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Beta-lactamase OXA-10 (EC 3.5.2.6) (Beta-lactamase PSE-2)

 BLO10_PSEAI             Reviewed;         266 AA.
P14489;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
01-JAN-1990, sequence version 1.
25-OCT-2017, entry version 111.
RecName: Full=Beta-lactamase OXA-10;
EC=3.5.2.6;
AltName: Full=Beta-lactamase PSE-2;
Flags: Precursor;
Name=bla; Synonyms=oxa10, pse2;
Pseudomonas aeruginosa.
Plasmid pMON234.
Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
Pseudomonadaceae; Pseudomonas.
NCBI_TaxID=287;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TRANSPOSON=Tn1404;
PubMed=3126705; DOI=10.1128/AAC.32.1.134;
Huovinen P., Huovinen S., Jacoby G.A.;
"Sequence of PSE-2 beta-lactamase.";
Antimicrob. Agents Chemother. 32:134-136(1988).
[2]
X-RAY CRYSTALLOGRAPHY (1.66 ANGSTROMS) OF 21-266, AND CARBAMYLATION AT
LYS-70.
PubMed=11188693; DOI=10.1016/S0969-2126(00)00534-7;
Maveyraud L., Golemi D., Kotra L.P., Tranier S., Vakulenko S.,
Mobashery S., Samama J.-P.;
"Insights into class D beta-lactamases are revealed by the crystal
structure of the OXA10 enzyme from Pseudomonas aeruginosa.";
Structure 8:1289-1298(2000).
-!- FUNCTION: Hydrolyzes both carbenicillin and oxacillin.
-!- CATALYTIC ACTIVITY: A beta-lactam + H(2)O = a substituted beta-
amino acid. {ECO:0000255|PROSITE-ProRule:PRU10103}.
-!- SIMILARITY: Belongs to the class-D beta-lactamase family.
{ECO:0000305}.
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EMBL; U37105; AAB60534.1; -; Genomic_DNA.
EMBL; J03427; AAA25648.1; -; Genomic_DNA.
PIR; S06462; S06462.
RefSeq; WP_000846390.1; NZ_NIJD01000051.1.
PDB; 1E3U; X-ray; 1.66 A; A/B/C/D=21-266.
PDB; 1E4D; X-ray; 1.80 A; A/B/C/D=21-266.
PDB; 1EWZ; X-ray; 2.40 A; A/B/C/D=21-266.
PDB; 1FOF; X-ray; 2.00 A; A/B=20-265.
PDB; 1K4E; X-ray; 2.00 A; A/B=20-266.
PDB; 1K4F; X-ray; 1.60 A; A/B=20-266.
PDB; 1K54; X-ray; 1.70 A; A/B/C/D=21-266.
PDB; 1K55; X-ray; 1.39 A; A/B/C/D=21-266.
PDB; 1K56; X-ray; 1.70 A; A/B/C/D=21-266.
PDB; 1K57; X-ray; 1.90 A; A/B/C/D=21-266.
PDB; 1K6R; X-ray; 2.30 A; A/B=20-266.
PDB; 1K6S; X-ray; 2.03 A; A/B=20-266.
PDB; 2HP5; X-ray; 2.70 A; A/B/C/D=20-266.
PDB; 2HP6; X-ray; 2.20 A; A/B=20-266.
PDB; 2HP9; X-ray; 2.50 A; A/B=20-266.
PDB; 2HPB; X-ray; 2.05 A; A/B=20-266.
PDB; 2RL3; X-ray; 1.90 A; A/B=20-266.
PDB; 2WGI; X-ray; 2.85 A; A/B=21-266.
PDB; 2WGV; X-ray; 1.80 A; A/B=20-266.
PDB; 2WGW; X-ray; 1.80 A; A/B=20-266.
PDB; 2WKH; X-ray; 1.79 A; A/B=20-266.
PDB; 2WKI; X-ray; 2.10 A; A/B=20-266.
PDB; 2X01; X-ray; 1.90 A; A/B=20-266.
PDB; 2X02; X-ray; 1.35 A; A/B=20-266.
PDB; 3LCE; X-ray; 2.00 A; A/B/C/D=21-266.
PDB; 4S2O; X-ray; 1.70 A; A/B=20-265.
PDB; 4WZ5; X-ray; 1.60 A; A/B/C/D=20-266.
PDB; 5FQ9; X-ray; 1.50 A; A/B=20-266.
PDB; 5MMY; X-ray; 1.88 A; A/B=20-264.
PDB; 5MNU; X-ray; 1.56 A; A/B=20-265.
PDB; 5MOX; X-ray; 1.41 A; A/B=20-265.
PDB; 5MOZ; X-ray; 1.34 A; A/B=20-265.
