTV FGLYAYSQNP
//
