ID A9HXX9_BORPD Unreviewed; 386 AA.
AC A9HXX9;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Alpha-galactosidase NEW3 domain-containing protein {ECO:0000259|Pfam:PF10633};
GN OrderedLocusNames=Bpet0291 {ECO:0000313|EMBL:CAP40623.1};
OS Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=340100 {ECO:0000313|EMBL:CAP40623.1, ECO:0000313|Proteomes:UP000001225};
RN [1] {ECO:0000313|EMBL:CAP40623.1, ECO:0000313|Proteomes:UP000001225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-461 / DSM 12804 / CCUG 43448
RC {ECO:0000313|Proteomes:UP000001225};
RX PubMed=18826580; DOI=10.1186/1471-2164-9-449;
RA Gross R., Guzman C.A., Sebaihia M., Martins Dos Santos V.A., Pieper D.H.,
RA Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V.,
RA Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S.,
RA Linke B., Meyer F., Mormann S., Nakunst D., Rueckert C.,
RA Schneiker-Bekel S., Schulze K., Vorhoelter F.J., Yevsa T., Engle J.T.,
RA Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O.,
RA Martinez-Arias R.;
RT "The missing link: Bordetella petrii is endowed with both the metabolic
RT versatility of environmental bacteria and virulence traits of pathogenic
RT Bordetellae.";
RL BMC Genomics 9:449-449(2008).
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DR EMBL; AM902716; CAP40623.1; -; Genomic_DNA.
DR AlphaFoldDB; A9HXX9; -.
DR STRING; 94624.Bpet0291; -.
DR KEGG; bpt:Bpet0291; -.
DR eggNOG; COG1470; Bacteria.
DR Proteomes; UP000001225; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR018905; A-galactase_NEW3.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR39198; HYPOTHETICAL MEMBRANE PROTEIN, CONSERVED; 1.
DR PANTHER; PTHR39198:SF1; NPCBM_ASSOC DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF10633; NPCBM_assoc; 1.
PE 4: Predicted;
KW Glycosidase {ECO:0000313|EMBL:CAP40623.1};
KW Hydrolase {ECO:0000313|EMBL:CAP40623.1};
KW Membrane {ECO:0000256|SAM:Phobius}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..386
FT /note="Alpha-galactosidase NEW3 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002738589"
FT TRANSMEM 360..381
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 267..341
FT /note="Alpha-galactosidase NEW3"
FT /evidence="ECO:0000259|Pfam:PF10633"
SQ SEQUENCE 386 AA; 39985 MW; B3AE16016A8E1B34 CRC64;
MRKALSFLAL AAAMLLSTPV LAQGGNIKGL YLVTDYPAVT AQPGTTSTVR LQLRNYGLPP
ERLGLAIDGV PDGWTATLLG GGQPVAAAMP STDDSVSLQL QLKVPADAGT QPRTLTVVAS
GDGQRIELPV HIMLAKELPT KLTLDTKLPA IKGGAQSSFD YSLTVKNDSG KDLTVSFAAK
APQYFDTRFT EGYGSQQISA LPIKAGESKD IKLTVRPPSS TEPGSYPVQV VASADGIEAS
SQLKLDIVGQ PRLQLAGRDG LMSGDAQAGK ASTIPVVIRN DGGAAADNVA LSGSGPSGWK
VEFEPKTIEH LAPGQQVEAQ ASITPSERSL AGDYMTHLSA SANGQSASGD FRITVSTSSL
WGIVGVIILA IAALILVGAV ARFGRR
//
