ID V4NXN0_9CAUL Unreviewed; 346 AA.
AC V4NXN0;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Glycoside hydrolase {ECO:0008006|Google:ProtNLM};
GN ORFNames=AEYBE204_07680 {ECO:0000313|EMBL:ESQ79714.1};
OS Asticcacaulis sp. YBE204.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Asticcacaulis.
OX NCBI_TaxID=1282363 {ECO:0000313|EMBL:ESQ79714.1, ECO:0000313|Proteomes:UP000017808};
RN [1] {ECO:0000313|EMBL:ESQ79714.1, ECO:0000313|Proteomes:UP000017808}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YBE204 {ECO:0000313|EMBL:ESQ79714.1,
RC ECO:0000313|Proteomes:UP000017808};
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:ESQ79714.1}.
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DR EMBL; AWGF01000004; ESQ79714.1; -; Genomic_DNA.
DR AlphaFoldDB; V4NXN0; -.
DR STRING; 1282363.AEYBE204_07680; -.
DR PATRIC; fig|1282363.3.peg.1523; -.
DR OrthoDB; 9763933at2; -.
DR Proteomes; UP000017808; 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; cd08981; GH43_Bt1873-like; 1.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR42812; BETA-XYLOSIDASE; 1.
DR PANTHER; PTHR42812:SF5; ENDO-ARABINASE; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361187};
KW Hydrolase {ECO:0000256|RuleBase:RU361187};
KW Reference proteome {ECO:0000313|Proteomes:UP000017808};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..346
FT /note="Glycoside hydrolase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004724152"
FT SITE 171
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 346 AA; 38113 MW; CCD90D1AF25CB3D3 CRC64;
MTTRRTLLAL TTALAVSELS LSAGQARAED APLTLPDMPL HDPWIVADDA TQTYYLYTSN
RERMSGQKGI GIMAYRSRDL IHWTKPSVVF ALPSGIWANA GAWAPEVHVW QGKYYLFVTL
HNEQMPLPGG TPEKPLYRRG TVLGVADTPA GPFTLVRDGE PVASKDLMTL DGTLYVDPKG
DPWMVFAHEW IQTGVGTMEA LPLNADLSAK GPPKTLFKGS ASPWAVPQQG AHIVTDGPEL
YRTSSGALMM LWSSWGKDGY IQTLACSRSG DLFGPWEQLP MLLDKGSGHG MVFKTFEGQL
MLVVHRPFKN ARGYLYEVHD TGTSIELTRQ RTDLDLDKNP LPPFTP
//
