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Protein

Beta-lactamase

Gene

ampC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

This protein is a serine beta-lactamase with a substrate specificity for cephalosporins.

Catalytic activityi

A beta-lactam + H2O = a substituted beta-amino acid.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei80Acyl-ester intermediatePROSITE-ProRule annotation1 Publication1
Active sitei166Proton acceptor1

GO - Molecular functioni

  • beta-lactamase activity Source: EcoliWiki

GO - Biological processi

Keywordsi

Molecular functionHydrolase
Biological processAntibiotic resistance

Enzyme and pathway databases

BioCyciEcoCyc:EG10040-MONOMER
MetaCyc:EG10040-MONOMER
BRENDAi3.5.2.6 2026
SABIO-RKiP00811

Protein family/group databases

MEROPSiS12.006

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-lactamase (EC:3.5.2.6)
Alternative name(s):
Cephalosporinase
Gene namesi
Name:ampC
Synonyms:ampA
Ordered Locus Names:b4150, JW4111
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10040 ampC

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Periplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi80S → D, E or G: Loss of activity. 1 Publication1
Mutagenesisi83K → Q or T: Lowers activity more than 1000-fold and increases protein stability. 1 Publication1
Mutagenesisi166Y → E: Lowers activity more than 1000-fold. 1 Publication1
Mutagenesisi168N → D or H: Lowers activity more than 1000-fold. 1 Publication1
Mutagenesisi331K → A: Lowers activity more than 1000-fold. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL2026
DrugBankiDB08551 (1R)-1-(2-THIENYLACETYLAMINO)-1-(3-CARBOXYPHENYL)METHYLBORONIC ACID
DB08552 (1R)-1-(2-thienylacetylamino)-1-phenylmethylboronic acid
DB07057 (3S)-1-(2-hydroxyphenyl)-5-oxopyrrolidine-3-carboxylic acid
DB07825 (3S)-1-(4-acetylphenyl)-5-oxopyrrolidine-3-carboxylic acid
DB07803 2-phenyl-1H-imidazole-4-carboxylic acid
DB02858 3-(4-Benzenesulfonyl-Thiophene-2-Sulfonylamino)-Phenylboronic Acid
DB08573 3-[(4-CHLOROANILINO)SULFONYL]THIOPHENE-2-CARBOXYLIC ACID
DB02797 3-Nitrophenylboronic Acid
DB08306 3-{[(3-NITROANILINE]SULFONYL}THIOPHENE-2-CARBOXYLIC ACID
DB07927 3-{[(4-CARBOXY-2-HYDROXYANILINE]SULFONYL}THIOPHENE-2-CARBOXYLIC ACID
DB02503 4-(Carboxyvin-2-Yl)Phenylboronic Acid
DB07541 4-(dihydroxyboranyl)-2-({[4-(phenylsulfonyl)thiophen-2-yl]sulfonyl}amino)benzoic acid
DB07114 4-[(METHYLSULFONYL)AMINO]BENZOIC ACID
DB03140 4-Carboxyphenylboronic Acid
DB04293 7-(2-Amino-2-Phenyl-Acetylamino)-3-Chloro-8-Oxo-1-Aza-Bicyclo[4.2.0]Oct-2-Ene-2-Carboxylic Acid
DB03530 Acylated Ceftazidime
DB09323 Benzathine benzylpenicillin
DB04360 Benzo[B]Thiophene-2-Boronic Acid
DB00456 Cefalotin
DB01147 Cloxacillin
DB02247 Hydrolyzed Cephalothin
DB01896 M-Aminophenylboronic Acid
DB02588 Moxalactam Derivative
DB02094 N-2-Thiophen-2-Yl-Acetamide Boronic Acid
DB08375 PCNOTAXIME GROUP
DB04035 Pinacol[[2-Amino-Alpha-(1-Carboxy-1-Methylethoxyimino)-4-Thiazoleacetyl]Amino]Methaneboronate
DB02772 Sucrose

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 191 PublicationAdd BLAST19
ChainiPRO_000001695820 – 377Beta-lactamaseAdd BLAST358

Proteomic databases

PaxDbiP00811
PRIDEiP00811

2D gel databases

SWISS-2DPAGEiP00811

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

BioGridi4261277, 168 interactors
IntActiP00811, 1 interactor
STRINGi316385.ECDH10B_4345

