HCPE_HELPJ
ID HCPE_HELPJ Reviewed; 355 AA.
AC Q9ZMJ9;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Putative beta-lactamase HcpE;
DE EC=3.5.2.6;
DE AltName: Full=Cysteine-rich protein E;
DE Flags: Precursor;
GN Name=hcpE; OrderedLocusNames=jhp_0220;
OS Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J99 / ATCC 700824;
RX PubMed=9923682; DOI=10.1038/16495;
RA Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT "Genomic sequence comparison of two unrelated isolates of the human gastric
RT pathogen Helicobacter pylori.";
RL Nature 397:176-180(1999).
CC -!- FUNCTION: May hydrolyze 6-aminopenicillinic acid and 7-
CC aminocephalosporanic acid (ACA) derivatives. {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the hcp beta-lactamase family. {ECO:0000305}.
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DR EMBL; AE001439; AAD05807.1; -; Genomic_DNA.
DR PIR; G71958; G71958.
DR RefSeq; WP_001022031.1; NZ_CP011330.1.
DR AlphaFoldDB; Q9ZMJ9; -.
DR SMR; Q9ZMJ9; -.
DR STRING; 85963.jhp_0220; -.
DR EnsemblBacteria; AAD05807; AAD05807; jhp_0220.
DR KEGG; hpj:jhp_0220; -.
DR PATRIC; fig|85963.30.peg.794; -.
DR eggNOG; COG0790; Bacteria.
DR OMA; IMIYDKG; -.
DR Proteomes; UP000000804; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; -; 2.
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; PTHR13891; 3.
DR Pfam; PF08238; Sel1; 8.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00671; SEL1; 8.
PE 3: Inferred from homology;
KW Antibiotic resistance; Disulfide bond; Hydrolase; Repeat; Secreted; Signal;
KW TPR repeat.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..355
FT /note="Putative beta-lactamase HcpE"
FT /id="PRO_0000013201"
FT REPEAT 27..60
FT /note="TPR 1"
FT REPEAT 63..96
FT /note="TPR 2"
FT REPEAT 98..131
FT /note="TPR 3"
FT REPEAT 132..166
FT /note="TPR 4"
FT REPEAT 202..240
FT /note="TPR 5"
FT REPEAT 245..275
FT /note="TPR 6"
FT REPEAT 276..311
FT /note="TPR 7"
FT REPEAT 312..344
FT /note="TPR 8"
FT DISULFID 54..62
FT /evidence="ECO:0000255"
FT DISULFID 90..98
FT /evidence="ECO:0000255"
FT DISULFID 126..134
FT /evidence="ECO:0000255"
FT DISULFID 160..168
FT /evidence="ECO:0000255"
FT DISULFID 197..205
FT /evidence="ECO:0000255"
FT DISULFID 234..242
FT /evidence="ECO:0000255"
FT DISULFID 270..278
FT /evidence="ECO:0000255"
FT DISULFID 306..314
FT /evidence="ECO:0000255"
FT DISULFID 338..346
FT /evidence="ECO:0000255"
SQ SEQUENCE 355 AA; 39320 MW; 30F140204B9BCA3A CRC64;
MNIKILKILV GGLFFLSLNA HLWGKQDNSF LGIGERAYKS GNYSKAASYF KKACNDGVSE
GCTQLGIIYE NGQGTRIDYK KALEYYKTAC QADDREGCFG LGGLYDEGLG TAQNYQEAID
AYAKACVLKH PESCYNLGII YDRKIKGNAA QAVTYYQKSC NFDMAKGCYI LGTAYEKGFL
EVKQSNHKAV IYYLKACRLN EGQACRALGS LFENGDAGLD EDFEVAFDYL QKACALNNSG
GCASLGSMYM LGRYVKKDPQ KAFNYFKQAC DMGSAVSCSR MGFMYSQGDT VSKDLRKALD
NYERGCDMGD EVGCFALAGM YYNMKDKENA IMIYDKGCKL GMKQACENLT KLRGY