Reviewed, UniProtKB/Swiss-Prot O08498 (BLAB1_FLAME)

Names and origin

Protein names

Recommended name:
    Carbapenem-hydrolyzing beta-lactamase blaB-1
      Short name=CHbetaL-1
    EC=3.5.2.6
Alternative name(s):
    Class B carbapenemase blaB-1

Gene names

Name:	blaB1
Synonyms:	blaB

Organism

Flavobacterium meningosepticum (Chryseobacterium meningosepticum) (Elizabethkingia meningoseptica)

Taxonomic identifier

238 [NCBI]

Taxonomic lineage

Bacteria › Bacteroidetes › Flavobacteria › Flavobacteriales › Flavobacteriaceae › Elizabethkingia

Protein attributes

Sequence length	249 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Hydrolyzes penicillins, cephalosporins (including cefoxitin), carbapenems and 6-beta-iodopenicillanate.
Catalytic activity	A beta-lactam + H2O = a substituted beta-amino acid.
Cofactor	Binds 2 zinc ions per subunit By similarity.
Subunit structure	Monomer.
Sequence similarities	Belongs to the class-B beta-lactamase family.

Ontologies

Keywords
Biological process	Antibiotic resistance
Domain	Signal
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	antibiotic catabolic process Inferred from electronic annotation. Source: InterPro response to antibiotic Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	beta-lactamase activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 22

22

Ref.1

Chain

23 – 249

227

Carbapenem-hydrolyzing beta-lactamase blaB-1

PRO_0000016949

Sites

Metal binding

98

1

Zinc 1 By similarity

Metal binding

100

1

Zinc 1 By similarity

Metal binding

102

1

Zinc 2 By similarity

Metal binding

161

1

Zinc 1 By similarity

Metal binding

180

1

Zinc 2 By similarity

Metal binding

222

1

Zinc 2 By similarity

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

249

Helix Strand Turn

Details...

Beta strand

28 – 34

7

Beta strand

37 – 46

10

Beta strand

49 – 60

12

Beta strand

63 – 68

6

Helix

73 – 75

3

Helix

76 – 87

12

Beta strand

91 – 95

5

Beta strand

97 – 100

4

Turn

101 – 103

3

Helix

107 – 112

6

Beta strand

116 – 120

5

Helix

121 – 129

9

Beta strand

136 – 141

6

Beta strand

143 – 147

5

Beta strand

150 – 155

6

Beta strand

159 – 164

6

Beta strand

167 – 170

4

Turn

171 – 174

4

Beta strand

175 – 179

5

Helix

198 – 211

14

Turn

212 – 214

3

Beta strand

216 – 223

8

Helix

230 – 243

14

Sequences

	Sequence		Length	Mass (Da)
	O08498-1 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: 0F042B5126E338F6	FASTA	249	28,144
	10 20 30 40 50 60 MLKKIKISLI LALGLTSLQA FGQENPDVKI EKLKDNLYVY TTYNTFNGTK YAANAVYLVT 70 80 90 100 110 120 DKGVVVIDCP WGEDKFKSFT DEIYKKHGKK VIMNIATHSH DDRAGGLEYF GKIGAKTYST 130 140 150 160 170 180 KMTDSILAKE NKPRAQYTFD NNKSFKVGKS EFQVYYPGKG HTADNVVVWF PKEKVLVGGC 190 200 210 220 230 240 IIKSADSKDL GYIGEAYVND WTQSVHNIQQ KFSGAQYVVA GHDDWKDQRS IQHTLDLINE YQQKQKASN

References

[1]	"Characterization and sequence of the Chryseobacterium (Flavobacterium) meningosepticum carbapenemase: a new molecular class B beta-lactamase showing a broad substrate profile." Rossolini G.M., Franceschini N., Riccio M.L., Mercuri P.S., Perilli M., Galleni M., Frere J.-M., Amicosante G. Biochem. J. 332:145-152(1998) [PubMed: 9576862] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 23-27, CHARACTERIZATION. Strain: ATCC 13254 / CCUG 4310 / CIP 6058 / LMG 12280 / NCTC 10585.
[2]	"Molecular and biochemical heterogeneity of class B carbapenem-hydrolyzing beta-lactamases in Chryseobacterium meningosepticum." Bellais S., Aubert D., Naas T., Nordmann P. Antimicrob. Agents Chemother. 44:1878-1886(2000) [PubMed: 10858348] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: PINT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X96858 Genomic DNA. Translation: CAA65601.1.
AF189298 Genomic DNA. Translation: AAF89154.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1M2X	X-ray	1.50	A/B/C/D	27-249	[»]

ModBase

Search...

Enzyme and pathway databases

BioCyc

MetaCyc:MON-13428.

BRENDA

3.5.2.6. 39124.

Family and domain databases

InterPro

IPR001018. Beta-lactamase_class-B_CS.
IPR001279. Blactmase-like.
[Graphical view]

Pfam

PF00753. Lactamase_B. 1 hit.
[Graphical view]

PROSITE

PS00743. BETA_LACTAMASE_B_1. 1 hit.
PS00744. BETA_LACTAMASE_B_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

BLAB1_FLAME

Accession

Primary (citable) accession number: O08498

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 23, 2003
Last sequence update:	July 1, 1997
Last modified:	June 16, 2009
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)