Chemistry databases

BindingDBiP00811

Structurei

Secondary structure

1377
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi22 – 39Combined sources18
Beta strandi42 – 50Combined sources9
Beta strandi53 – 63Combined sources11
Turni64 – 67Combined sources4
Beta strandi75 – 77Combined sources3
Helixi79 – 81Combined sources3
Helixi82 – 95Combined sources14
Helixi105 – 108Combined sources4
Helixi115 – 117Combined sources3
Helixi122 – 126Combined sources5
Helixi144 – 153Combined sources10
Beta strandi162 – 164Combined sources3
Helixi168 – 178Combined sources11
Turni179 – 183Combined sources5
Helixi186 – 193Combined sources8
Turni194 – 199Combined sources6
Beta strandi204 – 206Combined sources3
Helixi209 – 214Combined sources6
Beta strandi218 – 220Combined sources3
Beta strandi223 – 225Combined sources3
Turni229 – 231Combined sources3
Helixi233 – 236Combined sources4
Beta strandi240 – 242Combined sources3
Helixi243 – 254Combined sources12
Helixi256 – 258Combined sources3
Helixi262 – 271Combined sources10
Beta strandi273 – 278Combined sources6
Beta strandi281 – 283Combined sources3
Beta strandi288 – 293Combined sources6
Helixi296 – 301Combined sources6
Beta strandi303 – 305Combined sources3
Beta strandi306 – 308Combined sources3
Beta strandi310 – 313Combined sources4
Beta strandi315 – 321Combined sources7
Beta strandi325 – 335Combined sources11
Beta strandi338 – 345Combined sources8
Helixi346 – 348Combined sources3
Beta strandi350 – 358Combined sources9
Helixi362 – 376Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1C3BX-ray2.25A/B20-377[»]
1FCMX-ray2.46A/B20-377[»]
1FCNX-ray2.35A/B20-377[»]
1FCOX-ray2.20A/B20-377[»]
1FSWX-ray1.90A/B20-376[»]
1FSYX-ray1.75A/B20-376[»]
1GA9X-ray2.10A/B20-377[»]
1I5QX-ray1.83A/B20-377[»]
1IELX-ray2.00A/B20-377[»]
1IEMX-ray2.30A/B20-377[»]
1KDSX-ray2.15A/B20-377[»]
1KDWX-ray2.28A/B20-377[»]
1KE0X-ray2.30A/B20-377[»]
1KE3X-ray2.15A/B20-377[»]
1KE4X-ray1.72A/B20-377[»]
1KVLX-ray1.53A/B20-377[»]
1KVMX-ray2.06A/B20-377[»]
1L0DX-ray1.53A/B20-377[»]
1L0EX-ray1.90A/B20-377[»]
1L0FX-ray1.66A/B20-377[»]
1L0GX-ray1.50A/B20-377[»]
1L2SX-ray1.94A/B20-377[»]
1LL5X-ray1.80A/B20-377[»]
1LL9X-ray1.87A/B20-377[»]
1LLBX-ray1.72A/B20-377[»]
1MXOX-ray1.83A/B20-377[»]
1MY8X-ray1.72A/B20-377[»]
1O07X-ray1.71A/B20-377[»]
1PI4X-ray1.39A/B20-377[»]
1PI5X-ray1.49A/B20-377[»]
1XGIX-ray1.96A/B20-377[»]
1XGJX-ray1.97A/B20-377[»]
2BLSX-ray2.00A/B20-377[»]
2FFYX-ray1.07A/B20-377[»]
2HDQX-ray2.10A/B20-377[»]
2HDRX-ray2.20A/B20-377[»]
2HDSX-ray1.16A/B20-377[»]
2HDUX-ray1.49A/B20-377[»]
2I72X-ray2.20A/B20-377[»]
2P9VX-ray1.80A/B20-377[»]
2PU2X-ray1.86A/B20-377[»]
2PU4X-ray2.00A/B20-377[»]
2R9WX-ray1.80A/B20-377[»]
2R9XX-ray1.90A/B20-377[»]
2RCXX-ray2.00A/B20-377[»]
3BLSX-ray2.30A/B20-377[»]
3BM6X-ray2.10A/B20-377[»]
3FKVX-ray1.85A/B20-377[»]
3FKWX-ray1.50A/B20-377[»]
3GQZX-ray1.80A/B20-377[»]
3GR2X-ray1.80A/B20-377[»]
3GRJX-ray2.49A/B20-377[»]
3GSGX-ray2.10A/B20-377[»]
3GTCX-ray1.90A/B20-377[»]
3GV9X-ray1.80A/B20-377[»]
3GVBX-ray1.80A/B20-377[»]
3IWIX-ray1.64A/B20-377[»]
3IWOX-ray1.90A/B20-377[»]
3IWQX-ray1.84A/B20-377[»]
3IXBX-ray1.63A/B20-377[»]
3IXDX-ray2.64A/B20-377[»]
3IXGX-ray2.14A/B20-377[»]
3IXHX-ray2.30A/B20-377[»]
3O86X-ray1.60A/B20-377[»]
3O87X-ray1.78A/B20-377[»]
3O88X-ray1.64A/B20-377[»]
4E3IX-ray1.60A/B20-377[»]
4E3JX-ray1.80A/B20-377[»]
4E3KX-ray1.43A/B20-377[»]
4E3LX-ray1.43A/B20-377[»]
4E3MX-ray1.44A/B20-377[»]
4E3NX-ray1.49A/B20-377[»]
4E3OX-ray1.60A/B20-377[»]
4JXGX-ray1.65A/B20-377[»]
4JXSX-ray1.90A/B20-377[»]
4JXVX-ray1.76A/B20-377[»]
4JXWX-ray2.30A/B20-377[»]
4KENX-ray1.89B20-377[»]
4KG2X-ray1.89A/B20-377[»]
4KG5X-ray2.11A/B/C/D20-377[»]
4KG6X-ray1.75A/B/C/D20-377[»]
4KZ3X-ray1.67A/B20-377[»]
4KZ4X-ray1.42A/B20-377[»]
4KZ5X-ray1.35A/B20-377[»]
4KZ6X-ray1.68A/B20-377[»]
4KZ7X-ray1.43A/B20-377[»]
4KZ8X-ray2.28A/B20-377[»]
4KZ9X-ray1.72A/B20-377[»]
4KZAX-ray1.60A/B20-377[»]
4KZBX-ray1.37A/B20-377[»]
4LV0X-ray1.65A/B20-377[»]
4LV1X-ray1.74A/B20-377[»]
4LV2X-ray1.65A/B20-377[»]
4LV3X-ray1.42A/B20-377[»]
4OKPX-ray1.37A/B20-377[»]
4OLDX-ray1.48A/B20-377[»]
4OLGX-ray1.71A/B20-377[»]
5JOCX-ray1.75A/B21-377[»]
ProteinModelPortaliP00811
SMRiP00811
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00811

