ID D5V1H8_ARCNC Unreviewed; 362 AA.
AC D5V1H8;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=beta-lactamase {ECO:0000256|ARBA:ARBA00012865};
DE EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865};
DE Flags: Precursor;
GN OrderedLocusNames=Arnit_1758 {ECO:0000313|EMBL:ADG93412.1};
OS Arcobacter nitrofigilis (strain ATCC 33309 / DSM 7299 / CCUG 15893 / LMG
OS 7604 / NCTC 12251 / CI) (Campylobacter nitrofigilis).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Arcobacteraceae; Arcobacter.
OX NCBI_TaxID=572480 {ECO:0000313|EMBL:ADG93412.1, ECO:0000313|Proteomes:UP000000939};
RN [1] {ECO:0000313|EMBL:ADG93412.1, ECO:0000313|Proteomes:UP000000939}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33309 / DSM 7299 / CCUG 15893 / LMG 7604 / NCTC 12251 / CI
RC {ECO:0000313|Proteomes:UP000000939};
RX PubMed=21304714; DOI=10.4056/sigs.912121;
RA Pati A., Gronow S., Lapidus A., Copeland A., Glavina Del Rio T., Nolan M.,
RA Lucas S., Tice H., Cheng J.F., Han C., Chertkov O., Bruce D., Tapia R.,
RA Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C.,
RA Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Arcobacter nitrofigilis type strain (CI).";
RL Stand. Genomic Sci. 2:300-308(2010).
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; CP001999; ADG93412.1; -; Genomic_DNA.
DR RefSeq; WP_013135557.1; NC_014166.1.
DR AlphaFoldDB; D5V1H8; -.
DR STRING; 572480.Arnit_1758; -.
DR KEGG; ant:Arnit_1758; -.
DR eggNOG; COG0790; Bacteria.
DR HOGENOM; CLU_764280_0_0_7; -.
DR OrthoDB; 5348837at2; -.
DR Proteomes; UP000000939; 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 InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR11102:SF147; FIBRONECTIN TYPE-II DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR11102; SEL-1-LIKE PROTEIN; 1.
DR Pfam; PF08238; Sel1; 4.
DR Pfam; PF13181; TPR_8; 5.
DR SMART; SM00671; SEL1; 8.
DR SMART; SM00028; TPR; 5.
DR SUPFAM; SSF81901; HCP-like; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50005; TPR; 2.
PE 4: Predicted;
KW Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000000939};
KW Signal {ECO:0000256|SAM:SignalP};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..362
FT /note="beta-lactamase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003078215"
FT REPEAT 153..186
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 218..251
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
SQ SEQUENCE 362 AA; 42363 MW; 1FB786ACCC84BEED CRC64;
MKIISIIFLS ILFYSFSNAN EAIIKKETYN IKQCNKESYT KEDLKSYETL IKEGELQGYN
CVGLYYMRDK DYKTAEEYFN KGKEKGSIES YAQLGSLYSI FLNDKEKAIE YYTYAANKGH
AKAAHNLGVI YDKKFAYEKA LKWYKKSFEK GDTYSLLAIA HIYRKQKKYD KAIKTFEKAG
KLGESEAFFD LGVFYDKIKK DKEKSNTYFL KCYKLGLGKC AGAIGEAYED LKDYDKAIQW
YKKGFELGSE KSVIGLGLLY SDILKDYDKS IYWYKKCFDK FQYIGCALNI GLTYEIDLKN
YDKAIQWYKK GIELGDNRSA NNLGYFYHHV RKDRKKAIYW YRQAIKLGST KAENNLRDLN
NE
//
