ID C3XGH5_9HELI Unreviewed; 256 AA.
AC C3XGH5;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 24-JAN-2024, entry version 43.
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=HRAG_01171 {ECO:0000313|EMBL:EEO24114.1};
OS Helicobacter bilis ATCC 43879.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=613026 {ECO:0000313|EMBL:EEO24114.1, ECO:0000313|Proteomes:UP000005085};
RN [1] {ECO:0000313|EMBL:EEO24114.1, ECO:0000313|Proteomes:UP000005085}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43879 {ECO:0000313|EMBL:EEO24114.1,
RC ECO:0000313|Proteomes:UP000005085};
RX PubMed=25212613;
RA Shen Z., Sheh A., Young S.K., Abouelliel A., Ward D.V., Earl A.M.,
RA Fox J.G.;
RT "Draft genome sequences of six enterohepatic helicobacter species isolated
RT from humans and one from rhesus macaques.";
RL Genome Announc. 2:e00857-e00814(2014).
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|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:EEO24114.1}.
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DR EMBL; ACDN02000034; EEO24114.1; -; Genomic_DNA.
DR RefSeq; WP_005218576.1; NZ_KI392038.1.
DR AlphaFoldDB; C3XGH5; -.
DR eggNOG; COG0790; Bacteria.
DR HOGENOM; CLU_1084905_0_0_7; -.
DR OrthoDB; 5329787at2; -.
DR Proteomes; UP000005085; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 PANTHER; PTHR13891:SF1; CYTOCHROME C OXIDASE ASSEMBLY FACTOR 7; 1.
DR PANTHER; PTHR13891; UNCHARACTERIZED; 1.
DR SMART; SM00671; SEL1; 3.
DR SUPFAM; SSF81901; HCP-like; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|RuleBase:RU366075};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000005085};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|RuleBase:RU366075};
KW TPR repeat {ECO:0000256|ARBA:ARBA00022803};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 256 AA; 28491 MW; A149CCF88C10AEE0 CRC64;
MVNAIAMSAY RNKFKYIKVD SVLYRYLVVF FCNVFVAFAN PYMPHKANNI QRVQQDIMPL
LQQCSNGIKD SCSLLLKQGV PSVNECEIHV CHIIGATLSA NGSDREAIPY LQKSCQSSEK
LGCSLLGLLY QMSGNIDEAE IAYNAACNNA DVIGCYNMGV LQSMRSSSNV GGHAALQSFT
RACSMQYPQA CFNLAVVYAN YKKDFANALY FFHIACDYGM MESCKNVKLL KDSGITLPPL
QKKRGLYVRL DSKQKQ
//