PDBsum; 1E3U; -.
PDBsum; 1E4D; -.
PDBsum; 1EWZ; -.
PDBsum; 1FOF; -.
PDBsum; 1K4E; -.
PDBsum; 1K4F; -.
PDBsum; 1K54; -.
PDBsum; 1K55; -.
PDBsum; 1K56; -.
PDBsum; 1K57; -.
PDBsum; 1K6R; -.
PDBsum; 1K6S; -.
PDBsum; 2HP5; -.
PDBsum; 2HP6; -.
PDBsum; 2HP9; -.
PDBsum; 2HPB; -.
PDBsum; 2RL3; -.
PDBsum; 2WGI; -.
PDBsum; 2WGV; -.
PDBsum; 2WGW; -.
PDBsum; 2WKH; -.
PDBsum; 2WKI; -.
PDBsum; 2X01; -.
PDBsum; 2X02; -.
PDBsum; 3LCE; -.
PDBsum; 4S2O; -.
PDBsum; 4WZ5; -.
PDBsum; 5FQ9; -.
PDBsum; 5MMY; -.
PDBsum; 5MNU; -.
PDBsum; 5MOX; -.
PDBsum; 5MOZ; -.
ProteinModelPortal; P14489; -.
SMR; P14489; -.
BindingDB; P14489; -.
ChEMBL; CHEMBL5482; -.
DrugBank; DB02122; 4-iodo-acetamido phenylboronic acid.
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.
DrugBank; DB03801; Lysine Nz-Carboxylic Acid.
DrugBank; DB00760; Meropenem.
KEGG; ag:AAB60534; -.
KO; K18792; -.
BRENDA; 3.5.2.6; 5087.
EvolutionaryTrace; P14489; -.
PRO; PR:P14489; -.
GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-EC.
GO; GO:0008658; F:penicillin binding; IEA:InterPro.
GO; GO:0017001; P:antibiotic catabolic process; IEA:InterPro.
GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
InterPro; IPR012338; Beta-lactam/transpept-like.
InterPro; IPR002137; Beta-lactam_class-D_AS.
InterPro; IPR001460; PCN-bd_Tpept.
Pfam; PF00905; Transpeptidase; 1.
SUPFAM; SSF56601; SSF56601; 1.
PROSITE; PS00337; BETA_LACTAMASE_D; 1.
1: Evidence at protein level;
3D-structure; Antibiotic resistance; Disulfide bond; Hydrolase;
Plasmid; Signal; Transposable element.
SIGNAL 1 20
CHAIN 21 266 Beta-lactamase OXA-10.
/FTId=PRO_0000017030.
REGION 205 207 Substrate binding. {ECO:0000250}.
ACT_SITE 67 67 Acyl-ester intermediate.
MOD_RES 70 70 N6-carboxylysine.
{ECO:0000269|PubMed:11188693}.
DISULFID 44 51
STRAND 22 24 {ECO:0000244|PDB:2X02}.
HELIX 26 28 {ECO:0000244|PDB:2X02}.
HELIX 29 33 {ECO:0000244|PDB:2X02}.
TURN 34 36 {ECO:0000244|PDB:2X02}.
STRAND 39 47 {ECO:0000244|PDB:2X02}.
STRAND 50 54 {ECO:0000244|PDB:2X02}.
HELIX 56 59 {ECO:0000244|PDB:2X02}.
HELIX 66 69 {ECO:0000244|PDB:2X02}.
HELIX 70 79 {ECO:0000244|PDB:2X02}.
STRAND 81 83 {ECO:0000244|PDB:1E3U}.
HELIX 100 102 {ECO:0000244|PDB:2X02}.
HELIX 108 113 {ECO:0000244|PDB:2X02}.
HELIX 117 127 {ECO:0000244|PDB:2X02}.
HELIX 129 138 {ECO:0000244|PDB:2X02}.
TURN 150 152 {ECO:0000244|PDB:2X02}.
HELIX 153 156 {ECO:0000244|PDB:2X02}.
HELIX 163 174 {ECO:0000244|PDB:2X02}.
STRAND 178 180 {ECO:0000244|PDB:2X02}.
HELIX 182 191 {ECO:0000244|PDB:2X02}.
STRAND 193 196 {ECO:0000244|PDB:2X02}.
STRAND 198 208 {ECO:0000244|PDB:2X02}.
STRAND 214 216 {ECO:0000244|PDB:4WZ5}.
STRAND 218 228 {ECO:0000244|PDB:2X02}.
STRAND 231 242 {ECO:0000244|PDB:2X02}.
HELIX 244 248 {ECO:0000244|PDB:2X02}.
HELIX 249 260 {ECO:0000244|PDB:2X02}.
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


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