位置:首页 > 蛋白库 > BLP4_PSEAI
BLP4_PSEAI
ID   BLP4_PSEAI              Reviewed;         288 AA.
AC   P16897;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Beta-lactamase PSE-4;
DE            EC=3.5.2.6;
DE   AltName: Full=Beta-lactamase CARB-1;
DE   AltName: Full=Carbenicillinase 1;
DE   Flags: Precursor;
GN   Name=pse4; Synonyms=carB1;
OS   Pseudomonas aeruginosa.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Dalgleish; TRANSPOSON=Tn1405;
RX   PubMed=2295609; DOI=10.1016/s0021-9258(19)40181-6;
RA   Boissinot M., Levesque R.C.;
RT   "Nucleotide sequence of the PSE-4 carbenicillinase gene and correlations
RT   with the Staphylococcus aureus PC1 beta-lactamase crystal structure.";
RL   J. Biol. Chem. 265:1225-1230(1990).
CC   -!- FUNCTION: Hydrolyzes both carbenicillin and oxacillin.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA25979.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; J05162; AAA25979.1; ALT_INIT; Genomic_DNA.
DR   PIR; A35001; A35001.
DR   RefSeq; WP_063857835.1; NZ_LLOM01000076.1.
DR   PDB; 1G68; X-ray; 1.95 A; A=18-288.
DR   PDB; 1G6A; X-ray; 1.75 A; A=18-288.
DR   PDB; 4ID4; X-ray; 1.05 A; A=145-185.
DR   PDB; 4R4R; X-ray; 1.20 A; A=145-185.
DR   PDBsum; 1G68; -.
DR   PDBsum; 1G6A; -.
DR   PDBsum; 4ID4; -.
DR   PDBsum; 4R4R; -.
DR   AlphaFoldDB; P16897; -.
DR   BMRB; P16897; -.
DR   SMR; P16897; -.
DR   ChEMBL; CHEMBL1744489; -.
DR   BRENDA; 3.5.2.6; 5087.
DR   SABIO-RK; P16897; -.
DR   EvolutionaryTrace; P16897; -.
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; Disulfide bond; Hydrolase; Signal;
KW   Transposable element.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..288
FT                   /note="Beta-lactamase PSE-4"
FT                   /id="PRO_0000017047"
FT   ACT_SITE        65
FT                   /note="Acyl-ester intermediate"
FT   BINDING         229..231
FT                   /ligand="substrate"
FT   DISULFID        72..118
FT                   /evidence="ECO:0000250"
FT   HELIX           23..35
FT                   /evidence="ECO:0007829|PDB:1G6A"
FT   STRAND          39..46
FT                   /evidence="ECO:0007829|PDB:1G6A"
FT   TURN            47..50
FT                   /evidence="ECO:0007829|PDB:1G6A"
FT   STRAND          51..56
FT                   /evidence="ECO:0007829|PDB:1G6A"
FT   HELIX           64..66
FT                   /evidence="ECO:0007829|PDB:4R4R"
FT   HELIX           68..80
FT                   /evidence="ECO:0007829|PDB:1G6A"
FT   STRAND          89..91
FT                   /evidence="ECO:0007829|PDB:1G6A"
FT   HELIX           94..96
FT                   /evidence="ECO:0007829|PDB:1G6A"
FT   HELIX           104..106
FT                   /evidence="ECO:0007829|PDB:1G6A"
FT   STRAND          110..113
FT                   /evidence="ECO:0007829|PDB:1G6A"
FT   HELIX           114..124
FT                   /evidence="ECO:0007829|PDB:1G6A"
FT   HELIX           127..136
FT                   /evidence="ECO:0007829|PDB:1G6A"
FT   HELIX           145..149
FT                   /evidence="ECO:0007829|PDB:4ID4"
FT   HELIX           163..165
FT                   /evidence="ECO:0007829|PDB:4ID4"
FT   HELIX           178..185
FT                   /evidence="ECO:0007829|PDB:4ID4"
FT   STRAND          191..194
FT                   /evidence="ECO:0007829|PDB:1G6A"
FT   HELIX           196..207
FT                   /evidence="ECO:0007829|PDB:1G6A"
FT   TURN            213..215
FT                   /evidence="ECO:0007829|PDB:1G6A"
FT   HELIX           216..219
FT                   /evidence="ECO:0007829|PDB:1G6A"
FT   STRAND          225..232
FT                   /evidence="ECO:0007829|PDB:1G6A"
FT   HELIX           234..236
FT                   /evidence="ECO:0007829|PDB:1G6A"
FT   STRAND          238..246
FT                   /evidence="ECO:0007829|PDB:1G6A"
FT   STRAND          249..260
FT                   /evidence="ECO:0007829|PDB:1G6A"
FT   HELIX           265..284
FT                   /evidence="ECO:0007829|PDB:1G6A"
SQ   SEQUENCE   288 AA;  31406 MW;  0E618F058720F3A5 CRC64;
     MKFLLAFSLL IPSVVFASSS KFQQVEQDVK AIEVSLSARI GVSVLDTQNG EYWDYNGNQR
     FPLTSTFKTI ACAKLLYDAE QGKVNPNSTV EIKKADLVTY SPVIEKQVGQ AITLDDACFA
     TMTTSDNTAA NIILSAVGGP KGVTDFLRQI GDKETRLDRI EPDLNEGKLG DLRDTTTPKA
     IASTLNKFLF GSALSEMNQK KLESWMVNNQ VTGNLLRSVL PAGWNIADRS GAGGFGARSI
     TAVVWSEHQA PIIVSIYLAQ TQASMEERND AIVKIGHSIF DVYTSQSR
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2025