ID K2JZ58_HELPX Unreviewed; 290 AA.
AC K2JZ58;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Beta-lactamase {ECO:0000256|ARBA:ARBA00012865, ECO:0000256|RuleBase:RU366075};
DE EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865, ECO:0000256|RuleBase:RU366075};
GN ORFNames=OUC_0685 {ECO:0000313|EMBL:EKE80668.1};
OS Helicobacter pylori R018c.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1145110 {ECO:0000313|EMBL:EKE80668.1, ECO:0000313|Proteomes:UP000002808};
RN [1] {ECO:0000313|EMBL:EKE80668.1, ECO:0000313|Proteomes:UP000002808}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R018c {ECO:0000313|EMBL:EKE80668.1,
RC ECO:0000313|Proteomes:UP000002808};
RA Blanchard T.G., Czinn S.J., McCracken C.M., Abolude K.A., Shefchek K.S.,
RA Maroo A.M., Santana-Cruz I.S., Tallon L.J., Ficke F.W.F.;
RT "Comparative Sequence Analysis of H. pylori isolates.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Hydrolyzes 6-aminopenicillinic acid and 7-
CC aminocephalosporanic acid (ACA) derivatives.
CC {ECO:0000256|RuleBase:RU366075}.
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,
CC ECO:0000256|RuleBase:RU366075};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613,
CC ECO:0000256|RuleBase:RU366075}.
CC -!- SIMILARITY: Belongs to the hcp beta-lactamase family.
CC {ECO:0000256|ARBA:ARBA00008486, ECO:0000256|RuleBase:RU366075}.
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:EKE80668.1}.
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DR EMBL; AMOQ01000003; EKE80668.1; -; Genomic_DNA.
DR RefSeq; WP_000892715.1; NZ_AMOQ01000003.1.
DR AlphaFoldDB; K2JZ58; -.
DR PATRIC; fig|1145110.4.peg.673; -.
DR Proteomes; UP000002808; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR040239; HcpB-like.
DR InterPro; IPR006597; Sel1-like.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR13891:SF1; CYTOCHROME C OXIDASE ASSEMBLY FACTOR 7; 1.
DR PANTHER; PTHR13891; UNCHARACTERIZED; 1.
DR Pfam; PF08238; Sel1; 7.
DR SMART; SM00671; SEL1; 7.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF81901; HCP-like; 1.
DR PROSITE; PS50005; TPR; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU366075};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU366075};
KW TPR repeat {ECO:0000256|ARBA:ARBA00022803, ECO:0000256|PROSITE-
KW ProRule:PRU00339}.
FT REPEAT 29..62
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
SQ SEQUENCE 290 AA; 31518 MW; 334F1CE56084FCAE CRC64;
MLENVKKSFF RVLCLGALCL GGLMAEQDPK ELVGLGAKSY KEKDFTQAKK YFEKACDLKE
NSGCFNLGVL YYQGQGVEKN LKKAASFYAK ACDLNYSNGC HLLGNLYYSG QGVSQNTNKA
LQYYSKACDL KYAEGCASLG GIYHDGKVVT RDFKKAVEYF TKACDLNDGD GCTILGSLYD
AGRGTPKDLK KALALYDKAC GLKDSPGCFN AGNMYHHGDG VAKNFKEALA RYSKACELEN
GGGCFNLGAM QYNGEGATRN EKQAIENFKK GCKLGAKGAC DILKQLKIKV
//
