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Beta-lactamase HcpA (EC 3.5.2.6) (Cysteine-rich 28 kDa protein)

 HCPA_HELPJ              Reviewed;         250 AA.
Q9ZMM1;
24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
07-JUN-2017, entry version 119.
RecName: Full=Beta-lactamase HcpA;
EC=3.5.2.6;
AltName: Full=Cysteine-rich 28 kDa protein;
Flags: Precursor;
Name=hcpA; OrderedLocusNames=jhp_0197;
Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori
J99).
Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
Helicobacteraceae; Helicobacter.
NCBI_TaxID=85963;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=J99 / ATCC 700824;
PubMed=9923682; DOI=10.1038/16495;
Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G.,
Tummino P.J., Caruso A., Uria-Nickelsen M., Mills D.M., Ives C.,
Gibson R., Merberg D., Mills S.D., Jiang Q., Taylor D.E., Vovis G.F.,
Trust T.J.;
"Genomic sequence comparison of two unrelated isolates of the human
gastric pathogen Helicobacter pylori.";
Nature 397:176-180(1999).
-!- FUNCTION: Slowly hydrolyzes 6-aminopenicillinic acid and 7-
aminocephalosporanic acid (ACA) derivatives. May be involved in
the synthesis of the cell wall peptidoglycan (By similarity).
{ECO:0000250}.
-!- CATALYTIC ACTIVITY: A beta-lactam + H(2)O = a substituted beta-
amino acid.
-!- ENZYME REGULATION: Inhibited by cloxacillin and oxacillin but not
by ACA derivatives or metal chelators. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
-!- SIMILARITY: Belongs to the hcp beta-lactamase family.
{ECO:0000305}.
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EMBL; AE001439; AAD05781.1; -; Genomic_DNA.
PIR; B71961; B71961.
RefSeq; WP_000901652.1; NZ_CP011330.1.
ProteinModelPortal; Q9ZMM1; -.
SMR; Q9ZMM1; -.
STRING; 85963.jhp0197; -.
EnsemblBacteria; AAD05781; AAD05781; jhp_0197.
KEGG; hpj:jhp_0197; -.
PATRIC; fig|85963.30.peg.823; -.
eggNOG; ENOG4108730; Bacteria.
eggNOG; COG0790; LUCA.
KO; K07126; -.
OMA; ACFYLSG; -.
OrthoDB; POG091H02JQ; -.
Proteomes; UP000000804; Chromosome.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-EC.
GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
InterPro; IPR006597; Sel1-like.
InterPro; IPR019734; TPR_repeat.
Pfam; PF08238; Sel1; 6.
SMART; SM00671; SEL1; 6.
SMART; SM00028; TPR; 2.
3: Inferred from homology;
Antibiotic resistance; Complete proteome; Disulfide bond; Hydrolase;
Repeat; Secreted; Signal; TPR repeat.
SIGNAL 1 25 {ECO:0000255}.
CHAIN 26 250 Beta-lactamase HcpA.
/FTId=PRO_0000013195.
REPEAT 29 62 TPR 1.
REPEAT 67 98 TPR 2.
REPEAT 100 133 TPR 3.
REPEAT 134 169 TPR 4.
REPEAT 170 202 TPR 5.
DISULFID 56 64 {ECO:0000250}.
DISULFID 92 100 {ECO:0000250}.
DISULFID 128 136 {ECO:0000250}.
DISULFID 164 172 {ECO:0000250}.
DISULFID 196 204 {ECO:0000250}.
DISULFID 232 240 {ECO:0000250}.
SEQUENCE 250 AA; 27295 MW; 94EC37877E98C578 CRC64;
MLGSVKKTLF GVLCLGALCL RGLMAEPDAK ELVSLGIESV KKQDFAQAKA HFEKACELKE
GFGCVFLGAF YEEGKGVGKD LKKAIQFYTK GCELNDGYGC RLLGNLYYNG QGVSKDAKKA
SQYYSKSCEL NHAEGCTVLG SLHHYGVGTP KDLRKALDLY EKACDLKDSP GCINAGYMYG
VAKNFKEAIV RYSKACELKD GRGCYNLGVM QYNAQGTAKD EKQAVENFKK GCKSSVKEAC
DALKELKIEL


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