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni331 – 333Substrate bindingBy similarity3

Sequence similaritiesi

Belongs to the class-C beta-lactamase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG41066YJ Bacteria
COG1680 LUCA
HOGENOMiHOG000267102
InParanoidiP00811
KOiK01467
OMAiMTQGLGW
PhylomeDBiP00811

Family and domain databases

InterProiView protein in InterPro
IPR001466 Beta-lactam-related
IPR012338 Beta-lactam/transpept-like
IPR001586 Beta-lactam_class-C_AS
PfamiView protein in Pfam
PF00144 Beta-lactamase, 1 hit
SUPFAMiSSF56601 SSF56601, 1 hit
PROSITEiView protein in PROSITE
PS00336 BETA_LACTAMASE_C, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00811-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFKTTLCALL ITASCSTFAA PQQINDIVHR TITPLIEQQK IPGMAVAVIY
60 70 80 90 100
QGKPYYFTWG YADIAKKQPV TQQTLFELGS VSKTFTGVLG GDAIARGEIK
110 120 130 140 150
LSDPTTKYWP ELTAKQWNGI TLLHLATYTA GGLPLQVPDE VKSSSDLLRF
160 170 180 190 200
YQNWQPAWAP GTQRLYANSS IGLFGALAVK PSGLSFEQAM QTRVFQPLKL
210 220 230 240 250
NHTWINVPPA EEKNYAWGYR EGKAVHVSPG ALDAEAYGVK STIEDMARWV
260 270 280 290 300
QSNLKPLDIN EKTLQQGIQL AQSRYWQTGD MYQGLGWEML DWPVNPDSII
310 320 330 340 350
NGSDNKIALA ARPVKAITPP TPAVRASWVH KTGATGGFGS YVAFIPEKEL
360 370
GIVMLANKNY PNPARVDAAW QILNALQ
Length:377
Mass (Da):41,556
Last modified:July 21, 1986 - v1
Checksum:i3C6FB4FE4EF96C9F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01611 Genomic DNA Translation: AAA23441.1
U14003 Genomic DNA Translation: AAA97049.1
U00096 Genomic DNA Translation: AAC77110.1
AP009048 Genomic DNA Translation: BAE78154.1
V00277 Genomic DNA Translation: CAA23537.1
PIRiA01007 QKEC
RefSeqiNP_418574.1, NC_000913.3
WP_001336292.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC77110; AAC77110; b4150
BAE78154; BAE78154; BAE78154
GeneIDi948669
KEGGiecj:JW4111
eco:b4150
PATRICifig|1411691.4.peg.2548

Similar proteinsi

Entry informationi

Entry nameiAMPC_ECOLI
AccessioniPrimary (citable) accession number: P00811
Secondary accession number(s): Q2M6F2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: March 28, 2018
This is version 166 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome
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Main funding by: National Institutes of Health