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Database: UniProt
Entry: Q17Y63_HELAH
LinkDB: Q17Y63_HELAH
Original site: Q17Y63_HELAH 
ID   Q17Y63_HELAH            Unreviewed;       258 AA.
AC   Q17Y63;
DT   25-JUL-2006, integrated into UniProtKB/TrEMBL.
DT   25-JUL-2006, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   RecName: Full=beta-lactamase {ECO:0000256|ARBA:ARBA00012865};
DE            EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865};
GN   OrderedLocusNames=Hac_0600 {ECO:0000313|EMBL:CAJ99413.1};
OS   Helicobacter acinonychis (strain Sheeba).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=382638 {ECO:0000313|EMBL:CAJ99413.1, ECO:0000313|Proteomes:UP000000775};
RN   [1] {ECO:0000313|EMBL:CAJ99413.1, ECO:0000313|Proteomes:UP000000775}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sheeba {ECO:0000313|EMBL:CAJ99413.1,
RC   ECO:0000313|Proteomes:UP000000775};
RX   PubMed=16789826; DOI=10.1371/journal.pgen.0020120;
RA   Eppinger M., Baar C., Linz B., Raddatz G., Lanz C., Keller H., Morelli G.,
RA   Gressmann H., Achtman M., Schuster S.C.;
RT   "Who ate whom? Adaptive Helicobacter genomic changes that accompanied a
RT   host jump from early humans to large felines.";
RL   PLoS Genet. 2:1097-1110(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a beta-lactam + H2O = a substituted beta-amino acid;
CC         Xref=Rhea:RHEA:20401, ChEBI:CHEBI:15377, ChEBI:CHEBI:35627,
CC         ChEBI:CHEBI:140347; EC=3.5.2.6;
CC         Evidence={ECO:0000256|ARBA:ARBA00001526};
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DR   EMBL; AM260522; CAJ99413.1; -; Genomic_DNA.
DR   RefSeq; WP_011577527.1; NC_008229.1.
DR   AlphaFoldDB; Q17Y63; -.
DR   KEGG; hac:Hac_0600; -.
DR   eggNOG; COG0790; Bacteria.
DR   HOGENOM; CLU_000288_36_7_7; -.
DR   OrthoDB; 5372609at2; -.
DR   BioCyc; HACI382638:HAC_RS02650-MONOMER; -.
DR   Proteomes; UP000000775; Chromosome.
DR   GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR   InterPro; IPR006597; Sel1-like.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR11102:SF147; FIBRONECTIN TYPE-II DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR11102; SEL-1-LIKE PROTEIN; 1.
DR   Pfam; PF08238; Sel1; 6.
DR   SMART; SM00671; SEL1; 6.
DR   SUPFAM; SSF81901; HCP-like; 1.
PE   4: Predicted;
KW   Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157}.
SQ   SEQUENCE   258 AA;  28924 MW;  5B21CB2E3E8ABFFD CRC64;
     MGYASKLALK IGLIGLCLFG TLNGVEHLGH KGSFVYRGEV AYNNKDYERA VSLYKDAIKN
     GESIAYVLLG IMYKDGRGVP RNDKKAVEYF KKAVALDIPR GYNNLGVMYK EGRGVPKDEK
     KAVEYFQMAA NKGYTSAYMN LGIMYMEGRG VPSSYMKATE YFRLAMAKGS AEAYILLGDL
     YYSGNEQLGI EQDKEKAVIY YKMAADVGSS QAYEGLAKSY EYGLGVEKDK KQAEEFRQRA
     CDYDLDKNCR KRNASSHH
//
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