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BLC97_ECOLX
ID   BLC97_ECOLX             Reviewed;         291 AA.
AC   E1ANH6;
DT   06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2010, sequence version 1.
DT   03-AUG-2022, entry version 33.
DE   RecName: Full=Beta-lactamase CTX-M-97;
DE            EC=3.5.2.6;
DE   Flags: Precursor;
GN   Name=bla;
OS   Escherichia coli.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROBABLE FUNCTION.
RC   STRAIN=B275;
RX   PubMed=23117265; DOI=10.1007/s10096-012-1765-9;
RA   Karfunkel D., Carmeli Y., Chmelnitsky I., Kotlovsky T., Navon-Venezia S.;
RT   "The emergence and dissemination of CTX-M-producing Escherichia coli
RT   sequence type 131 causing community-onset bacteremia in Israel.";
RL   Eur. J. Clin. Microbiol. Infect. Dis. 32:513-521(2013).
CC   -!- FUNCTION: Is probably capable of hydrolyzing cephalosporins such as
CC       ceftriaxone and ceftazidime, thus conferring resistance to these
CC       antibiotics.
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; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU10101};
CC   -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC       {ECO:0000305}.
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DR   EMBL; HM776707; ADM08178.1; -; Genomic_DNA.
DR   RefSeq; WP_063860093.1; NG_049051.1.
DR   PDB; 5A90; Neutron; 1.70 A; A=30-291.
DR   PDB; 5A91; X-ray; 1.20 A; A=30-291.
DR   PDB; 5A92; X-ray; 1.05 A; A=30-291.
DR   PDB; 5A93; Other; 1.60 A; A=30-291.
DR   PDB; 5G18; X-ray; 1.10 A; A=30-291.
DR   PDBsum; 5A90; -.
DR   PDBsum; 5A91; -.
DR   PDBsum; 5A92; -.
DR   PDBsum; 5A93; -.
DR   PDBsum; 5G18; -.
DR   AlphaFoldDB; E1ANH6; -.
DR   SMR; E1ANH6; -.
DR   KEGG; ag:ADM08178; -.
DR   GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030655; P:beta-lactam antibiotic catabolic process; IEA:InterPro.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.710.10; -; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR045155; Beta-lactam_cat.
DR   InterPro; IPR000871; Beta-lactam_class-A.
DR   InterPro; IPR023650; Beta-lactam_class-A_AS.
DR   PANTHER; PTHR35333; PTHR35333; 1.
DR   Pfam; PF13354; Beta-lactamase2; 1.
DR   PRINTS; PR00118; BLACTAMASEA.
DR   SUPFAM; SSF56601; SSF56601; 1.
DR   PROSITE; PS00146; BETA_LACTAMASE_A; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antibiotic resistance; Hydrolase; Signal.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..291
FT                   /note="Beta-lactamase CTX-M-97"
FT                   /id="PRO_0000420868"
FT   ACT_SITE        73
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10101"
FT   BINDING         237..239
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   HELIX           33..44
FT                   /evidence="ECO:0007829|PDB:5A92"
FT   STRAND          46..54
FT                   /evidence="ECO:0007829|PDB:5A92"
FT   TURN            55..57
FT                   /evidence="ECO:0007829|PDB:5A92"
FT   STRAND          60..64
FT                   /evidence="ECO:0007829|PDB:5A92"
FT   HELIX           72..75
FT                   /evidence="ECO:0007829|PDB:5A92"
FT   HELIX           76..87
FT                   /evidence="ECO:0007829|PDB:5A92"
FT   STRAND          97..99
FT                   /evidence="ECO:0007829|PDB:5A92"
FT   HELIX           102..104
FT                   /evidence="ECO:0007829|PDB:5A92"
FT   HELIX           112..115
FT                   /evidence="ECO:0007829|PDB:5A92"
FT   STRAND          118..121
FT                   /evidence="ECO:0007829|PDB:5A92"
FT   HELIX           122..132
FT                   /evidence="ECO:0007829|PDB:5A92"
FT   HELIX           135..145
FT                   /evidence="ECO:0007829|PDB:5A92"
FT   HELIX           148..157
FT                   /evidence="ECO:0007829|PDB:5A92"
FT   HELIX           171..173
FT                   /evidence="ECO:0007829|PDB:5A92"
FT   HELIX           186..198
FT                   /evidence="ECO:0007829|PDB:5A92"
FT   STRAND          199..202
FT                   /evidence="ECO:0007829|PDB:5A92"
FT   HELIX           204..215
FT                   /evidence="ECO:0007829|PDB:5A92"
FT   TURN            221..223
FT                   /evidence="ECO:0007829|PDB:5A92"
FT   HELIX           224..227
FT                   /evidence="ECO:0007829|PDB:5A92"
FT   STRAND          232..240
FT                   /evidence="ECO:0007829|PDB:5A92"
FT   STRAND          246..253
FT                   /evidence="ECO:0007829|PDB:5A92"
FT   STRAND          255..257
FT                   /evidence="ECO:0007829|PDB:5A92"
FT   STRAND          260..267
FT                   /evidence="ECO:0007829|PDB:5A92"
FT   HELIX           277..288
FT                   /evidence="ECO:0007829|PDB:5A92"
SQ   SEQUENCE   291 AA;  31279 MW;  8E91A7B8C810A2D1 CRC64;
     MMTQSIGRSM LTVMATLPLL FSSATLHAQA NSVQQQLEAL EKSSGGRLGV ALINTADNSQ
     ILYRADERFA MCSTSKVMAA AAVLKQSESD KHLLNQRVEI KKSDLVNYNP IAEKHVNGTM
     TLAELGAAAL QYSDNTAMNK LIAHLGGPDK VTAFARSLGD ETFRLDRTEP TLNTAIPGDP
     RDTTTPLAMA QTLKNLTLGK ALAETQRAQL VTWLKGNTTG SASIRAGLPK SWVVGDKTGS
     GDYGTTNDIA VIWPENHAPL VLVTYFTQPE QKAESRRDIL AAAAKIVTHG F
 
 
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