BLO10_PSEAI
ID BLO10_PSEAI Reviewed; 266 AA.
AC P14489;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Beta-lactamase OXA-10;
DE EC=3.5.2.6;
DE AltName: Full=Beta-lactamase PSE-2;
DE Flags: Precursor;
GN Name=bla; Synonyms=oxa10, pse2;
OS Pseudomonas aeruginosa.
OG Plasmid pMON234.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TRANSPOSON=Tn1404;
RX PubMed=3126705; DOI=10.1128/aac.32.1.134;
RA Huovinen P., Huovinen S., Jacoby G.A.;
RT "Sequence of PSE-2 beta-lactamase.";
RL Antimicrob. Agents Chemother. 32:134-136(1988).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.66 ANGSTROMS) OF 21-266, AND CARBOXYLATION AT
RP LYS-70.
RX PubMed=11188693; DOI=10.1016/s0969-2126(00)00534-7;
RA Maveyraud L., Golemi D., Kotra L.P., Tranier S., Vakulenko S.,
RA Mobashery S., Samama J.-P.;
RT "Insights into class D beta-lactamases are revealed by the crystal
RT structure of the OXA10 enzyme from Pseudomonas aeruginosa.";
RL Structure 8:1289-1298(2000).
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:PRU10103};
CC -!- SIMILARITY: Belongs to the class-D beta-lactamase family.
CC {ECO:0000305}.
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DR EMBL; U37105; AAB60534.1; -; Genomic_DNA.
DR EMBL; J03427; AAA25648.1; -; Genomic_DNA.
DR PIR; S06462; S06462.
DR RefSeq; WP_000846390.1; NZ_WXZW01000004.1.
DR PDB; 1E3U; X-ray; 1.66 A; A/B/C/D=21-266.
DR PDB; 1E4D; X-ray; 1.80 A; A/B/C/D=21-266.
DR PDB; 1EWZ; X-ray; 2.40 A; A/B/C/D=21-266.
DR PDB; 1FOF; X-ray; 2.00 A; A/B=20-265.
DR PDB; 1K4E; X-ray; 2.00 A; A/B=20-266.
DR PDB; 1K4F; X-ray; 1.60 A; A/B=20-266.
DR PDB; 1K54; X-ray; 1.70 A; A/B/C/D=21-266.
DR PDB; 1K55; X-ray; 1.39 A; A/B/C/D=21-266.
DR PDB; 1K56; X-ray; 1.70 A; A/B/C/D=21-266.
DR PDB; 1K57; X-ray; 1.90 A; A/B/C/D=21-266.
DR PDB; 1K6R; X-ray; 2.30 A; A/B=20-266.
DR PDB; 1K6S; X-ray; 2.03 A; A/B=20-266.
DR PDB; 2HP5; X-ray; 2.70 A; A/B/C/D=20-266.
DR PDB; 2HP6; X-ray; 2.20 A; A/B=20-266.
DR PDB; 2HP9; X-ray; 2.50 A; A/B=20-266.
DR PDB; 2HPB; X-ray; 2.05 A; A/B=20-266.
DR PDB; 2RL3; X-ray; 1.90 A; A/B=20-266.
DR PDB; 2WGI; X-ray; 2.85 A; A/B=21-266.
DR PDB; 2WGV; X-ray; 1.80 A; A/B=20-266.
DR PDB; 2WGW; X-ray; 1.80 A; A/B=20-266.
DR PDB; 2WKH; X-ray; 1.79 A; A/B=20-266.
DR PDB; 2WKI; X-ray; 2.10 A; A/B=20-266.
DR PDB; 2X01; X-ray; 1.90 A; A/B=20-266.
DR PDB; 2X02; X-ray; 1.35 A; A/B=20-266.
DR PDB; 3LCE; X-ray; 2.00 A; A/B/C/D=21-266.
DR PDB; 4S2O; X-ray; 1.70 A; A/B=20-265.
DR PDB; 4WZ5; X-ray; 1.60 A; A/B/C/D=20-266.
DR PDB; 5FQ9; X-ray; 1.50 A; A/B=20-266.
DR PDB; 5MMY; X-ray; 1.88 A; A/B=20-264.
DR PDB; 5MNU; X-ray; 1.56 A; A/B=20-265.
DR PDB; 5MOX; X-ray; 1.41 A; A/B=20-265.
DR PDB; 5MOZ; X-ray; 1.34 A; A/B=20-265.
DR PDB; 6RTN; X-ray; 2.17 A; A/B=20-265.
DR PDB; 7B3R; X-ray; 1.83 A; A/B=20-265.
DR PDB; 7B3S; X-ray; 1.85 A; A/B=20-265.
DR PDB; 7B3U; X-ray; 1.60 A; A/B=20-265.
DR PDBsum; 1E3U; -.
DR PDBsum; 1E4D; -.
DR PDBsum; 1EWZ; -.
DR PDBsum; 1FOF; -.
DR PDBsum; 1K4E; -.
DR PDBsum; 1K4F; -.
DR PDBsum; 1K54; -.
DR PDBsum; 1K55; -.
DR PDBsum; 1K56; -.
DR PDBsum; 1K57; -.
DR PDBsum; 1K6R; -.
DR PDBsum; 1K6S; -.
DR PDBsum; 2HP5; -.
DR PDBsum; 2HP6; -.
DR PDBsum; 2HP9; -.
DR PDBsum; 2HPB; -.
DR PDBsum; 2RL3; -.
DR PDBsum; 2WGI; -.
DR PDBsum; 2WGV; -.
DR PDBsum; 2WGW; -.
DR PDBsum; 2WKH; -.
DR PDBsum; 2WKI; -.
DR PDBsum; 2X01; -.
DR PDBsum; 2X02; -.
DR PDBsum; 3LCE; -.
DR PDBsum; 4S2O; -.
DR PDBsum; 4WZ5; -.
DR PDBsum; 5FQ9; -.
DR PDBsum; 5MMY; -.
DR PDBsum; 5MNU; -.
DR PDBsum; 5MOX; -.
DR PDBsum; 5MOZ; -.
DR PDBsum; 6RTN; -.
DR PDBsum; 7B3R; -.
DR PDBsum; 7B3S; -.
DR PDBsum; 7B3U; -.
DR AlphaFoldDB; P14489; -.
DR SMR; P14489; -.
DR BindingDB; P14489; -.
DR ChEMBL; CHEMBL5482; -.
DR DrugBank; DB02122; 4-iodo-acetamido phenylboronic acid.
DR DrugBank; DB04342; 7-((Carboxy(4-Hydroxyphenyl)Acetyl)Amino)-7-Methoxy-(3-((1-Methyl-1h-Tetrazol-5-Yl)Thio)Methyl)-8-Oxo-5-Oxa-1-Azabicyclo[4.2.0]Oct-2-Ene-2-Carboxylic Acid.
DR DrugBank; DB03801; Lysine Nz-Carboxylic Acid.
DR DrugBank; DB00760; Meropenem.
DR KEGG; ag:AAB60534; -.
DR BRENDA; 3.5.2.6; 5087.
DR EvolutionaryTrace; P14489; -.
DR PRO; PR:P14489; -.
DR GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-EC.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0017001; P: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; IPR002137; Beta-lactam_class-D_AS.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56601; SSF56601; 1.
DR PROSITE; PS00337; BETA_LACTAMASE_D; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; Disulfide bond; Hydrolase; Plasmid;
KW Signal; Transposable element.
FT SIGNAL 1..20
FT CHAIN 21..266
FT /note="Beta-lactamase OXA-10"
FT /id="PRO_0000017030"
FT ACT_SITE 67
FT /note="Acyl-ester intermediate"
FT BINDING 205..207
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 70
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000269|PubMed:11188693"
FT DISULFID 44..51
FT STRAND 21..24
FT /evidence="ECO:0007829|PDB:5MOZ"
FT HELIX 26..29
FT /evidence="ECO:0007829|PDB:5MOZ"
FT HELIX 30..33
FT /evidence="ECO:0007829|PDB:5MOZ"
FT TURN 34..36
FT /evidence="ECO:0007829|PDB:5MOZ"
FT STRAND 39..45
FT /evidence="ECO:0007829|PDB:5MOZ"
FT TURN 46..49
FT /evidence="ECO:0007829|PDB:5MOZ"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:5MOZ"
FT HELIX 56..59
FT /evidence="ECO:0007829|PDB:5MOZ"
FT HELIX 66..69
FT /evidence="ECO:0007829|PDB:5MOZ"
FT HELIX 70..79
FT /evidence="ECO:0007829|PDB:5MOZ"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:1E3U"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:5MOZ"
FT HELIX 108..113
FT /evidence="ECO:0007829|PDB:5MOZ"
FT HELIX 117..127
FT /evidence="ECO:0007829|PDB:5MOZ"
FT HELIX 129..138
FT /evidence="ECO:0007829|PDB:5MOZ"
FT TURN 150..155
FT /evidence="ECO:0007829|PDB:5MOZ"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:5MOZ"
FT HELIX 163..174
FT /evidence="ECO:0007829|PDB:5MOZ"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:5MOZ"
FT HELIX 182..192
FT /evidence="ECO:0007829|PDB:5MOZ"
FT STRAND 193..197
FT /evidence="ECO:0007829|PDB:5MOZ"
FT STRAND 200..208
FT /evidence="ECO:0007829|PDB:5MOZ"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:7B3S"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:4WZ5"
FT STRAND 218..228
FT /evidence="ECO:0007829|PDB:5MOZ"
FT STRAND 231..242
FT /evidence="ECO:0007829|PDB:5MOZ"
FT HELIX 244..248
FT /evidence="ECO:0007829|PDB:5MOZ"
FT HELIX 249..260
FT /evidence="ECO:0007829|PDB:5MOZ"
SQ SEQUENCE 266 AA; 29507 MW; 9ABFF429D028F240 CRC64;
MKTFAAYVII ACLSSTALAG SITENTSWNK EFSAEAVNGV FVLCKSSSKS CATNDLARAS
KEYLPASTFK IPNAIIGLET GVIKNEHQVF KWDGKPRAMK QWERDLTLRG AIQVSAVPVF
QQIAREVGEV RMQKYLKKFS YGNQNISGGI DKFWLEGQLR ISAVNQVEFL ESLYLNKLSA
SKENQLIVKE ALVTEAAPEY LVHSKTGFSG VGTESNPGVA WWVGWVEKET EVYFFAFNMD
IDNESKLPLR KSIPTKIMES EGIIGG
